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Exam 3 Flashcards

1
Q

Microfilaments (actins)

A

• support/organize plasma membrane
• Cell shape and division and motility

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2
Q

Microtubules (tubulins)

A

• organize cytoplasm
• Intracellular transport
• Cell division
• Cilia/flagellae motility

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3
Q

Intermediate filaments (IF proteins)

A

• strengthen cytoplasm/tissues
• Support nucleus
• Epidermal appendages (hair/nails)

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4
Q

Actin

A

• medium sized globular proteins (45kDa)
• Six actin gene, including muscle (alpha-actin) and non-muscle (beta and gamma-actin) subtypes

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5
Q

Tubulin

A

• medium sized globular protein (55kDa)
• Two dozen tubulin genes, alpha, beta, and gamma subunits
• expressed in all cells especially neurons
• binds and hydrolyzes GTP—>GDP
• interacts with motor proteins 

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6
Q

Basic building subunits of microtubules

A

Heterodimers of Alpha-beta tubulin

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7
Q

Intermediate filament proteins

A

• 50-200kDa
• 70 gene products categorized into six sub-families
• present in tissue specific manner

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8
Q

Monomers of intermediate filament proteins

A

Long, linear molecules that assemble during polymerization like threads forming a rope

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9
Q

Tubulin polymers

A

Tubules formed from Proto filaments that display chemically different ends (polar) 

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10
Q

Types of actins

A

Muscle— skeletal, cardiac, smooth

Cytoplasmic —beta and gamma cytoplasmic

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11
Q

Types of tubulins

A

• alpha tubulin, 8 genes
• Beta tubulin, 10 genes
• Gamma tubulin, 2 genes

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12
Q

IF proteins subfamilies

A
  1. Acidic keratins
  2. Neutral/basic keratins
  3. Vimentin, desmin, GFAP
  4. Neurofilament IF proteins
  5. Lamins
  6. Lens-specific beaded IFs
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13
Q

polarized polymers are formed by:

A

Actin and tubulin

  • subunits are easily added to the plus end, and removed from the minus end 
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14
Q

Actin and tubulin as nucleotide-binding proteins

A

ATP/GTP and ADP/GDP respectively

ATP and GTP binding stabilize the polymers, and ADP and GDP destabilize the polymers

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15
Q

Dynamic instability

A

The rapid cycling between microtubule polymerization and depolymerization that occurs continuously in cells 

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16
Q

Actin polymerization is initiated by:

A

1.) Formin (parallel bundles)

2.) Arp complexes (branching networks)

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17
Q

Tubulin polymerization is nucleated by:

A

1.) Ring complexes containing gamma tubulin (TURCs)

2.) Alpha and beta tubulin bind to form a heterodimer

3.) Alpha subunit bind to TURC’s beginning the formation of a microtubule (at - end)

4.) TURCs in centrosome

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18
Q

Major phosphorylation sites in an intermediate filament protein (lamin)

A

PSer-22

PSer-392

PSer-628

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19
Q

IF proteins regulated by:

A

Phosphorylation —> Depolymerization

Dephosphorylation —> Polymerization

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20
Q

Taxol (paclitaxel)

A

A clinically useful drug that works by stabilizing microtubules, thereby interfering with mitotic spindle function in dividing cells. Used to treat some types of cancers

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21
Q

Where is actin cytoskeleton?

A

Localized near plasma membrane, including forming specialized arrays at cell—cell and cell—ECM junctions

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22
Q

Functions of microfilaments

A

• support an organization
• cell—cell adhesions at adheren junctions 
• cell—ECM adhesion at focal contacts
• regulate gene expression

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23
Q

Actin and myosin interaction

A

Muscle of the cell

• Controls cell shape
• Drives cytokinesis during cell division
• Drives cell motility

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24
Q

Proteins that link microfilaments to the plasma membrane

A

1.) talin

2.) catenins

3.) dystrophin

4.) ERM proteins

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25
Q

Myosin

A

Motor proteins associated with Actin cytoskeleton

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26
Q

Type II myosin

A

Conventional, they can form bipolar filaments through ability of their long tails to wrap around each other and an anti-parallel orientation

This allows them to pull microfilaments past each other (contraction)

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27
Q

Other types “ unconventional” myosin

A

Act as monomers or dimers. Do not form bipolar fibers, but bind to different types of cargoes in the cytoplasm

Participate in vesicular trafficking, and interact with Rab small GTPases

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28
Q

Steps of myosin activation

A

1.) ATP hydrolysis, conformational changes

2.) binding of ATP releases a myosin head from a microfilament

3.) Hydrolysis to ADP plus Pi “cocks” the head, which reattaches to microfilament

4.) Pi released, confirmational change that pulls the microfilament—tightly bound 

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29
Q

Myosin in the absence of ATP

A

Heads cannot be displaced from tightly binding actin, resulting in rigor mortis 

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30
Q

 Rho family of G-proteins

A

Promotes stress fiber formation (parallel) 

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31
Q

Rac family of G-Proteins

A

Promotes lamellipodia formation (peripheral MF network stabilized with filamin)

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32
Q

Cdc42

A

Promotes filopodia formation (parallel microfilament bundles stabilized with cross-linking proteins that support fingerlike cell extensions)

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33
Q

Focal adhesion

A

Contains integrins, microfilaments, linking proteins, focal adhesion kinases

Play Central roles in adhesion and cell motility. Communicate status of attachment to ECM

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34
Q

Microvilli

A

• Increase the absorptive area of the plasma membrane
• are supported by a core bundle of actin microfilaments, but are non-motile
• Prominent in intestinal epithelial

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35
Q

Adherens junctions

A

1.) Cadherins: IMPs that adhere to each other in the presence of Ca2+

2.) linking (anchor) proteins: alpha and beta-catenins.  Can travel into the nucleus, and function as transcriptional regulators

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36
Q

Sub-plasma membrane-associated microfilaments

A

• physically support the plasma membrane

• Interact with IMP’s and linking proteins

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37
Q

Actin and muscular dystrophy

A

Distroglycan complex: IMPs

Dystrophin: linking protein

ECM: laminin and collagen

^^ Mutations in these proteins (esp. dystrophin) weakens the muscle cell membrane leading to cell death

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38
Q

Centrosome 

A
  • the microtubule organizing center (MTOC)
    - Nucleates and organizes microtubules
  • Located near nucleus and Golgi apparatus

• composed of a pair of centrioles

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39
Q

Pericentriolar materials (PCM)

A

Amorphous material surrounding centrioles. Contains TURC‘s which nucleate microtubule polymerization

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40
Q

Three forms of centrosomes

A

1.) MTOCs

2.) Basal Bodies

3.) Spindle Poles

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41
Q

Centrosome: Basal bodies

A

Specialized centrioles that arise through repeated duplication of centrosome centrioles

Migrate to apical (top) region of a cell and nucleate microtubules extension that form cilia and flagellae

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42
Q

Centrosome: spindle poles

A

Duplicated centrosomes that nucleate the spindle apparatus in dividing cells

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43
Q

Primary Cilium

A

One per cell, non-motile, 9+0 axoneme, Sensory and signaling functions, formed when cells stop dividing, important in early development

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44
Q

Polycystic kidney disease and obesity causes:

A

Deficits associated with primary cilium

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45
Q

Microtubule structural proteins

A

• MAP1,2,4
• Tau
• Plectin

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46
Q

Microtubule motor proteins

A

• Dyneins

• Kinesins 

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47
Q

Alzheimer’s disease and TAU

A

TAU hyper phosphorylation is linked to its condensation into neurofibrillary tangles— Aggregates are toxic to brain cells

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48
Q

Dyneins

A

Move cargo towards the (-) end of MTs

Drives ciliary and flagellar motility

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49
Q

Kinesins

A

Move cargo toward the (+) end of MTs

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50
Q

Kartagener’s Syndrome (ciliary dyskinesia)

A

Cilia and flagellae are immotile due to mutations in dynein 

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51
Q

Blistering diseases originate due to:

A

1.) Auto antibodies produced against normal desmosomal and hemidesmosomal proteins

2.) mutations in IF proteins or other hemi/desmosomes

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52
Q

Pemphigus (bullous pemphigus)

A

Affects outer layers of skin, auto antibodies to Desmosomal desmogleins 

Blisters are easily ruptured

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53
Q

Pemphigoid (bullous pemphigus)

A

Effects lower layers of skin (junction of epi-dermis and dermis)

Autoantibodies produced against: ColXVII, BPAG2/BP180, and dystonin (BPAG1/BP230)

Stiff blisters that do not break open easily

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54
Q

Epidermolysis bullosa Simplex

A

EBS — caused from loss of function mutations in keratin

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55
Q

Nuclear lamina functions

A

• Physical support for the nuclear envelope
• interconnects nucleus with cytoskeleton and ECM
• organize chromatin
• cell differentiation
• cell cycle and apoptosis
• gene expression

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56
Q

Progeria

A

Disease of accelerated aging Caused by perturbations in lamin farensylation 

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57
Q

Penicillin and penicillin related compounds

A

Contain thiazolidine ring, beta-lactam ring, And a variable side chain that dictates it’s microbicidal activity

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58
Q

How penicillin works:

A

Beta lactam ring Affects penicillin binding proteins by blocking transpeptidation

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59
Q

Naturally derived penicillins

A

Penicillin G

penicillin V

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60
Q

Penicillinase-sensitive penicillins

A

Amoxicillin, ampicillin

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61
Q

Penicillinase-resistant penicillins

A

Dicloxacillin, nafcillin, oxacillin

Do NOT need to pair with beta lactamase inhibitors

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62
Q

Antipseudomonal penicillins

A

Piperacillin, Ticarcillin

High resistance to drugs

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63
Q

Beta lactamase inhibitors

A
  1. Clavulnic acid
  2. Sublactam
  3. Tazobactam

They bind to and inactivate the beta lactamases to protect the penicillin drugs

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64
Q

Cephalosporin drugs

A

Contain beta-lactam ring, broad-spectrum and resistant to Penicillinases, Commonly given via IV, fewer allergic reactions

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65
Q

First generation cephalosporin drugs

A

• Good against gram positive cocci and a few Gram negative

  1. cefazolin
  2. Cephalexin
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66
Q

Second generation cephalosporin drugs

A

More broad spectrum than first generation, can target more Gram negative bacteria

  1. Cefaclor
  2. Cefoxitin
  3. Cefuroxime
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67
Q

Third generation cephalosporin drugs

A

Broad spectrum with especially well developed activity against enteric bacteria that produce beta lactamases

  1. Cefotaxime
  2. Ceftadime
  3.  Ceftriaxone— Crosses BBB
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68
Q

Fourth generation cephalosporin drugs

A

Broad-spectrum for both gram-positive and gram-negative with increased activity against pseudomonas and gram-positive organisms

  1. Cefapime
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69
Q

Fifth generation cephalosporin drugs

A

Broad gram positive and gram-negative coverage including MRSA but not pseudomonas

  1. Ceftaroline
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70
Q

Carbapenems

A

Have beta lactam ring, used in the hospital setting when other antibiotics aren’t working (side effects: G.I. distress, skin rash, CNS toxicity)

  1. Doripenem
  2. Ertapenem
  3. Imipenem
  4. Meropenem 
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71
Q

 Cilastatin + imipenem why?

A

To block renal hydropeptidase in order to decrease the inactivation of the drug in the renal tubules

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72
Q

Non-beta-lactam cell wall targeting drugs

A

Bacitracin (streptococci/staphylococci), isoniazid (Mycobacterium TB), Vancomycin (Staphylococcal infection), fosfomycin (phosphoric acid agent)

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73
Q

Bacitracin

A

Narrow spectrum antibiotic produced by a strain of the bacterium bacillus subtilis

Combats superficial skin infection by streptococci and staphylococci

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74
Q

isoniazid

A

Bacteriocidal to mycobacterium TB, But only against growing cells

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75
Q

Vancomycin

A

Narrow spectrum antibiotic most effective in treating staphylococcal infections in case of penicillin resistance or allergy

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76
Q

Fosfomycin

A

Phosphoric acid agent effective as alternate treatment for urinary tract infections caused by enteric bacteria

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77
Q

Oxazolidinones (Linezolid)

A

• 50S subunit inhibitor

• Bacteriocidal/bacteriostatic

• Inhibits protein synthesis by binding to the 50S subunit, preventing the formation of initiation complex

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78
Q

Oxazolidinones are used against:

A

Gram-positive bacteria including MRSA and VRE (Vancomycin resistant enterococci) 

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79
Q

Side effects of Oxazolidinones 

A

Bone marrow suppression (thrombocytopenia), peripheral neuropathy, and serotonin syndrome

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80
Q

Resistance to Oxazolidinones

A

Resistance via a point mutation in the ribosomal RNA

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81
Q

Aminoglycoside drugs

A

• 30 S subunit inhibitors

• Bacteriocidal

• Irreversible inhibition of the initiation complex through binding of the 30S subunit. Can cause misreading of the mRNA

• Requires oxygen for optic. Drugs ineffective against anaerobes


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82
Q

Types of aminoglycoside drugs

A
  1. Amikacin
  2. Gentamicin
  3. Neomycin
  4. Streptomycin
  5. Tobramycin
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83
Q

Side effects of the aminoglycoside drugs

A

Nephrotoxicity, neuromuscular blockade, ototoxicity, teratogen (pregnant women) 

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84
Q

Resistance of aminoglycoside drugs

A

Resistance via bacterial transferase enzymes that inactivate the drug by acetylation, phosphorylation, or adenylation 

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85
Q

Aminoglycoside drugs used against

A

• severe gram-negative rod infections

• Synergistic with beta lactamases

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86
Q

Tetracycline drugs

A

• 30 S Subunit inhibitors

• bacteriostatic

• binds to the 30 S subunit and prevents the attachment of aminoacyl tRNA in the A site

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87
Q

Types of tetracycline drugs

A
  1. Doxycycline
  2. Minocycline
  3. Tetracycline
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88
Q

Side effects of tetracycline drugs 

A

G.I. distress, discoloration of teeth and inhibition of bone growth in children, photo sensitivity, NOT used during pregnancy

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89
Q

Resistance of tetracycline drugs

A

Resistance via decreased uptake or increased efflux out of the bacterial cells by plasmid-encoded transport pumps

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90
Q

Macrolide drugs 

A

• 50S subunit inhibitors
• bacteriostatic
• inhibit protein synthesis by blocking translocation, bind to the 23S rRNA of the 50S ribosomal unit : bind to E site

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91
Q

Tetracycline drugs used against

A

Borrelia burgdorferi, mycoplasma pneumoniae, Rickettsia, and chlamydia

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92
Q

Macrolide drugs used against

A

Atypical pneumonia’s, sexually transmitted infections, gram-positive cocci, and Bordetella pertussis 

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93
Q

Side effects of macrolides 

A

G.I. motility issues, arrhythmia caused by prolonged QT interval, acute cholestatic hepatitis, rash, eosinophilia, theophylline serum increase, Inhibition of cytochrome P450

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94
Q

Types of macrolides

A
  1. Azithromycin
  2. Clarithromycin
  3. Erythromycin
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95
Q

Chloramphenicol

A

• 50 S subunit inhibitor

• Blocks P site, blocks peptidyl transferase

• Bacteriostatic

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96
Q

Chloraphenicol used against:

A

Meningitis, and rocky mountain spotted fever

Has limited use due to toxicities, continued use in developing countries because of low cost

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97
Q

Chloraphenicol side effects

A

Anemia, aplastic anemia, grey baby syndrome

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98
Q

Chloramphenicol resistance

A

Resistance via plasmid-encoded acetyltransferase that inactivates the drug

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99
Q

Clindamycin

A

• 50 S subunit inhibitor

• Bacteriostatic

• Blocks peptide transfer and translocation at the 50 S ribosomal unit

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100
Q

Clindamycin used against: 

A

Anaerobic infections, aspiration pneumonia, lung abscesses, and oral infections

Group A strep infections

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101
Q

Clindamycin side effects

A

C. Diff, Fever, diarrhea

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102
Q

Clindamycin VS metronidazole

A

Clindamycin treats infections above the diaphragm, well metronidazole treats anaerobic infections below the diaphragm

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103
Q

Dalfopristin/quinupristin

A

Mechanism:

Combined action is bactericidal for some organisms. Binds 50 S to inhibit translocation

Spectrum:

Reserved for infections caused by multiple drug resistant gram-positive bacteria. Not a first line of treatment

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104
Q

Resistance of  Dalfopristin/quinupristin

A

• Ribosomal methylation prevents binding of drug to its target.

• Enzymes inactivate the drugs.

• Efflux proteins that pump them out of the cell.

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105
Q

Macrolides/ clindamycin relation to dalfopristin/quinupristin

A

Cross resistance. Resistance to one of these drugs is equal to resistance to all of these drugs

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106
Q

Side effects of  Dalfopristin/quinupristin

A

High incidence of althralgias, Inhibits CYP3A4 and is likely to have significant drug interactions

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107
Q

Drugs you not use with newborns

A

Chloramphenicol

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108
Q

Drugs you do not use in children

A

Tetracyclines

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109
Q

Drugs you do not use during pregnancy

A

Tetracycline, aminoglycosides, clarithromycin, chloramphenicol, etc.

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110
Q

Adjust drug based off of elderly renal function

A

Beta lactams, aminoglycosides

Half-life of these drugs will be increased, retention of drugs increases

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111
Q

Seizures caused by:

A

Beta lactams, mostly carbapenems

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112
Q

Hepatotoxicity Caused by:

A

Rifampin

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113
Q

Nephrotoxicity via:

A

Impenems, Aminoglycosides, vancomycin

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114
Q

 Ototoxicity caused by:

A

Aminoglycosides, vancomycin

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115
Q

Anemia caused by:

A

Chloraphenicol

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116
Q

Arthralgia caused by:

A

Dalfopristin/quinupristin

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117
Q

Superinfection caused by:

A

Clindamycin, third generation cephalosporin, ampicillin

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118
Q

Causes disulfiram reaction when taken with alcohol:

A

Second generation cephalosporin with methylthiotetrazole groups

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119
Q

Aminoglycoside + penicillin synergy

A

Penicillin increases permeability of cell membranes increasing the ability of amino glycosides to enter the cell

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120
Q

Vancomycin + aminoglycoside combination drug

A

Each alone have some nephrotoxicity. If given together you get marked renal impairment

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121
Q

Penicillin + tetracycline

A

79% mortality for pneumococcal meningitis

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122
Q

Folic acid synthesis and reduction inhibitors

A
  1. Sulfadiazine
  2. Sulfamethoxazole
  3. Sulfisoxazole
  4. Trimethoprim

Cause sensitivities in bacteria that need to synthesize their own dihydrofolic acid

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123
Q

Sulfonamides

A

• bacterial static

• Competitive inhibitors if dihydropternoate synthase resulting in a disruption of folic acid synthesis

• Inhibits bacterial growth by decreasing nucleotides

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124
Q

Sulfonamide resistance

A

Comes from altered enzyme, decreased uptake, or increased PABA synthesis

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125
Q

Sulfonamide side effects:

A

Nausea, vomiting, diarrhea, rash, fever, headache, depression, jaundice, hepatic necrosis, drug induced lupus, and serum sickness-like syndrome

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126
Q

Sulfonamides and G6PD

A

Sulfonamides can cause a deficiency in G6PD, leading to acute hemolytic anemia

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127
Q

Sulfonamide competition with bilirubin

A

Competitive inhibitor for bilirubin binding sites on plasma albumin, may increase fetal blood levels of unconjugated bilirubin —kernicterus 

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128
Q

Sulfonamides and warfarin

A

Sulfonamides displays albumin binding sites for warfarin, increasing the effective activity of the displaced drug

Anticoagulant dosage should be reduced during sulfonamide therapy

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129
Q

Major uses for sulfonamides:

A

• CNS and ocular toxoplasmosis

• Infection by nocardia bacteria

• Malaria

• UTIs

• Otitis media

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130
Q

Trimethoprim

A

• bacteriostatic

• Inhibits bacterial dihydrofolic reductase (downstream)

• inhibits purine and DNA synthesis

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131
Q

Major uses for trimethoprim

A

Primary use is for the prevention of recurrent, uncomplicated urinary tract infections

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132
Q

TMP + SMX

A

Trimethoprim + sulfamethoxazole 

Bacteriocidal = static + static

• High degree of synergistic activity by inhibiting same pathway

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133
Q

Types of Quinolones

A
  1. Ciprofloxacin
  2. Enoxacin
  3. Gemifloxacin
  4. Levofloxacin
  5. Moxifloxacin
  6. Nalidixic acid
  7. Norfloxacin
  8. Ofloxacin 
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134
Q

Quinolone drugs

A

• Bacteriocidal

• Inhibit the enzymatic activity of topoisomerase class enzymes: DNA gyrase and topoisomerase IV

• Promote the cleavage of DNA in these enzyme DNA complexes

• Cannot be taken with antiacids

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135
Q

Quinolones are used against:

A

Aerobic gram-negative bacilli, Particularly members of the family enterobacteriaceae 

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136
Q

What drug is strong enough to use against pseudomonas (P. Aeruginosa)?

A

Levofloxacin 

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137
Q

Side effects of quinolones

A

G.I. side effects, confusion, CDF, yeast infection, cartilage damage, arthropathy

tendinitis in those older than 60 also taking prednisone

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138
Q

Metronidazole

A

• Bacteriocidal

• Inert, activity is determined by the capacity of susceptible organisms to activate the drugs once it enters the cell via passive diffusion

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139
Q

Metronidazole used against:

A

Anaerobic infections, bacterial septicemia, CNS infections, bacterial vaginosis, acne rosacea

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140
Q

Disulfuram reaction with alcohol + metronidazole 

A

Disulfiram ethanol reaction due to increased serum acetyl-aldehyde

Metronidazole blocks aldehyde dehydrogenase, inhibiting the oxidation of acetylaldehyde

^^^ hangover feeling results

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141
Q

Rifampin

A

• Bacteriocidal

• Find bacterial RNA polymerase at the active Center, blocking the elongation of mRNA

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142
Q

Rifampin used against:

A

Active TB, asymptomatic carriers of Neisseria meningitidis 

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143
Q

Side effects of rifampin

A

Induction of cytochrome P450, leading to organ rejection, loss of seizure control, and risk of pregnancy if on birth control

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144
Q

Mitochondria DNA is hypermutable

A

• not bound to histones in a chromatin structure

• Exposed to higher concentrations of ROS

• Balanced by copy number genes, heteroplasmy

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145
Q

MtDNA copy number can be affected by:

A

Metabolic state, hormones, and drugs

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146
Q

TCA cycle functions:

A

• oxidized two carbons from acetate to CO2

• Make NADH, FAD2H, and GTP

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147
Q

PDH and the TCA cycle occur in:

A

The mitochondria

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148
Q

Glycolysis occurs in:

A

Cytosol

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149
Q

Inherited point mutations in MPC1 can cause:

A

Lactic acidosis and hyper pyruvatemia (pyruvate—> lactate dehydrogenase)

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150
Q

Four subunits of PDH

A

E1: pyruvate decarboxylase, TPP

E2: Transacetylase, Lipoate and CoA

E3: dihydrolipoyl dehydrogenase, FAD,
NAH+
X:

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151
Q

PDH Kinases 

A

Inhibits: pyruvate, ADP

Activates: Hypoxia, acetyl-CoA, and ADH, ATP

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152
Q

PDH phosphatase

A

Activated by calcium

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153
Q

PDH regulation

A

Phosphorylation and dephosphorylation of serine residues on E1 alpha subunits

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154
Q

Key regulator of the TCA cycle

A

Isocitrate dehydrogenase is the key rate limiting enzyme in the TCA cycle

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155
Q

Positive deltaG reactions in the TCA cycle

A

 citrate—aconitase—> isocitrate

Malate—malate dehydrogenase—> oxaloacetate 

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156
Q

Build up of citrate leads to what other metabolism?

A

Fatty acid, cholesterol synthesis

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157
Q

Buildup of Malate leads to what other metabolism?

A

Gluconeogenesis

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158
Q

Citrate synthase

A

Hydrolyzes the thiolester bond of acetyl Coa to join acetate and oxaloacetate forming citrate

Tricarboxylic acid

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159
Q

Aconitase 

A

Catalyze is a two step isomerization to convert citrate to isocitrate producing Intermediate aconitate 

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160
Q

Isocitrate dehydrogenase (IDH3)

A

Catalyzes oxidative decarboxylation for TCA cycle, producing CO2.

IDH1 in the cytosol and IDH2 in the mitochondria catalyze the same reaction but use NADP+/NADPH

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161
Q

Alpha ketoglutarate dehydrogenase

A

Catalyzes the final oxidative decarboxylation. At this point to carbons are released as carbon dioxide

162
Q

Succinate thiokinase 

A

Cleaves the thioester bond linking succinate and CoA— exergonic.

Uses cleaving energy to phosphorylate GDP to GTP

163
Q

Succinate dehydrogenase

A

Oxidizes succinate to introduce double carbon, reducing FAD in the process

Is part of complex II of the electron transport chain, transferring e- from FAD2H to coenzyme Q

164
Q

Mesenchyme

A

A part of the mesoderm of an embryo which develops into connective tissue/cartilage/bone/Lymphatic vessels, blood vessels

Appears at every stage of animal life

165
Q

Mesoderm

A

One of the three germ layers in the embryo of a Metazoan animal.  located between ectoderm and endoderm.

Gives rise to connective tissue, bone, cartilage, muscle, blood, blood vessels, lymphoid organs, pericardium, notochord, Kidney, gonads

166
Q

Components of connective tissue proper

A

Extra cellular matrix
- Fibers
- Ground substance

Cells

167
Q

What are ECM fibers?

A

Collagen, elastic fibers, reticular fibers

168
Q

What is ECM ground substance?

A

Glycosaminoglycans (GAGs), proteoglycans, glycoproteins, integrins 

169
Q

Physical characteristics of collagenous fibers

A

• 1-20 nm in diameter
• comprised of smaller fibrils
• Irregular, undulating shape
• Inelastic
• Forms gelatin in boiling water
• Leather industry: tanning process
• Stains with acid dyes (pink in H&E)


170
Q

Most common amino acids in collagen

A

Lysine, proline, hydroxyproline, hydroxylysine

171
Q

Collagen synthesis

A
  1. Alpha chains (in golgi and ER)
  2. Procollagen (In secretory vesicle)
  3. Tropocollagen macromolecule (outside of cell)— assembles into fibrils
172
Q

Type I collagen

A

Ordinary connective tissue (loose and dense) and bone

173
Q

Type II collagen

A

hyaline collagen

174
Q

Type III collagen

A

Loose connective tissue, blood vessel wall, skin, liver, long, support for lymphoid tissue

175
Q

Type IV collagen

A

Basement membranes, network forming

176
Q

Type V collagen

A

Widespread

177
Q

Type VII collagen

A

Anchoring filaments attach basal lamina to underlying connective tissue

178
Q

Where do collagen fibers originate from?

A

Fibroblasts

179
Q

Elastic fibers

A
  • thinner than collagen
  • May reach 10 to 12 mm in length in elastic ligaments
  • branch freely
  • Highly refract tile, yellowish
  • May be in arterial walls (fenestrated)
180
Q

Elastic fibers staining

A

Orcein, resorcin-fuchsin, aldehyde-fuchsin

— relaxed elastic fibers have a wavy appearance in H&E sections

181
Q

Chemical composition of elastic fibers

A
  1. Elastin: Amorphous component
    — High proline, glycine, valine
    — Desmosine and isodesomosine amino acid cross-links
    
  2. Fibrillin: microfibrillar component
    — Cysteine
    — marfan’s syndrome & aged skin
182
Q

Origin of elastic fibers

A

Fibroblasts, smooth muscle cells

183
Q

Reticular fibers (type III collagen)

A
  • small (0.03-0.04mm)
  • Stained by silver or PAS stains
  •  more carbohydrate dense
  • Located in muscle cells, nerves, epithelial structures, glandular organs, lymphatic tissues, red bone marrow, skin, liver, lungs 
184
Q

Origin of reticular fibers

A

Fibroblasts, reticular cells

185
Q

Amorphous intracellular substance (Ground substance) 

A

• viscous solution <—> Thin gel

• Homogeneous and transparent

• significant amount of bound water, GAGs, proteoglycans and proteoglycans aggregates

186
Q

Glycoproteins definition

A

Mostly protein and are glycosylated with monosaccharides or disaccharides in the ER and Golgi

• Secreted or integrated into the membrane
• Laminin in fibronectin are secreted from cells into the ECM


187
Q

Glycosaminoglycan (GAGs) definition

A

Polysaccharides produced by processing enzymes in the Golgi and outside the cell

• Often sulfated to produce a negative charge

188
Q

Proteoglycans definition

A

Heavily glycosylated proteins and are primarily composed of polysaccharide/carbohydrate

• Aggregates of a core protein produced in the ER and glycosylated with GAG’s in the Golgi

• Polysaccharide component of proteoglycans and GAGs attract water, and act well as lubricant or shock absorbers

189
Q

Hyaluronic acid (Non-sulfonated GAG)

A

• very viscous insulation

• High molecular weight

• Alternating glucosamine and glycouranate units

• accounts for many of the physical characteristics of ground substance (Barrier to bacteria and present in synovial joints)


190
Q

Fibronectin

A

• glycoprotein

• Soluble (hepatocytes): in blood plasma

• insoluble (fibroblasts): in ECM

• Organize cellular matrix, barn to different macromolecular species

191
Q

Laminin

A

• confined to basement membrane (lamina densa)

• Structural and adhesive functions

192
Q

Origin of laminin

A

Epithelial and smooth muscle cells

193
Q

Connective tissue cells

A

1.) fibroblast
2.) Mesenchymal cells and pericyte 
3.) fat cell

Visitors from the blood: Macrophage, plasma cell, mast cell, lymphocytes, Eosinophil, neutrophil

194
Q

Fibroblasts

A

Most common CT cell

Large, oval nuclei, distinct nucleolus, basophilic cytoplasm, abundant RER and ribosomes, enlarged Golgi, numerous cytoplasmic vesicles with fine threads


195
Q

Function of fibroblasts

A

Production of connective tissue fibers, production of amorphous intracellular substance (ground substance) 

196
Q

Scurvy

A

• generalized degeneration of connective tissue
• Deficiency in vitamin C
• Necessary for conversion of proline to hydroxyproline
• Cannot form hydrogen bonds to join alpha chains

197
Q

Ehler’s Danlos syndrome

A

• short stature, stretchable skin, hyper mobility
• Cannot Cleve N-terminus of procollagen to create tropocollagen
• Mutations in collagen or processing in the face

198
Q

Osteogenesis imperfecta: brittle bone disease

A

Abnormal production of collagen I

199
Q

Mesenchymal cells

A

•Relatively primitive, undifferentiated cells
• along blood vessels, especially capillaries
• Functions: Precursor of fibroblasts, Fat cells, mast cells, smooth muscle cells, Endothelial cells

200
Q

Fat cells

A

• Occur singly or in small groups in loose CT
• large masses in adipose tissue
• Undifferentiated mesenchymal cells

201
Q

Macrophages

A

Monocyte: in blood
Macrophage: in tissue

Capable of ameboid movement— Moves to site of inflammation


202
Q

Plasma cells

A

• produce antibodies
• Not comment except for in connective tissue of the digestive tract, greater omentum, reticular connective tissue of blood forming organs
• Numbers increase in areas of chronic inflammation

• Derived from activated B lymphocytes

203
Q

Mast cell

A

• present in most loose connective tissues
• Originate from hematopoietic stem cells (Bone marrow)

204
Q

Mast cells contain granules of:

A
  1. Heparin
  2. Histamine

Function: degranulate to mediate information in allergies and anaphylaxis

205
Q

Loose areolar CT

A

• Arranged irregularly, appears cobwebby, understained spaces due to ground substances

• made of fibroblasts, macrophages, fibers (Mostly collagen), amphorous ground substance

206
Q

Dense, irregular CT

A

• constituent fibers irregularly arranged
• Made of fibers (Coarse collagenous fibers), cells (Fibroblasts and macrophages), ground substance

207
Q

Dense regular CT

A

• Two forms: collagenous and elastic
• lined up in parallel, well suited for withstanding tension in one direction
•  fibroblast is the major cell between the fibers
• Poor blood supply = injury slow to heal

208
Q

Adipose tissue

A

• many fat cells, arranged in groups or lobules.
• Cells surrounded by external lamina and fine collagenous, reticular, and elastic fibers
• Very little amphorous ground substance



209
Q

Reticular connective tissue

A

— Provides a fine fibrillar Network in lymphoid tissues (spleen, lymph node, bone marrow)

— Made of reticular cells and reticular fibers

210
Q

Fumarate hydrotase

A

Add a proton and hydroxyl from water to fumarate double bond to form Malate

211
Q

Malate Dehydrogenase

A

Oxidizes Malate hydroxyl to a keto group, producing NAD to NADH in the process

212
Q

Ethanol metabolism produces NADH. In alcohol poisoning:

A

The massive amount of NADH produced blocks of the TCA cycle. Gluconeogenesis stops, and patients can become hypoglycemic

213
Q

NADH created from beta oxidation and the TCA cycle

A

NADH from beta oxidation also inhibits TCA cycle and drives Acetyl-CoA towards ketone bodies synthesis

214
Q

Isocitrate dehydrogenase is regulated by:

A

Ratio of ADP to ATP. ADP increases affinity for substrate (Activator)

215
Q

The TCA cycle is amphibolic:

A

Catabolic: oxidizes carbons and reduces NAD and FAD for the generation of ATP via e- chain

Anabolic: TCA intermediates are feedstock for other biosynthetic pathways

216
Q

Myoadenylate deaminase deficiency

A

Inherited mutation in the gene coding for AMPD1 resulting in inactive AMP deaminase.

Exercise intolerance, muscle pain, weakness

217
Q

Intermediates of the TCA cycle affect gene expression through:

A

1. Histone acetylation and methylation
2. Cytosine methylation

218
Q

Lysine specific demethylase-1 (LSD1)

A

Transfers electrons from methyl group to FAD, then removes the carbon as formaldehyde 

219
Q

Jumanji Domain demethylases (JHDM)

A

Use molecular oxygen to hydroxylate the methyl carbon directly. Alpha KG is decarboxylated to succinate 

220
Q

Oxidation of benzopyrene and covalent bonding of DNA

A

• Benzopyrene is an aromatic polycystic hydrocarbon from cigarettes, oxidized within the cells to become carcinogenic 

221
Q

Transversion

A

 purine —> Pyrimidine

222
Q

Transition

A

Purine —> Purine

Pyrimidine —> Pyrimidine

223
Q

Strand directed mismatch repair

A
  • MUTL binds to mismatch base pair, MUTL scans the nearby DNA for a Nick
  • MUTL triggers the degradation of the next strand all the way back through the mismatch: Cut by Helicase
  • Repair occurs by DNA polymerase and DNA ligase
224
Q

MLH one mismatch repair defect

A

Common in HNPCC, Common colorectal cancer hereditary genes 

225
Q

Base excision repair

A

• DNA glycosylase removes deaminated base

• The sugar phosphate is cut out by AP endonuclease And phosphodiesterase

• The gap of a single nucleotide is filled by DNA polymerase and DNA ligase

226
Q

Nucleotide excision repair

A

• Bulky lesion is recognized
• One cut is made on each side of the Legion by DNA helicase, Removing a portion of the strand
• The DNA polymerase and ligase repair the strand 

227
Q

Xeroderma pigmentosum (XP) 

A

Genetically heterogeneous, Autosomal recessive disease of defective DNA repair that causes sensitivity to UV radiation, shortened lifespan

Cockayne is a closely related disease

228
Q

Double stranded break repair

A

• homologous end-joining with RecA/Rad51 — requires BRCA1&2 as accessory proteins (Uses sister chromatid to fill in missing DNA sequence)

• non-homologous end-joining with Ku protein (end joins Resulting in deletion of DNA sequence piece) 

229
Q

p53

A

Important G1 checkpoint control gene

  • 50% of all cancers have a defect in p53 Transcription factor
230
Q

Aneuploidy

A

Unusual chromosome number, occurs as a result of meiotic or mitotic non-disjunction

  1. Meiotic nondisjunction: causes embryonic lethality
  2. Mitotic nondisjunction go on a common event in cancer
231
Q

Chronic myelogenous leukemia (CML)

A

A translocation between chromosomes nine and 22

BRC-ABL: Philadelphia chromosome

232
Q

Mitotic Spindle Checkpoint

A

Maintains chromosome segregation Fidelity, Aneuploidy is often caused by defects in this pathway

233
Q

Translesion synthesis (TLS)

A

Damage tolerance process that allows DNA replication machinery to replicate past DNA lesions such as thymine dimers

234
Q

Desmosomes

A
  1. Cadherins (nonclassical)
  2. Linking proteins (armadillo proteins: plakoglobin, plankophilin)
  3. Keratin IFs
235
Q

Adherens junctions

A
  1. Cadherins (classical)
  2. Linking proteins (armadillo proteins: catenin, plakoglobins, vinculin)
  3. Actin MFs
236
Q

Hemidesmosomes

A
  1. Integrins, collagen XVII (BPAG2/BP180)
  2. Linking proteins (plakins: dystonin, BPAG1/BP230, Plectin)
  3. Keratin IFs
  4. Basal lamina and ECM
237
Q

Focal adhesions

A
  1. Integrins
  2. Linking proteins (vinculin, talin, paxillin)
  3. Actin MFs
  4. Basal lamina and ECM
238
Q

Restriction enzyme analysis

A

Restriction enzymes Find DNA at specific sequences, make double stranded cuts and cleave the DNA

Can be used to identify DNA, or recombine DNA (EcoR1) 

239
Q

Visualizing DNA fragments created by restriction enzyme digestion

A

Gel electrophoresis

DNA is sorted by charge, and by size

240
Q

Southern blotting

A

A technique to identify a specific region of DNA

Target DNA is identified by size and hybridization to a probe buy artificial complementary base pairing

241
Q

Sanger/Conventional DNA sequencing

A

Gives exact order of base pairs in a piece of DNA

Region to be sequenced is determined by choice of primer, Fragments of defined the lengths are generated by ddNTPs chain terminators

MOST SPECIFIC WAY TO IDENTIFY DNA

242
Q

Dideoxynucleotide chain terminators

A

DNA synthesis depends on 3’ OH of final nucleotide

Dioxane nucleotides are chain terminators because they lack 3’OH

243
Q

Polymerase chain reaction (PCR)

A

PCR amplifies a defined region of DNA— Specificity and amplification

Repeated cycles of in vitro DNA replication

Specificity because region to be amplified is determined by hybridization of short primers

244
Q

Clinical applications of DNA techniques

A

HPV, BRCA1, BRCA2 identification

245
Q

Northern blotting

A

The RNA equivalent of southern blotting. Based on DNA to RNA binding, or hybridization, through complementary base pairing

RNA in cell is separated by size, transferred to a membrane, defined piece of DNA or RNA probe binds specifically to target RNA, probe is labeled 

246
Q

RT-qPCR

A

Adapts PCR to quantitatively measure mRNA levels

All mRNA is converted to cDNA Using specific primers and PCR— fluorescent dye used to tag

Application is proportional to the initial number of mRNAs

247
Q

Ct (cycle threshold)

A

A measure of mRNA expression. It is inversely related to expression (More mRNA expression, less cycles needed)

248
Q

Microarray analysis 

A

Global analysis of mRNA levels, Identify all mRNAs that change expression in a disease state

Based on hybridization of cDNA population derived from sample mRNAs to a grid containing known DNAs at specific locations 

249
Q

Array

A

• DNA Oligos, 25 bases long
• Each oligo sequence matches an mRNA to be analyzed
• Oligos are arranged in grid sequence corresponding to mRNA and location

250
Q

Clinical applications of microarrays

A

COVID-19 detection — RT-qPCR to detect virus

Remdesivir— treatment for Covid. Analog of the endogenous nucleoside adenosine. Blocks viral reproduction by blocking synthesis of new RNA strand 

251
Q

Antibodies

A

• Antibodies are proteins made by B cells
• primary antibody targets specific protein
• Secondary antibody for visualization of primary (fluorescent)

252
Q

ELISA— Enzyme linked immunosorbent assay

A

Used to detect specific protein in a complex mixture

Primary anti- X (what you’re looking for)

Secondary: anti primary

253
Q

COVID-19 rapid antigen test ELISA

A

If a person has COVID-19 they will make viral proteins. The viral spike protein is abundant and immunogenic— Immobilizes primary antibody onto spike proteins

254
Q

Western blotting

A

Identifies a specific protein in the complex mix

Target protein is identified by size and specific interaction between antibody and protein 

255
Q

Clinical application of western blotting

A

Herceptin/trastuzamab as an antibody to HER2 growth factor receptor

— expressed in breast cancers

256
Q

Immune checkpoint blockade

A

Nivolumb and Pembrolizumab

These antibodies block an inhibitory checkpoint (PD-1-PD1-Ligand) which then releases the patient’s own immune system to attack the tumor.

257
Q

Next generation sequencing (NGS)

A

Faster, more information, identify mutations or genetic variants, identify somatic mutations, $1000 per genome, <24hrs 

258
Q

Clinical application of next generation sequencing (NGS)

A

Finding Somatic mutations— Sporadic cancer develops through acquisition of mutations that provide selective advantage to tumor

Molecular prenatal diagnosis: trisomy 21 

259
Q

RNA interference (RNAi)

A

Small non-coding RNAs regulate gene expression in the cell through RNA interference — miRNAs (micro) and siRNAs (short interfering) Can target specific mRNAs for degradation

260
Q

Clinical use of RNAi pathways 

A

Hepatitis B- Thought to work by targeting viral RNA for degradation

261
Q

CRISPR-CAS9

A

A system for making genomics alterations in DNA and living cells and organisms

• CAS9, endonuclease, sgRNA

Clinically: treating sickle cell disease

262
Q

Complex II (Succinate dehydrogenase) Does not span the inner mitochondrial membrane

A

No protons are pumped across the inner mitochondrial membrane, making complex II Create less ATP (FAD) 

263
Q

Proton motive force

A

The combined difference in proton concentration, pH, and difference in charge across the inner mitochondrial membrane

264
Q

12 protons = How many ATP?

A

3 ATP

4 protons = 1 ATP

265
Q

Chemical uncouplers

A

Dinitrophenol, salicylate

266
Q

Block complex I, NADH dehydrogenase

A

Amytal, rotenone

267
Q

Block complex II, Succinate dehydrogenase

268
Q

Block complex III, cytochrome b-c1 complex

A

Antimycin A 

269
Q

Block complex IV, cytochrome C oxidase

A

Azide, cyanide, CO

270
Q

Block complex V, ATP synthase 

A

Oligomycin 

271
Q

Blocks DNA pol-gamma, The mitochondrial DNA replication enzyme

A

AZT (zidovudine) <— anti-retro viral

272
Q

Adaptive thermogenesis in response to cold

A

• Norepinephrine activates a lipase which forms free fatty acids from triacylglycerol in brown fat cells

• A proton channel called thermogenin (UCP1) activated (proton hole, uncoupled— Dissipates gradient)

^^ Allows fat to be utilized for heat, independently of ATP conception



273
Q

Chemical uncoupler

A

Dinitrophenol (DNP) 

Carries over proton across gradient

274
Q

Mechanical uncoupling

A

• Peroxidation (ROS)
• Mitochondrial swelling do the influx of water

• proton leaking through holes in the membrane, cannot maintain sufficient gradient for ATP synthase to function

275
Q

Mitochondrial permeability transition pore (MPTP)

A

• Between ANT, VDAC, and other proteins

• this nonspecific poor causes depolarization of mitochondrial membrane and disrupts proton gradient

• regulated by cyclophilin D (CD)
• Inhibited by a high electrochemical gradient
• Activated by calcium, inorganic phosphate, and ROS

276
Q

Fasted state dominant hormone

277
Q

Fed state dominant hormone

278
Q

Starved state Dominant hormones 

A

Catecholamines, and glucagon

279
Q

Pancreatic beta cells express what gene?

A

INS1 gene

• A single large proteins, processed into two chains through the removal of C-peptide. Disulfide bonds link the two peptide chains after C-peptide is removed

280
Q

How is mature insulin stored?

A

Hexameric crystals stabilized by zinc atoms

281
Q

Insulin release process

A

Glucose —> ATP —> inhibits K+ outflow —> promotes Ca2+ inflow —> proteins fuse with membrane and insulin is released 

282
Q

Insulin receptor is a:

A

Receptor tyrosine kinase

• Insulin binding activates a kinase that phosphorylates tyrosine on itself and other proteins which make binding sites and aggregate proteins at the membrane

283
Q

Two main signaling arms from insulin receptor:

A

Phosphatidylinositol 3-kinase to PKB

Grb2 to MAPK 

284
Q

AKT activation by insulin results in:

A

Translocation of intracellular vesicles that contain the GLUT4 glucose transporter to the plasma membrane

285
Q

Primary source of energy during fasting

A

Amino acid synthesis to glucose

286
Q

Primary source of energy in a starved state:

A

Lipolysis to glycerol to glucose

Avoid proteolysis to preserve body

287
Q

Glucagon signaling a fasted state

A

Pancreas —> glucagon —> Second messenger cAMP —> Cellular response (Activation of protein kinase A)

288
Q

Where is glucagon stored?

A

In vesicles within pancreatic islet alpha cells

289
Q

Alpha cell glucagon release inhibited by

A
  1. Insulin
  2. GABA
  3. Zn 2+
    ^^^^^^^^ all from beta cell
    4 somatostatin from delta-cell 
290
Q

Hormone sensitive lipase (HSL) 

A

Inhibited by insulin, activated by glucagon

Triggers fatty acid energy synthesis

291
Q

Activation of protein kinase A for glucagon release

A

Glucagon—> cAMP—> PKA—> use of stored fuel 

292
Q

Positive sense genome

A

• mRNA, read easily
• The genome is the mRNA, no copy necessary


293
Q

Negative sense genome

A

• Copying step (opposite) where copy is read
• The genome contains an RNA dependent RNA polymerase, and needs to be copied— Copy is mRNA

294
Q

DNA binding proteins

A

Interact with DNA in a sequence specific manner

Major group of DNA is the main site of protein binding, inverted repeats frequently are binding site for regulatory proteins by homodimers

295
Q


Operon

A

Cluster of genes arranged in a linear fashion whose expression is under control of a single operator

Operator is located downstream of the promoter

Transcription is physically blocked when repressor binds to operator

296
Q

Arginine as a co-repressor

A

Arginine excess binds with repressor and activate it to shut off Gene operator that normally makes more arginine

Low arginine causes the release of arginine to repressor and synthesis begins again

297
Q

Negative control of transcription

A

Pulls something off to begin transcription

298
Q

Positive control of transcription

A

Puts something on to begin transcription

299
Q

Quorum sensing

A

Mechanism by which bacteria assess their population density

• Bacteria can create autoinducer molecule that diffuses freely across cell envelope in response to the presence of other cells of the same species— Allowing for transcription of specific same genes

300
Q

Conjugation as horizontal gene transfer

A

Direct contact between two cells where DNA transfer occurs— Specifically have plasmids

Example: F plasmid 

301
Q

Transformation as a horizontal gene transfer

A

Fragments of genomic material floating in space gets up taken by a cell an incorporated into their genome

Homologous recombination

302
Q

Transduction as a horizontal gene transfer

A

Genomic material from one cell enters another via a viral vector/bacteriophage

303
Q

Competent cells in transformation

A

Cells capable of taking up DNA and being transformed

Example: Griffiths experiment S and R cells

304
Q

Generalized transduction

A

DNA derived from virtually any portion of the host genome is packaged inside the mature virion 

305
Q

Specialized transduction

A

DNA from a specific region of the host chromosome is integrated directly into the virus genome

306
Q

Lytic pathway

A
  1. Viral DNA replicates
  2. Coat proteins synthesized; virus particles assembled
  3. Cell lysis and viral dumping occurs
307
Q

Lysogenic pathway

A
  1. Temperate virus inserted into host cell
  2. Viral DNA is integrated into the host DNA
  3. Cell divides, spreading viral and host DNA to the daughter cells
  4. When ready, phage DNA circularizes and detaches from host to DNA
  5. Detached DNA replicates and the cell lyses
    
308
Q

Rare event of transduction

A

When phage DNA attempts to detach, a portion of the host DNA is exchanged for phage DNA causing recombinant DNA that can enter new cells and spread the original host cell’s DNA

309
Q

HFR strains

A

Cells possessing an integrated plasmid, they cannot transfer the full chromosome plasmid, so they cannot create an F (+) cell from an F (-) cell

310
Q

Conservative transposition

A

Transposon is excised from one location and reinserted at a second location

One transposon total

311
Q

Replicative transposition

A

A new copy of transposon is produced and inserted at a second location

To transposons total (after 1 replication)

312
Q

Plasma versus serum

A

Plasma clots, serum does not

Plasma contains fibrinogen where serum does not (serum’s fibrinogen is in the blood)

313
Q

Lymph fluid

A
  • Lacks erythrocytes and platelets
  • less proteins
  • More leukocytes
  • Clots slowly (Some fibrinogen present)
314
Q

Never let monkeys eat bananas

A

Differential count for white blood cells (leukocytes)

N-eutrophils
L-ymphocytes
M-onocytes
E-osinophils
B-asophils 

315
Q

Granulocytes

A

Neutrophils, eosinophils, basophils 

316
Q

Agranulocytes

A

Lymphocytes, monocytes

317
Q

Thrombocytes

A

Platelets, derived from megakaryocytes. Platelets release from cytoplasm and have clotting mechanisms

318
Q

Neutrophil

A

Multi lobed nucleus, small red and purple granules

First line of defense, most common cell 

2X The size of a RBC

319
Q

Neutrophilic function

A
  1. Chemoattractants cause neutrophils to migrate to sides of infection
  2. Phagocytose bacteria, foreign objects, etc.
  3. Produce cytokines that attract and modulate other immune cells
320
Q

Neutrophilic Pathogen killing mechanisms

A

Phagocytosis, degranulation, neutrophil extracellular traps (NETs)

321
Q

Eosinophil

A

Bi- lobular nucleus, large granules, stains red, Has crystalline sub structure in granules

Destruction of parasitic worms

322
Q

Basophils

A

Irregular nucleus you can barely see, lots of dark hematoxylin stained granules

Increase for leukemia, chickenpox, small box, sinus inflammation

323
Q

Basophil functions

A
  1. Allergy and Inflammatory response
  2. Phagocytosis
  3. Release histamine, serotonin, heparin
  4. Produce leukotrienes (smooth muscle contraction)
324
Q

Lymphocytes

A

Large nucleus with hill and valley staining

B lymphocytes, T lymphocytes, natural killer cells

Creates large Buffy region in centrifuge 

325
Q

Monocyte

A

Kidney bean nucleus, large cell

Second line of defense against invading organisms. The differentiate into macrophages in the connective tissue and other places

326
Q

Chylomicrons

A

Found in plasma, enable fats and cholesterol to travel in water base solution of bloodstream

327
Q

Hemoconia

A

Junk in the bloodstream —> Cell debris —> spleen and liver process it out

If hemoconia is high, consider spleen or liver pathology

328
Q

Single cell motility

A

Important to embryonic development, necessary for immune cells circulation throat body, and would healing

329
Q

Mesenchymal motility

A

Rac and Cdc42 G proteins promote Acton polymerization at leading edge of the cell

Rho reorganize actin filaments into parallel arrays of stress fibers that connect to focal adhesions— myosin II interacts with actin stress fibers to pull the back end of the cell forward while focal adhesions dissemble

330
Q

Mesenchymal cells motility accompanied by release of proteases at the front of the cell does what?

A

Allows the front of the cell to digest impeding extra cellular matrix material, thereby allowing the cell to TUNNEL its way through dense ECM

331
Q

Focal adhesions

A

Provide necessary traction points for mesenchymal motility

Regions were bundles of microfilaments are physically linked with extra cellular matrix through into grins and linking/adapter proteins 

332
Q

Essential driver of cell motility

A

Rapid assembly and disassembly of focal adhesions. Preventing this freezes motility

333
Q

FAK and Src

A

Focal adhesion kinases, non-receptor tyrosine kinases that influence three major signaling pathways 

  1. Rho/Rac— Cytoskeleton organization
  2. MAPkinase— Regulate cell Proliferation and adhesion
  3. PI3K/PKB (AKT)— Promotes cell survival
334
Q

Amoeboid motility

A

Driven by actin myosin contraction

Microfilaments and myosin around cell periphery squeeze the cytoplasm forward— Movement only occurs if there are spaces large enough to accommodate the size of the nucleus/cell 

335
Q

EMT— Epithelial mesenchymal transition

A

Involves a loss of epithelial characteristics and a gain of mesenchymal characteristics. Interconnected cells in an epithelium can break loose and become motile

336
Q

The hippo pathway

A

Activated hippo pathway inhibits Yap/Taz which are two related transcriptional regulators That promote cell proliferation and motility

Hippo pathway phosphorylates yap/Taz (with kinases Mst1/2 abs Lats1/2) leading to their ubiquitination



337
Q

Yap/Taz

A

Transcriptional regulators that promote cell proliferation and motility when they are dephosphorylated 

They can enter the nucleus when dephosphorylated, and bind to an activate TEAD family transcription factors— inhibit apoptosis, promote cell division, promote cell motility 

338
Q

Loss of function mutations in the hippo pathway

A

Hyperactivate yap/Taz and thereby enhance growth and create unusually large organs

339
Q

Yap is active when:

A

• ECM is stiff
• Large surface area
• Sparse cells (far away)
• stretched cells

340
Q

Fibroblast activity feedforward loop

A

Fibroblast activity stiffens the ECM, stimulates Yap, Which further stimulates stiffening, leading to fibrotic diseases

341
Q

Cell density and hippo pathway

A

Growing tissues reached their appropriate size and cell density, hippo pathway is active to suppress yap and further Proliferation.

A reduction in cell density, like wounds, increase cell spreading and inhibit hippo and activate Yap

342
Q

Actin polymerization when high does what to hippo?

A

Inhibits hippo, activating yap

Actin in crowded cells is less polymerized which activates hippo

343
Q

Tension promotes what?

A

Microfilament assembly and myosin association

344
Q

Stretching of a cell promotes what?

A

Actin polymerization, and therefore inhibiting hippo and activating yap

345
Q

Cytoskeletal generated tension bridging and cell stretching do what for Yap/Taz?

A

Allow yap/Taz into the nucleus through pores 

346
Q

TGF beta signaling and ECM stiffness

A

When ECM is more stiff, LTBP1 and LAP can bind and cause pulling forces that release TGF-beta and allow it to activate SMAD transcription factors

347
Q

Soluble monomeric actin and MRTF

A

G Actin + MRTF keep MRTF in the cytoplasm by inhibition

When G Actin is pulled away by attention, allowing for Actin polymerization (to F actin) MRTF can enter the nucleus to regulate gene expression

MRTF used for gene survival

348
Q

High amounts of collagen

A

Higher collagen content increases ECM stiffness which activates yap/Taz, promoting cell proliferation and motility and inhibiting apoptosis

^^ causes tumors in dense breasts

349
Q

Stretch activated ion channels (SACs)

A

Activated by membrane stretching, membrane deformation, and fluid shear potentially releasing calcium into the cell

 Caveolae can flatten immediately to provide more membrane stretchiness so that the membrane won’t tear— Caveolae stretching signals to the cell 

350
Q

Activation of KlF2

A

Inhibits motility and proliferation of genes

Turbulent flow inhibits KlF2 expression resulting in plaques from proliferation, ROS generation, and inflammation

351
Q

Hydrophilic signaling molecules

A

Require cell surface receptors to generate signals inside the cell

352
Q

Hydrophobic signaling molecules

A

Can diffuse across the plasma membrane and bind to receptors inside the target cell either in the cytoplasm or nucleus

353
Q

Extra cellular signaling pathway

A

• ligand gated ion channels
• G-protein linked receptors
• Enzyme link receptors
• Proteolysis linked receptors

354
Q

Intracellular signaling pathways

A

• nuclear hormone receptors
• Nitric oxide and other dissolved gases

355
Q

Other signaling mechanisms

A

• Gap junction signaling
• Synaptic signaling

356
Q

Examples of a second messengers

A

• cAMP, cGMP
• IP3, DAG
• Ca2+

They transfer transduction signal to the target proteins

357
Q

Response types to signals

A

Graded response: the response proportional to the signal

Switch like response: all on or all off

358
Q

Switch like responses are regulated by:

A
  1. Adjusting the half life of a signaling protein
  2. Whether multiple subunits cooperate to trigger an action
  3. Positive feedback loops
  4. Involvement of protein kinases and G-proteins
359
Q

G proteins

A

Some signaling pathway components can be turned on via G-protein association, which themselves are activated or in activated by GTP or GDP

360
Q

Ways to desensitize a signal molecule

A
  1. Ligand binding to cell surface
  2. Ligand induced receptor endocytosis
  3. Phosphorylation of receptors or proteins involved
  4. Production of an inhibitor that blocks the transduction process
361
Q

Ligand gated ionotropic signaling

A

Binding of a signaling molecule to an ion channel that opens the channel. Very fast

Examples: GABA, serotonin, vanilloid, Acetylcholine 

362
Q

Ligand gated metabotropic signaling

A

Activates molecular cascades upon ligand binding, receptors are almost always GPCRs 

Releases G proteins that bind to ion channels and or intermediary effector proteins to open the channels, SLOW

Examples: Glutamate, Epinephrine, acetylcholine, serotonin

363
Q

Voltage gated ion channels

A

Found in cardiac muscle and neurons, membrane depolarization

364
Q

Mechanically gated ion channels

A

Associated with sensory functions including hearing, touch, stretch

365
Q

G-protein linked signaling is carried out by the interaction of what two components?

A
  1. G protein coupled receptors (GCPRs)
  2. Heterotrimeric G proteins
366
Q

Alpha monomer of a G protein

A

GTP/GDP binding switch

367
Q

Heterotrimeric G proteins are regulated by:

A

RGS: regulators of G-protein signaling

They function as GTPase activating proteins (GAP proteins)

368
Q

Activation of G-protein linked signaling 

A

GPCR binds in active heterotrimeric G-protein complex (acting as GTP exchange factor) Promoting exchange of GDP for GTP, activating the alpha subunit

369
Q

G-protein inactivation

A

Binding of the activated subunit to target protein stimulates the alpha subunits ability to hydrolyze GTP to GDP, turning it off soon after activating the target protein

370
Q

Three ways G-protein pathway is regulated by GPCR signaling

A
  1. Adenylate cyclase
  2. Phospholipase C
  3. Rho, Rac, Cdc42 Monomeric G proteins
371
Q

Gs and Gi

A

Stimulate and inhibit adenylyl cyclase, respectively

This increases and decreases protein phosphorylation, respectively

372
Q

Gq

A

Phospholipase C, increases protein phosphorylation by PKC, and activates calcium binding proteins by Ca2+ release 

373
Q

G12-13

A

Stimulate Rac, Cdc42, RhoA :

Rac: lamelipodia formation, actin polymerization, microtubule growth

Cdc42: filopodia formation, cell polarity, microtubule stabilization

RhoA: actin stress fiber formation, Actin filament stabilization, actinomyosin contractility, microtubule stability

374
Q

What is the main target of cAMP?

A

PKA (protein kinase A)

375
Q

 Calcium is released into the cytoplasm via three main types of calcium channels

A
  1. Voltage dependent calcium channels in the plasma membrane open in response to membrane depolarization
  2. IP3-gated receptors/channels allow escape from ER
  3.  RYR in the ER translate changes in membrane potential into calcium release from ER
  4. NOT RELEASE: SERCA Moves calcium back into ER
376
Q

Receptor desensitization

A

The decreased responsiveness that occurs with repeated or chronic exposure to an agonist

377
Q

Receptor downregulation

A

A decrease in the total receptor number due to endocytosis and subsequent degradation of the receptors 

378
Q

Arrestin binds to phosphorylated GPCRs and inhibits signaling by:

A

• blocking GPCR interaction with G proteins
• Promoting internal sequestration of GPCRs via endocytosis
• Routing GPCRs to protosomes for destruction

379
Q

Arrestin is stimulated by:

A

GRK (Like PKA and PKC)

380
Q

Glycogen synthase genes

A

GYS1: muscle

GYS2: liver

381
Q

What is a branching enzyme?

A

Glycosyl-4,6-transferase cleaves the chain after it hits around 11 glucose molecules, and creates a 1-6-glycostatic linkage

382
Q

Debranching enzyme

A

Cuts 1,4 bond one unit away from branching point and transfers the short chain to another non-reducing end: 4:4 transferase — glu-1-P

Cuts remaining 1:6 bond to get a glucose molecule

383
Q

Glycogen phosphorylase is activated when:

A

It is phosphorylated

384
Q

Glycogen synthase is active when:

A

It is DEphosphorylated

385
Q

GSD0

A

Glycogen synthase deficiency

GYS2: Liver, fasting ketotic hypoglycemia, small liver

GYS1: Muscle, skeletal and cardiac dysfunction

386
Q

GSD I: Vin Gierke disease

A

A deficiency in glucose-6-phosphatase

Fasting hypoglycemia, lactic acidosis, Hepatomegaly due to glycogen accumulation, hyper uricemia, hyperlipidemia

387
Q

GSD III: Cori Disease

A

Deficiency of 1,6-glucosidase activity of debranching enzyme — can’t debranch to give glucose (still makes Glu-1-P)

Fasting hypoglycemia, ketoacidosis, hyper lipidemia, Hepatomegaly

GSDIIIa: Liver and muscle
GSDIIIb: liver only 

388
Q

Is GSDIIIa or a GSDIIIb more severe?

A

1,6-glucosidase is more severe if it involves both liver and muscle— GSDIIIa

389
Q

GSD IV: Anderson disease

A

Severe, fatal in infancy: FTT, hepatomegaly, liver failure

Deficiency of branching enzyme 4,6- transferase — Long wavy form of glycogen that cannot be broken down

390
Q

GSD V: McArdle disease

A

Deficiency of muscle glycogen phosphorylase

Exercise and tolerance, myoglobinuria after exercise, Increased creatine kinase and increased ammonia after exercise

391
Q

GSD II: Pompe’s disease

A

Deficiency of lysosomal alpha-1,4-glucosidase activity

 — glycogen accumulates in heart and lysosomal tissue. Cardiomegaly 

392
Q

What is only found in the liver?

A

Glucose-6-phosphatase (removes phosphate to form glucose to be sent to other cells)

GLUT2, Glucokinase

393
Q

Key enzymes in glycogen synthesis

A

Glycogen synthase

Branching enzyme

394
Q

Key enzymes in glycogenolysis

A

Glycogen phosphorylase

Debridging enzyme

395
Q

Types of carbon bonds in glycogen

A

1:4 — linear chains

1:6 — branched points off linear chains

396
Q

Reducing end vs nonreducing end

A

1 C is reducing end (ketone)

397
Q

What does glycogen phosphorylase do?

A

Breaks the 1,4 bonds between glucose units and adds inorganic phosphate to create gluc-1-P to either be used for glycolysis in skeletal muscle, or the phosphorylated to glucose in the liver 

398
Q

GSD VI: Hers disease

A

Mutations in liver glycogen phosphorylase— opposite of McArdles disease 

399
Q

What controls the phosphorylation state of glycogen phosphorylase?

A

Hormone glucagon, epinephrine, norepinephrine, cortisol

Phosphorylated by: PKA, glycogen synthase kinase-3 

400
Q

Glycogen phosphorylase

A

In the Fasted State, glycogen phosphorylase is active promoting glycogen breakdown

401
Q

Glycogen synthase

A

In the fed state, glycogen synthase is active promoting the creation of glycogen

FOM (5 decks)

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