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FOM > Exam 2 > Flashcards

Exam 2 Flashcards

1
Q

Goldilocks of oral dose

A

Keep above minimum effective concentration but below toxicity level

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2
Q

Pharmacodynamics

A

What drug does to the body

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3
Q

Pharmacokinetics

A

What body does to the drug. ADME, absorption, distribution, metabolism, elimination

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4
Q

Absorption

A

Passage of drug molecules from admin site to the blood

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5
Q

Distribution

A

Passage of drug molecules from blood to tissues

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6
Q

Metabolism/biotransformation

A

Chemical mods of the molecule to typically make it more water-soluble and excreted

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7
Q

Elimination

A

Passage of molecules through the blood to the outside of the body via urine, bile, etc

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8
Q

Free drugs

A

Only the free drug can be moved around: no protein or plasma binding

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9
Q

Transport

A

Move molecules across concentration gradient. Both active and passive

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10
Q

Passive transport

A

Channel-mediated and carrier mediated with the concentration gradient

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11
Q

Active transport

A

Carrier protein. Against concentration gradient, requires ATP

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12
Q

Endocytosis

A

Requires ATP, bulk flow, moves in both directions

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13
Q

Filtration

A

Does not require ATP, moves with the gradient

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14
Q

Ionization: weak acid

A

Proton donor, easily absorbed/cross membranes from stomach: in an acidic environment

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15
Q

Ionization: weak base

A

Proton acceptor, not readily absorbed in stomach. Bases readily cross membranes in basic environment (increase stomach pH)

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16
Q

Ion trapping

A

Ability to trap compounds on one side of the membrane or if there is a pH gradient across the membrane (trapped in anionic form)

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17
Q

Henderson-Hasselbach

A

pH - pKa = log [nonprotonated]/[protonated]

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18
Q

HH for weak acids

A

A-/HA = [ionized]/[nonionized]

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19
Q

HH for weak bases

A

B/BH+ = [nonionized]/[ionized)

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20
Q

Ratio of protonated to nonprotonated in ionic trapping

A

Is the Rate limiting step. Ex: base in plasma (pH:7.4) is log 1, where in stomach (pH:1.4) is log 1/10^6

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21
Q

Ion trapping weak acids

A

Trapped in basic environments

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22
Q

Ion trapping weak bases

A

Trapped in acidic environments

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23
Q

Oral administration advantages

A

Easy, drug stable at room temp, cost, good patient compliance

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24
Q

Oral admin disadvantages

A

Destroyed in GI, 1st pass hepatic metabolism, variable rate, diet affects absorption rate

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25
Q

Bioavailability

A

How much drug makes it into the circulating plasma (absorption)

eqn: F = AUC.oral / AUC.iv where AUC is area under the curve and 0

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26
Q

Bioavailability of IV admin

A

100%

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27
Q

Things that affect drug distribution

A

1.) tissue perfusion rates
2.) plasma protein binding
3.) partitioning between plasma and tissues

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28
Q

Distribution: Perfusion Rate

A

Higher rate: faster equilibrium
Highest: kidney, liver, lung, brain
Intermediate: muscle
Slowest: adipose / fat tissue, bone

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29
Q

Distribution: plasma protein binding

A

Bound drugs are inert, do not cross membranes (ex. Albumin and a1-acid glycoprotein)

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30
Q

Albumin

A

Plasma protein that binds weak acids

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31
Q

a1-acid glycoprotein (AGP)

A

AGP binds many weak acids

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32
Q

Distribution: Plasma partitioning

A

Concentration of drug between plasma and tissue not equal from
1.) ion trapping
2.) tissue protein binding
3.) lipid solubility

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33
Q

Blood Brain Barrier

A

Tight endothelium junctions in capillary bed and glial cells. Astrocytes and glial cells also protect

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34
Q

VD : apparent volume of distribution

A

Total amount in body/ total concentration in a measured reference area (in L because g/g/L)

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35
Q

VD variation causes

A

1.) bodily accumulation of fat for lipid-soluble drugs
2.) accumulation of fluids for water-soluble drugs

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36
Q

VD increase/decrease

A

VD increase: things that cause drug to LEAVE plasma
VD decrease: things that cause drug to STAY IN plasma

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37
Q

Cofactor

A

Non-protein molecule that is a part of an enzymatic rxn. Organic material or metal ions.

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38
Q

Cofactors as substrates

A

Enzyme activity (particularly for apoenzymes) is dependent on cofactor concentration

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39
Q

Diet deficiency

A

Not enough of a cofactor or cofactor precursor in the diet (ex. Niacin, B12, etc)

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40
Q

Functional deficiency

A

No vitamin modification by cellular enzymes present OR inability of cofactor to bind to active site of enzyme

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41
Q

Prosthetic groups

A

Tightly, covalently bound cofactors to their enzymes: for lifetime of enzyme (ex. FAD). Cofactor modifications occur while still attached to enzyme

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42
Q

Transiently bound cofactor

A

Act like any other substrate or product. Bind for the rxn and release afterward. Separate rxn occurs to restore cofactor. (Ex. NAD for ADH)

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43
Q

Functions of redox reactions

A

1.) fuel oxidation: succinate dehydrogenase
2.) detoxification: alcohol dehydrogenase, cytochrome P450s
3.) biosynthesis: HMG CoA reductase

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44
Q

Redox potential

A

The willingness of molecules to accept electrons. Dictated by NERST eqn: deltaG0’ = -n F deltaE0’

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45
Q

Redox cofactors

A

NADH
NADPH
FAD(2H)
Ascorbic acid
Metals: Cu, Fe, etc

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46
Q

NADH and NADPH

A

Derived from niacin (B3 in diet). NADH is important for fuel oxidation. NADPH is important for biosynthesis and detoxification enzymes

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47
Q

Cytochrome P450s

A

Has NADPH as cofactor (and FAD, FMN, and Fe-heme) Fxn: add oxygen to chemicals to make them more soluble and easier to excrete

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48
Q

Cholesterol biosynthesis rate limiting step

A

NADPH oxidized by HMG-CoA reductase

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49
Q

Sources of Niacin (B3)

A

Meat, whole grains, fortified cereals, tryptophan (causes B6 deficiency)

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50
Q

Niacin deficiency

A

Causes: Pellegra Affects:
- pellegra - reliance on corn
- dermatitis - alcoholics
- diarrhea - sun exposed areas
- death
- glossitis

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51
Q

ADP Ribosylation

A

NAD+ is a substrate for enzymes that post-translationally modify arginine (glycosylation) residues on proteins. Nicotinamide is removed from NAD+ and the remaining portion is covalently linked to arginine.
- occurs by PARP1 when DNA is damaged and ADP ribosylation of histones initiates DNA repair

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52
Q

PARP1 inhibitors

A

Used in cancer treatments: cancer cells cannot signal repair for their DNA (ex. BRCA1 & BRCA2 genes)

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53
Q

Cholera toxin (CTA-1)

A

Uses NAD+ as substrate for ADP ribosylation of Arg AAs. This blocks GTPase activity resulting in constitutive activity (Cl- floods so H2O floods: diarrhea)

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54
Q

FMN and FAD

A

Derived from B2– riboflavin. Prosthetic groups for redox enzymes. They accept single e- (in the form of H) one at a time. They are involved in creating and destroying double bonds

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55
Q

Succinate dehydrogenase and FAD

A

FAD reduced to FAD(2H) by enzymes that convert single bonds to double bonds. TCA Cycle succ. Dehydrogenase does this

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56
Q

Dietary riboflavin, B2 (FAD and FMN)

A

Milk, eggs, organ meats, legumes, mushrooms

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57
Q

Riboflavin deficiency

A
  • Cheilosis (mouth sores), and glossitis (swollen, beefy tongue)
  • keratitis
  • seborrheic dermatitis
  • normochromic/normocytic anemia
  • fatigue
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58
Q

Glutathione

A

Important antioxidant in cells, glutathione reductases use NADPH and FAD to transfer electrons to the sulfur atoms

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59
Q

Ascorbic acid (vitamin C) functions

A

A redox cofactor for
1.) hydroxylase enzymes (collagen synthesis, neurotransmitter synthesis, and oxygen sensing)
2.) a non-enzymatic anti-oxidant

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60
Q

Ascorbic radical

A

Vitamin C intermediate between L-ascorbate and Dehydro-L-ascorbic acid. Can gain/lose 2 e- which helps stabilize free radicals

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61
Q

Prolyl hydroxylases and Ascorbic acid

A

Vit. C is a redox cofactor helping w post-translational hydroxylation of lysine and proline for collagen synthesis

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62
Q

Lysyl hydroxylase and Ascorbic acid

A

Vit. C is redox cofactor. Post-trans mod hydroxylation of lysine and proline for collagen

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63
Q

Collagen

A

Important connective tissues. Every third AA is glycine, 3 collagen peptides form triple helix. Stabilized by hydrogen bonding of hydroxyproline and hydroxylysine

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64
Q

Ascorbic acid deficiency

A

Scurvy. Characterized by defects in connective tissue, slow wound healing, apathy, anemia, gingival lesions, petechiae, and enlargement of costochondral junctions

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65
Q

Metal electron conducting cofactors in redox rxns

A

Iron (Fe2+-> Fe3+) copper (Cu+-> Cu2+), cobalt (Co2+-> Co3+), manganese (Mn2+-> Mn3+), molybdenum (Mo4+-> Mo6+)

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66
Q

Activation transfer reactions

A

Move fxnal groups around
Examples: kinase, acyltransferase, acetyltransferase, aminotransferase, and pyrophosphatase

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67
Q

Kinase

A

Transfers phosphate group to and from ATP

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68
Q

Acyltransferase

A

Transfers carbon chains from one substrate to another *most common

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69
Q

Acetyltransferase

A

Transfers acetyl groups from one substrate to another

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70
Q

Aminotransferase

A

Transfers amine groups on amino acids

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71
Q

What other rxns do activation transfer reactions couple with?

A

Redox rxns, and lyase rxns

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72
Q

Pyruvate dehydrogenase complex

A

Links glycolysis with the TCA cycle and regulates the oxidation of carbon derived from glucose

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73
Q

Pyruvate dehydrogenase (PDH) and mitochondria

A

PDH is a gatekeeper that regulates glycolytic substrates’ complete oxidation in the mitochondria

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74
Q

PDH inactivated

A

Glucose is conserved and the TCA cycle is powered by fatty acid and amino acid catabolism

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75
Q

Multi subunit complex that catalyzes the oxidative decarboxylation of the three carbon Pyruvate

A

Pyruvate dehydrogenase

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76
Q

PDH complex rxn to create acetyl-CoA

A

-3 transfer and 2 redox cofactors
1.) decarboxylation (thiamine pyrophosphate)
2.) reduction and oxidation (FAD and NAD+)
3.) transfer acyl group (Lipoate and CoASH)

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77
Q

Thiamine pyrophosphate

A

TPP participates in decarboxylation rxns (including of Pyruvate, where the remaining 2 C covalently bond to TPP)

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78
Q

Thiamine

A

Vitamin B1 : meat, legumes, whole grains, fortified cereals. Heat labile

Phosphorylated to diphosphate form, and binds to decarboxylases creating an active apoenzyme

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79
Q

SLC19A transporter

A

Transports thiamine from diet into the cell

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80
Q

Thiamine deficiency occurs in what cases?

A

Malnutrition, alcoholism, and monotonous diet

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81
Q

Beriberi

A

Thiamine deficiency: headache, malaise, peripheral neuropathy, heart failure

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82
Q

Wet Beriberi

A

Cardiac problems

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83
Q

Dry beriberi

A

Neuropathy

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84
Q

Wernicke encephalopathy

A

Thiamine deficiency: confusion, AMS, nystagmus, ataxia

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85
Q

Karsokoff psychosis

A

Thiamine deficiency: amnesia, confabulation, evident in ~80% of people diagnosed with Wernicke

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86
Q

Thiamine responsive magaloblastic anemia syndrome

A

Inherited mutations in the thiamine transporter SLC19A2: anemia, deafness, non-type I diabetes

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87
Q

Lipoate

A

Forms covalent bond w lysine residue on transacylase subunits of alpha-keto acid dehydrogenase complexes

Cofactor for E2 subunit of pyruvate dehydrogenase

Accepts the 2 Cs from TPP and becomes lipoic acid

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88
Q

Lipoate in born errors

A

Epilepsy can occur. No deficiency ever seen

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89
Q

Coenzyme A (CoASH or CoA) action mechanism:

A

Covalently binds acyl groups through high energy thioester bond and transfers them

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90
Q

Coenzyme A dietary precursor

A

Pantothenic acid, B5 : no deficiency present

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91
Q

Coenzyme A and TCA cycle

A

Coenzyme A accepts the 2 Carbon acetates from lipoamide in PDH rxn to form acetyl CoA: used in TCA cycle

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92
Q

Biotin participates in what reactions?

A

Participate in carboxylation rxns.

Cofactor for: acetyl CoA carboxylase, pyruvate carboxylase, propionyl CoA carboxylase, methylcrotinyl carboxylase

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93
Q

Acetyl CoA carboxylase

A

Fatty acid synthesis

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94
Q

Pyruvate carboxylase

A

Gluconeogenesis

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95
Q

Propionyl CoA carboxylase

A

Branched chain fatty acid metabolism

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96
Q

Methylcrotinyl CoA carboxylase

A

Branched chain amino acid metabolism

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97
Q

Biotin as a cofactor

A

Covalently bound to the app carboxylase to form a holocarboxylase

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98
Q

Biotin in the diet

A

Free or covalently bound to lysines in protein

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99
Q

Biotinidase

A

Removes free biotin from protein form

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100
Q

Biotin deficiency

A

From raw eggs: Avidin binds to biotin and makes in indigestible

Symptoms: scaly dermatitis, thinning hair, alopecia

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101
Q

Pyridoxal phosphate (PLP) function

A

A cofactor for enzymes that metabolize amino acids (ex. Transaminases)

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102
Q

Pyridoxal phosphate dietary precursors

A

Pyrodoxine, Pyridoxal, and Pyridoxamine. All considered vitamin B6 found in cereal, meat, bananas, etc

Phosphorylated by cellular kinases

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103
Q

Pyridoxal phosphate deficiency

A

Infants: seizures, diarrhea, EEG abnormalities
Adults: peripheral neuropathy

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104
Q

PLP as a cofactor

A

Converts tryptophan to niacin: double deficiency. The kynureninase requires PLP in trp —> niacin rxn

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105
Q

PLP Overdose

A

Symptoms: sensory neuropathy, ataxia

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106
Q

Pyridoxine oxidase deficiency/ antiquitin deficiency

A

Inborn errors of metabolism resulting in B6 deficiency symptoms in newborns

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107
Q

Cobalmin B12 functions

A

Transfers and rearranges methyl groups

2 forms in body: deoxyadenosylcobalmin and methylcobalmin

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108
Q

Methionine synthase cofactor

A

Methylcobalmin

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109
Q

Methylmalonyl CoA mutase cofactor

A

Adenosylcobalmin: essential for catabolism of branched chain AAs and fatty acids

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110
Q

Cobalmin B12 dietary groups

A

Produced by bacteria in animals. Animal products have B12. Vegans do not get B12

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111
Q

Cobalmin deficiency

A

Symptoms: Macrocyctic/megaloblastic anemia (failure to make nucleotides), weakness, fatigue, seizures, sensory defects, FTT

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112
Q

Homeostasis

A

Physiological control processes incorporating + and - feedback loops

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113
Q

Variability

A

Contributes to inter and intrapersonal differences in homeostasis

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114
Q

Homeostasis regulation steps

A

1.) detects changes in condition and operation

2.) control systems regulate responses

3.) mechanism to effect change in operational state

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115
Q

Physiological agonist

A

Effectors that work to return the system to the set point (return to homeostasis)

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116
Q

Physiological antagonist

A

Effectors that move conditions away from the set point

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117
Q

Negative feedback loop

A

Change in variable to return set point (homeostasis)

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118
Q

Positive feedback loop

A

Further from set point

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119
Q

Nested loop

A

When + amplifies a bigger - loop and vice versa

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120
Q

Mechanism for negative feedback loop

A

-stimulus changes variable
- sensor detects change and signals to controller
- controller activates/inactivated effector
-effector alters conditions so the variable is returned to set point

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121
Q

Mechanism for positive feedback loop

A

-change in variable to further change by the stimulus
- sensor detects change and signals controller
- controller activates/inactivates effector
- activated effectors alter conditions and the change is amplified
- regulator (required) stops the process

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122
Q

The 3 levels of control

A

Tissue, involuntary, and voluntary

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123
Q

Local homeostasis is maintained by:

A

Direct connections between tissue sensors and effectors

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124
Q

Info from local processes flows:

A

Up to a higher control system

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125
Q

The voluntary system receives:

A

Direct sensory input and info from lower centers

Voluntary system can directly and indirectly control effectors

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126
Q

Feedback

A

Positive and negative adjustment AFTER the regulated variable has changed

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127
Q

Feedforward

A

Adjustment occurs BEFORE changes in the regulated variable occur (ex HR before exam)

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128
Q

Autocrine signaling

A

The signal itself

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129
Q

Paracrine signaling

A

Signals nearby cells

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130
Q

Endocrine signaling

A

Signals distant cells via hormones secreted

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131
Q

Neurocrine signaling

A

Signal nearby OR distant cells via neurotransmission

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132
Q

Immune signaling

A

Inflammation during injury, etc

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133
Q

Translation

A

The conversion of info on RNA into proteins — in cytosol

64 3 nucleotide codons in mRNA encode 20 AAs

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134
Q

Direction of codon reading

A

5’ —> 3’ with the n-terminus containing AUG (met) for the start codon of translation

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135
Q

Stop codons

A

UAA, UAG, UGA

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136
Q

Reading frame

A

Starting the read at 5’ end either on the first, second, or third nucleotide causing frameshifting for formation of different polypeptide strands

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137
Q

Frameshift mutations

A

Insertion or deletion of nucleotides in anything besides multiples of 3

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138
Q

TRNA region that recognizes and binds to specific AA

A

Short, single stranded region on 3’ end of tRNA

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139
Q

Aminoacyl-tRNA synthetase

A

Recognize and attach correct AA to the tRNA covalently (different aa-tRNAs for each AA)

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140
Q

HIGH ENERGY BOND IN TRANSLATION

A

Synthetases use ATP hydrolysis to produce high energy bond between 3’ end of tRNA and AA: the energy of breaking this bond is used to link the AA covalently to the growing peptide chain

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141
Q

The two adapters that act one after another in translation

A

1.) Aminoacyl-transferase (couples AA and tRNA)
2.) tRNA molecule itself (anticodon forms base pair w appropriate codon on mRNA)

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142
Q

EPA sites

A

On ribosomes:
E: exit site
P: peptide bond (peptidyl-tRNA)
A: incoming site (aminoacyl-tRNA)

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143
Q

Prokaryotic ribosome

A

70s
^
50s 30s
^ ^
5s 23s 16s

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144
Q

Eukaryotic ribosome

A

80s
^
60s 40s
^ ^
5s 28s 5.8s 18s

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145
Q

Start of protein synthesis

A

-AUG (met) typically removed by protease later
- eukaryote: initiator tRNA loaded into small subunit (eIFs)
- small subunit binds to 5’ end of mRNA (recognized by 5’ cap bound to eIF4E and eIF4G)
- AUG found: initiation factors disperse, larger ribosomal unit binds
- tRNA occupies P-site
- A site available and ready for aminoacyl-tRNA

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146
Q

Shine Delgarno sequence

A

5’ AGGAGGU 3’ forms base pairs with the RNA 16S subunit in order to position the AUG start codon

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147
Q

Elongation factors for prokaryotes

A

EF-Tu and EF-G

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148
Q

Elongation factors for eukaryotes

A

eEF-1 and eEF-2

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149
Q

What do elongation factors do?

A

Speed up processes but also cause 2 pauses between codon-anticodon base pairing and peptide elongation to remove incorrectly bound tRNAs before they are added to the chain

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150
Q

Protein release factors: termination

A

Bind to ribosome w/ stop codon in the A site and this binding forces peptidyl transferase to add a water molecule instead of an AA to the peptidal-tRNA which frees the carboxyl end from its attachments to tRNA and the chain floats into cytoplasm & ribosome units are released

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151
Q

Tetracycline

A

Antibiotic: blocks binding of amino acyl-tRNA to the A site of the ribosome. Small ribosomal unit

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152
Q

Streptomycin

A

Antibiotic: prevents the transition from translation initiation to chain elongation and also causes miscoding. Small ribosomal subunit

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153
Q

Chloramphenicol

A

Antibiotic: Blocks the peptidyl transferase rxn on ribosome. Large ribosomal subunit

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154
Q

Erythromycin

A

Antibiotic: Blocks the exit channel of the ribosome and thereby inhibits elongation of the peptide chain. Large ribosomal unit

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155
Q

Rifamycin

A

Antibiotic:blocks initiation of RNA chains by binding to RNA polymerase (prevents RNA synthesis).

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156
Q

Presumptive diagnosis

A

Differential, vague

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157
Q

Definitive diagnosis

A

Specific: identifies causative microorganisms using diagnostic tests

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158
Q

Empiric treatment

A

Common, treats many diseases only okay

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159
Q

Definitive treatments

A

Specific: treats specific disease and targets specific organism

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160
Q

The gram stain

A

1.) heat fixed smear: all cells purple
2.) add iodine solution: all cells purple and fixes the gram + purple color
3.) decolonize w alcohol: gram + cells purple, gram - cells colorless
4.) counterstain w safranin: gram + cells purple, gram - cells pink/red

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161
Q

Antony Can Leeuwenhoek

A

1684: created first magnifying glass which had 200x magnification

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162
Q

Robert Hooke

A

1665: first to visualize bacteria in book minute bodies

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163
Q

Louis Pasteur

A

Work against spontaneous generation led to the development for controlling the growth of microorganisms. Sterile broth vs broth exposed to the air

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164
Q

Spontaneous generation

A

Hypothesis that live can generate from non-living matter

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165
Q

Robert Koch

A

-Germ Theory of Disease
- Koch’s postulates:
1.) the suspected pathogen must be present in ALL cases of disease and absent from healthy animals
2.) the suspected pathogen must be grown in pure culture
3.) cells from pure culture of pathogen must infect healthy animal
4.) pathogen must be reisolated and be the same as the original

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166
Q

Fredrick Griffith

A

1928: proved DNA is heritable w experiment w rough strain (non virulent) and smooth strain (virulent) disease

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167
Q

Virulence

A

The ability for microorganism to cause disease. Degree of pathology caused by organism (ex: toxins, surface coats, receptors, etc)

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168
Q

Mechanism of bacterial disease

A

1.) Toxin production: bacteria released toxin that causes illness
2.) host immune response
3.) bacterial proliferation and invasion

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169
Q

Mechanism of viral disease

A

1.) cytopathic effect: affects normal cell physiology
2.) host immune response
3.) tumorgenesis

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170
Q

Bioenergetics

A

Differences in potential energy between substrates and products of a rxn

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171
Q

Kinetics

A

The speed at which a rxn occurs — substrates converted to products

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172
Q

Enzymes:

A

Increase speed of rxn — do not alter bioenergetics

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173
Q

DeltaG

A

Release of free energy of the system.

DeltaG = deltaH - T•deltaS

174
Q

DeltaH < 0

A

Exothermic, gives off heat/energy

175
Q

DeltaH > 0

A

Endothermic, absorbs heat/energy

176
Q

DeltaS

A

Entropy: amount of disorder

S >0 order decreases

S <0 order increases

177
Q

Michaelis-Meten eqn

A

V= Vmax [S]/ Km + [S]

• measure the effects of pH
• compare different isoforms
• measure PTMs
• identify potency

178
Q

Enzyme kinetics are dependent on pH because

A

1.) the ionization of AAs at the active site is dependent on pH
2.) some enzymes use protons (H+) as substrates or products

179
Q

Lineweaver Burke

A

Creates linear model of michaelis Menten eqn

180
Q

Competitive inhibitors

A

Increase the Km, Vmax unchanged

  • adding more substrate will outcompete the competitor
181
Q

Km

A

The concentration of substrate required to permit the enzyme to achieve half Vmax

182
Q

Non competitive inhibitors

A

Lower Vmax, permanent, does not change Km

  • no amount of additional substrate will fix this
183
Q

Allosteric regulations

A

-taut (T) or relaxed (R) conformations

  • inhibitors or activators bind at allosteric site and alter enzymes conformation and activity
184
Q

Taut conformation

A

-tense, does not want to bind, low affinity for binding

185
Q

Relaxed conformation

A

Binds substrate more readily, higher affinity

186
Q

Activators of allosteric regulation

A

Make the curve more hyperbolic and reaches v max more quickly (left shift)

187
Q

Inhibitors of allosteric regulation

A

Flattens the sigmoidal curve (right side U) (right shift)

188
Q

Pasteurization

A

Process of using precisely controlled heat to reduce microbial load in heat sensitive liquids: does not sterilize

189
Q

Nonionizing radiation

A

Causes abnormal bonds, thymine dimers are most common: 240-280nm is most lethal

190
Q

Confidence intervals

A

CI = p +/- (coefficient)•SE

Coefficient of 95%: 1.96
Coefficient of 99%: 2.58

191
Q

Membrane functions

A

•establish specialized environments
•scaffold to organize biochem rxns
•semi-permeable barrier (ion gradient)
•transport

192
Q

Membrane organization is driven by what?

A

Amphipathic nature of phospholipids

193
Q

Mobility types of membrane phospholipids

A

Lateral diffusion, flexion, rotation

  • flip-flop is rare
194
Q

Three major groups of membrane proteins:

A

• receptors
• transporters
• enzymes

195
Q

Cytosolic leaflet

A

Faces the cytoplasm

196
Q

Non-cytosolic leaflet

A

Faces the lumen (inside) of an organelle, or extra cellular environment (plasma membrane)

197
Q

Phosphatidylserine

A

Negatively charged, affects electrochemical features of the membrane. Fxns include: apoptosis and blood clotting

*** concentrated in the cytosolic leaflet

198
Q

Sphingomyelin

A

Enriched lipid rafts, can be GLYCOSYLATED to form glycolipids. Fxns include: cell identity, adhesion, and protection

*** extracellular space, on non-cytosolic leaflet

199
Q

Gangliosides

A
  • made from sphingomyelin
  • prominently in neurons
  • over accumulation= toxic to neurons
200
Q

Ganglioside GM1

A

Cell surface receptor for bacterial toxin that causes cholera diarrhea (continuous Cl- flow)

201
Q

Cholesterol

A

Interacts w fatty acid tails and modulates bilayer characteristics. Changes: fluidity, thickness, compressibility, water penetration, and intrinsic curvature

202
Q

Phosphatidylinositol

A

EXTREMELY IMPORTANT:
1.) cell signaling pathways
2.) imparting organelle membrane identities

Turtle: inositol positions 3,4,5 can be Phosphorylated, where C1 holds onto diester phosphate linkage

203
Q

Phosphotidylinositol functions

A

• cell signaling
• Ca2+ regulation
• enzyme activation
• gene regulation
• membrane identification
• seeding biochem rxns

204
Q

Cardiolipin

A

Unique dimeric phospholipid w 4 fatty acyl chains in mitochondria — Fxns: chemiosmatic events associated w oxidative phosphorylation

205
Q

Lipid rafts

A

Special membrane domains w a concentration of specific lipids and proteins. (Sphingolipids). Fxns: transport vesicle formation and signal transduction

206
Q

Caveolae

A

Curved membrane domains— special lipid raft. Phospholipids w cholesterol + sphingolipids + CAV1 (caveolin)

Fxns: signal transduction, regulation of metabolism, reservoir membrane, and cancer

207
Q

Membrane lipids formed in the ER

A

• Phosphotidylinositol
• phosphatidylserine
• phosphatidylcholine
• phosphatidylethanolamine
• cholesterol

208
Q

Membrane lipids formed in the ER & Golgi A

A

• sphingomyelin
• glycolipids

209
Q

Lipid membranes formed in mitochondria

A

Cardiolipin

210
Q

The enzymes that assemble phospholipids are located on the:

A

Cyotplasmic surface of the ER membrane

211
Q

Flippases

A

Translocate phospholipids from non-cytosolic to cytosolic

212
Q

Floppases

A

Translocate phospholipids from cytosolic to non-cytosolic

213
Q

Scramblases

A

Randomly flip phospholipids between leaflets

214
Q

Fxns of phosphatidylserine on the non-cytosolic leaflet of plasma membranes: platelets

A

Platelets: externalized PS= platform where coagulation factors assemble

215
Q

Fxns of phosphatidylserine on the non-cytosolic leaflet of plasma membranes: apoptotic cells

A

Apoptotic cells: externalized PS = EAT ME signal for phagocytic cells

216
Q

Glycosylation and lipid membranes

A

• enzymes that glycosylate are in the ER LUMEN
• oligosaccharide chains are modified in golgi A
• Fxns: receptors, cell-cell recognition, modulating membrane stability

217
Q

Where are sugars and oligosaccharides of glycolipids/proteins present?

A

SURFACE OF THE MEMBRANE

218
Q

Integral membrane proteins

A

Anchored in lipid bilayer:
1.) polypeptide chain embedded/transversing membrane
2.) covalently bonded to lipid bilayer

219
Q

Peripheral membrane protein

A

Associate w integral membrane proteins/ membrane lipids. Are easy to displace

220
Q

Lipid modifications that anchor integral membrane proteins

A

1.) glycosylphosphatidylinositol anchors (GPI anchors)

2.) prenylation (farnesylation or geranyl-geranylation) include RAS superfamily of small G-proteins

221
Q

RAS small G-proteins

A

Important regulators of cell division and cytoskeletal organization

222
Q

Functions of glycoproteins

A

• modulation of membrane surface properties
• cell identification
• cell adhesion

223
Q

Glycosylation

A

Glycosylation occurs in ER and modified by Golgi A

224
Q

Glycocalyx function

A

Protection
- found commonly in intestinal epithelial cells

225
Q

Membrane damaging conditions

A

Ca2+ serves as trigger to initiate repair mechanisms

226
Q

RER function

A

• synthesis of integral membrane, luminal, and secreted proteins
• lipid synthesis
• Ca2+ signaling

227
Q

SER function

A

• lipid synthesis (Steroids)
• detoxification rxns
• Ca2+ signaling

228
Q

Vesicular transport

A

ER—>Golgi A—>lysosome—>plasma membrane

229
Q

Signal Recognition Particles (SRPs)

A

Recognize polypeptides by their signal sequence, and bind to ribo-mRNA-polyp SRP complex to bring PP into ER

230
Q

Lumenal proteins

A

Signal sequence is hydrophobic, gets immobilized in bilayer. Protein gets released into ER LUMEN and signal sequence is degraded.

231
Q

Integral membrane proteins

A

Start/stop transfer sequence also immobilized in bilayer. Finished protein + sequence released into plane of MEMBRANE by lateral opening of transport complex

232
Q

Glycosylation: N-linked and O-linked

A

N-linked: asparagine via Nitrogen (most common) in the ER

O-linked: serine and threonine via Oxygen in the Golgi A at the surface. sometimes ER

233
Q

Chaperone proteins BiP/GRP78

A

Help proteins fold correctly

234
Q

ERAD

A

ER-associated protein degradation. Proteins deglycosylated, ubiquitinated, and targeted by PROTEASOMES for destruction

235
Q

Protein misfolding diseases

A

• Alzheimer’s disease
• Parkinson’s disease
• Huntington’s disease
• Cystic fibrosis
• Gaucher’s disease
• Creutzfeldt Jakob disease

236
Q

unfolded protein response (UPR)

A

UPR- ATF6, IRE1, and PERK draw out BiP from its original position (keeping proteins inactive) which activates proteins and the UPR — Triggering ERAD

237
Q

Remediation of protein misfolding

A

1.) suppresses overall translation except genes involved in the UPR to reduce processing load

2.) Increases the expression of chaperones, other folding mediators, and proteins of the ERAD system

3.) if not corrected UPR primes cells for apoptosis and autophagy 

238
Q

MAMs

A

Mitochondrial associated membranes, specialized areas of ER – mitochondrial apposition involved in mutual lipid and ca2+ metabolism and signaling

239
Q

SERCA (sarco-ER calcium ATPase)

A

Pumps Ca2+ out of the cytoplasm and into the ER lumen

240
Q

IP3-gated and RyR channels

A

Open to release calcium into the cytosol under appropriate stimulation for multiple cell responses

241
Q

Malignant hyperthermia

A

Mutation in RyRs that pump calcium out of ER. The ATP hydrolysis to pump calcium back into ER (out of cytosol) raise body temperature to fatal levels

242
Q

Detoxification

A

— mostly in SER
— cytochrome p450
— oxidizing enzymes, make compound more hydrophilic so they enter bloodstream
— liver cells have good SER detox system

243
Q

ER Stress diseases

A

Alzheimer’s, Parkinson’s, amyotrophic lateral sclerosis, type two diabetes, atherosclerosis, nonalcoholic fatty liver disease, HCV, HPV, alcoholic liver disease, cancer

244
Q

CHOP

A

A transcription factor upregulated by the UPR that promotes apoptosis

245
Q

Golgi apparatus function

A

• Modifies N- linked glycoproteins received from the ER
• Glycosylated O-linked glycoproteins and proteoglycans
• Participates in sphingomyelin and glycolipid synthesis
• Sorts and packages material for transport

246
Q

COP- coat protein complex

A

Protein complexes involved in the secular trafficking 

247
Q

COP-II

A

ER —> Golgi. including: Sar1

248
Q

COP-I

A

Golgi—> ER. Including: Arf

KDEL sequence - brings proteins back to ER that shouldn’t have left

249
Q

Monomeric G-proteins

A

• can bind GTP or GDP
• Have inherent GTPase activity
• Function as switches, ON when bound to GTP, OFF when bound to GDP


250
Q

Rho family

A

Cytoskeleton G-proteins

251
Q

Ran family

A

Nuclear transport G-proteins. Regulates directionality of nuclear-cytoplasmic transport

252
Q

RAS family

A

Cell division, G-proteins

253
Q

Sar/Arf and Rab family

A

Membrane trafficking G-proteins

254
Q

GEF: Guanine nucleotide exchange factor

A

Turns G-proteins ON by exchanging GDP for GTP

255
Q

GAP: GTPase Activating protein

A

Turns G-protein OFF by activating the GTPase activity, resulting in the hydrolysis of GTP—>GDP

256
Q

GDI: Guanine dissociation inhibitor

A

Inhibits GDP dissociation, keeping a G-protein turned OFF

257
Q

Processing events in Golgi A

A

1.) Oligosaccharide modification of N-linked glycol proteins made in the ER

2.) Formation of proteoglycans through O-linked glycosylation

3.) Addition of a phosphorylated mannose tag (M6P) to proteolytic enzymes destined for lysosomes

258
Q

GAGs

A

Glycosaminoglycan: Long, unbranched polysaccharides with a repeating disaccharide structure. They help make up proteoglycans

259
Q

COG: Conserved oligomeric Golgi

A

Keep different components of the glycosylation machinery and their correct cis-to-trans locations. Ensures correct sequence of glycosylation rxns

260
Q

COG mutations (CDGs)

A

• severe neurological impairment
• Liver and muscle dysfunction
• infant lethality 

261
Q

All bacteria have:

A

1.) cell membrane
2.) chromosome or nucleiod
3.) ribosomes
4.) cytoplasm

262
Q

Two major systems for disposal in cells

A

Proteasomes and lysosomes

263
Q

Lysosome:

A

Polymorphic membrane-enclosed compartments that are filled with hydrolytic enzymes and substrates in the process of being digested

264
Q

Proteasomes

A

Digest protein molecule by molecule

265
Q

Endocytosis

A

Primarily extracellular material taken up by the cell

266
Q

Autophagy

A

Includes parts of the cell itself, from individual molecules and macromolecular arrays, to organelles and volumes of cytoplasm

267
Q

Lysosomes contain about 40 enzymes:

A

Proteases, nucleases, glycosidases, lipases, phospholipases, phosphatases, and sulfatases

268
Q

Acid hydrolases:

A

What make up Lysosomes, maximally active at low pH of 4.5-5.0

269
Q

Specializations of the lysosomal membrane:

A

• lysosomal membrane proteins are highly glycosylated for protection

• Contain proton pumps (H+ ATPases) to create an acidic lumen for maximal activation of the acid hydrolases

• contain numerous transporters to shuttle material past the membrane in both directions (Substrates in, products out)

270
Q

MP6 receptors in the trans Golgi concentrate what?

A

Lysosomal enzymes into vesicles

271
Q

What does endocytosis use to digest?

A

1.) Pinocytosis
2.) receptor-mediated endocytosis
3.) chaperone-mediated autophagy

272
Q

What does Autophagy use to digest?

A

1.) macroautophagy
2.) microautophagy
3.) chaperone-mediated autophagy

273
Q

Pinocytosis (cell drinking)

A

Constitutive non-specific endocytosis that internalizes extracellular fluid and plasma membrane via small uncoated vesicles

274
Q

Receptor-mediated endocytosis

A

Receptor-ligand binding and internalization of specific cargo molecules

275
Q

Phagocytosis

A

Engulfment of large particles (bacteria, dead cells,etc) into large specialized and dissolves called phagosomes

276
Q

Responsible for plasma membrane turnover and renewal. The entire area of plasma membrane engulfed every 30 to 60 minutes in some cells

A

Pinocytosis

277
Q

Macropinocytosis

A

Engulfment of larger volumes via extensions of cytoplasm that fold over and fuse, entrapping extracellular fluid and associated material

278
Q

Where is Pinocyted material routed to for lysosomal digestion?

A

Endosomes

279
Q

Receptor-mediated endocytosis

A

Employs receptor-ligand interactions at plasma membrane to internalize SPECIFIC molecules

280
Q

Clathrin

A

A coat protein similar to COPI and COPII, helps drive vesicle formation. Removal of coat helps vesicles fuse with target membrane

281
Q

Triskelions

A

Formed by clathrin, self-assemble to form basket-like cage around forming vesicles

282
Q

Steps in clathrin vesicle formation

A

1.) receptors bind to their specific ligands (cargo)

2.) Adapter proteins bind receptor-ligand complexes

3.) clathrin assembles onto the adapter proteins, deforming the membrane informing a coated pit

4.) vesicle invaginates as more clathrin added, DYNAMIN protein pinches off neck of vesicle

5.) uncoating ATPases remove clathrin coat, vesicle can fuse w target membranes

283
Q

Hsp70 family

A

Uncoating ATPases

284
Q

Familial hypercholesterolemia (FH)

A

Mutations in LDLR receptor for LDL particles or in apoplipoprotein B (ligand for LDLR)  Resulting in high circulating LDL/cholesterol levels

285
Q

Endosomes

A

Collection of irregular and dynamic membrane bound compartments that receive both plasma membrane derived vesicles filled with endocided material and vesicles filled with acid hydrolases from Golgi a

286
Q

Endosomes can be functionally subdivided into:

A

1.) early and recycling Endosomes

2.) late Endosomes/multivesicular bodies 

287
Q

What can fuse with Endosomes?

A

• Receptor-mediated endocytotic vesicles
• Pinocytotic vesicles
• caveolae-originating vesicles
• macropinosomes

288
Q

Transcytosis

A

Transfer of endocytosed material across the cell, which is then released, essentially unmodified, through exocytosis

289
Q

Sorting signal for proteins to be degraded in lysosomes

A

Ubiquination

290
Q

Intraluminal vesicles

A

Ubiquinated Cytoplasmic material can bind to specific endosomal subdomains causing INWARD pinch to form cargo-containing vesicles

291
Q

ILVs transform Endosome regions into:

A

Multivesicular body (MVB)

292
Q

ESCRT complexes

A

Endosomal sorting complexes required for transport: function to invaginate and endosomal membranes inward to form ILV’s within the lumen of the endosome

293
Q

PH change during lysosomal maturation

A

PH decreases to 4.5 for acid hydrolase activity optimization

294
Q

Phagosome

A

Formed by the formation of cytoplasmic extensions called pseudopods over the material desired

Process is driven by the actin cytoskeleton

295
Q

Phagolysosome

A

When phagosomes fuse with lysosomes for digestion

296
Q

Two classes of specialized phagocytes

A

Macrophages and neutrophils

297
Q

Macroautophagy

A

Refers to self eating. The process by which a cell turns over its own components. Survival mechanism

298
Q

Microautophagy

A

Formation and internalization of vesicles formed by invaginating lysosome membranes that entrap cytoplasmic material to be digested

299
Q

Chaperone-mediated autophagy

A

Individual molecules in the cytoplasm can be transferred through the lysosome membrane to be digested.

Proteins are denatured by chaperones so they can be spooled through membrane transporters

300
Q

Autophagosome

A

Formed by Cisterna of ER to wrap around an engulf material to be disposed. This double-membrane-bound structure than fuses with a lysosome

301
Q

COP and Clathrin

A

 COP involved in trafficking between ER and Golgi. Clathrin is involved in receptor mediated endocytosis and lysosomal trafficking.

Both are protein coats required to be removed diffused with target membranes

302
Q

Constitutive secretion

A

Vesicle contents not specifically segregated or concentrated by the Golgi, are released continuously in small vesicles.

Vesicle membrane itself is important cargo in terms of replenishing the plasma membrane

303
Q

Regulated secretion

A

Secretary granules accumulate in cells and the granule content is released by exocytosis upon appropriate stimulation. 

Used for bio active compounds necessary for cell and tissue function

304
Q

Exosomes

A

Released by ILVs outside of the cell by exocytosis of MVBs

305
Q

What do exosomes do?

A

Signal and influence the behavior of other cells. 

Exosomes released from cancer cells can interact with potential metastatic tissue sites to make colonization by circulating tumor cells more likely

306
Q

Microvesicle formation:

A

A direct outpouching and pinching off of cytoplasm-containing vesicles from the plasma membrane

307
Q

Exosomes and mircovesicles may:

A

• fuse with plasma membrane of a target cell

• Be endocytosed by a target cell. Both endocytosis and fusion release vesicle contents into recipient cell cytoplasm

• bind to the target cell surface

• Open to release their contents in the extracellular environment


308
Q

Function of microvesicles

A

Intercellular communication: which can include transfer of membrane, cytosolic proteins, lipids, and RNA

309
Q

Phosphatidylinositol lipid markers

A

Marks organelles and membrane domains. This helps determine which adapter proteins bind to which cargo receptors throughout the endocytic and secretary pathways 

310
Q

PI(4,5)P2 binds:

A

Adapter AP2

311
Q

AP2 binds:

A

Cargo receptors

312
Q

Assembles on PIP2-cargo receptor-AP2 complex and vesicle formation is initiated

A

Clathrin

313
Q

RAB G-proteins

A

Regulate the motility and directionality of vesicle trafficking

314
Q

V-SNARES and t-SNARES

A

Bind at the target site and wind around each other to draw vesicle and target membranes close enough to drive fusion

315
Q

Where does intracytoplasmic vesicle transport take place?

A

Along tracks of microtubules

316
Q

SNARE proteins

A

Mediate the final recognition and fusion of cargo carrying vesicles with target membranes/organelles

317
Q

Lipofuscin granules

A

Indigestible residues from lysosomal activity that accumulate in the cell. Promoted by accumulation of glycosphingolipids

Age/wear and tear pigments

318
Q

Fenton rxns

A

Production of reactive oxygen species (ROS) from iron ions concentrated in lipofuscin granules

319
Q

Ferroptosis

A

A type of cell death triggered by ROS generation due to the buildup of iron ions.

Neurons are particularly sensitive to this process

320
Q

Lysosomal storage diseases (LSDs)

A

Caused by genetic defects that affect one or more lysosomal hydrolases.

Results in the accumulation of undigested substrates in the lysosomes with severe pathological consequences, most often in the nervous system

321
Q

I-cell disease (mucolipidosis II)

A

Autosomal recessive disorder resulting in a Deficiency in phosphotransferase activity, preventing M6–>M6P. Leads to the failure to route almost ALL lysosomal enzymes to lysosomes.

322
Q

Mitochondria

A

• double membrane bound
• Inner membrane thrown into folds or tubules called cristae
• electron transport chain located on inner membrane 

323
Q

Mitochondrial matrix contains:

A

Mitochondrial DNA, ribosomes, proteins and enzymes that facilitate the citric acid, urea cycles, and beta oxidation

324
Q

Fission and fusion

A

Mitochondria continually undergo fission and fusion, which is necessary for optimal functioning.

325
Q

Fission/fusion state

A

Depends in part on the respiratory activity of the mitochondria

326
Q

Mitophagy

A

Autophagy of damaged mitochondria

327
Q

Microtubules in mitochondria

A

Help organize mitochondria within the cell. And helps coupling with the ER

328
Q

Location of mitochondria

A

Generally localized to where ATP is needed.

Muscle fibers, sperm flagellar anoxeme, salivatory glands, etc.

329
Q

GRP75

A

Glucose regulated proteins

330
Q

IP3R

A

Inositol triphosphate receptor

331
Q

mCU

A

Mitochondrial calcium uniporter

332
Q

MFN

A

Mitofusin 

333
Q

MAMs Ca2+ transfer

A

Calcium from the ER to the mitochondria occurs at MAM‘s, via A linkage between ER inositol triphosphate receptor, and mitochondrial voltage dependent anion channel (VDAC)

334
Q

MAMs phospholipid exchange

A

Phospholipid exchange proteins (PEPs) mediate exchange of membrane lipids between ER and mitochondria.  this is how mitochondria gets most membrane lipids, except cardiolipin

335
Q

Mitochondrial genome

A

A circular chromosome containing about 40 genes. Includes 413 proteins that are important for the electron transport chain.

OXPHOS genes in mitochondria help with immediate transcriptional responsiveness to redox state of mitochondria

336
Q

Heteroplasmy

A

Each mitochondrion contains multiple chromosome copies, so some of these copies may exhibit mutations but not all of them.

The more heteroplasmy, the worse the disease

337
Q

Mitochondrial inheritance

A

Maternal in humans, resulting from the fact that sperm mitochondria degenerate after fertilization

338
Q

Mitochondrial biogenesis

A

Input of two genetic systems: the mitochondrial and nuclear genomes.

Proteins encoded by mitochondrial genome are made in the mitochondrial matrix and then transported to correct location

339
Q

Translocator complexes

A

TOM: trance locator of the outer mitochondrial membrane

TIM: translocator of the inner mitochondrial membrane

OXA: cytochrome oxidase assembly trans locator. Transports proteins synthesized in the matrix into the inner mitochondrial membrane

340
Q

Anterograde signaling for mitochondria

A

Signals from nucleus—> Mitochondria

Mainly depends on nuclear-encoded transcription factors

341
Q

Retrograde signaling in mitochondria

A

Signals from mitochondria—> Nucleus

This happens in response to perturbations within mitochondria such as proteostasis stress, ROS production increases, and energy deficiencies

342
Q

Mitochondrial nuclear communication and aging

A

Mitochondrial DNA is more prone to damage and mutation, resulting in positive feedback loop where increased mitochondria damage leads to more ROS which leads to more damage. This place is central role in aging

343
Q

Peroxisome

A

Involved in a variety of oxidation reactions, including the production and removal of hydrogen peroxide

Fxns include:
• Detoxification reactions
• Formation of myelin phospholipids
• breakdown of very long chain fatty acids and branched chain fatty acids (VLCFAs and BCFAs)

344
Q

Specialized regions of chromosomes

A

1.) telomeres
2.) Origins of replication
3.) Centromere
4.) Heterochromatin
5.) Euchromatin
6.) Nucleolar organizing region
7.) Matrix attachment regions

345
Q

Chromosome location

A

Chromosomes tend to occupy discreet territories in the nucleus.

Active regions of chromosomes can move to preferred nuclear locations during transcription

346
Q

Fibrillarin

A

A component of snoRNPs and nucleoli

347
Q

Nuclear speckles

A

Enriched in pre-mRNA splicing factors

348
Q

Coilin

A

A component of cajal bodies

349
Q

Nuclear pore complex

A

A few thousand pores per nucleus. Each pore is comprised of about 30 nucleoporins. Pores are semi-permeable 
• 5000 Da or less = Freely permeable
• Between 5000 and 60,000 Da = Permeable but at a slower rate
• Over 60,000 Da = Not freely permeable, must be actively transported


350
Q

Determining directionality of nuclear cytoplasmic transport

A

Increase GDP and GAPs = cytosol

Increased GTP and GEFs = nucleus

RAN family G-proteins

351
Q

LINC

A

Linker of nucleoskeleton and cytoskeleton

352
Q

Adapter proteins (vincullin, talin) and integrins (IMPs) 

A

Physically connect the acting cytoskeleton to the extracellular matrix

353
Q

Nuclear lamina

A

Underlays the nuclear envelope. A meshwork of filament serving as a physical support, and may also participate in regulating gene expression.

354
Q

SUN/ Nesprin proteins

A

Connect the nucleus and cytoskeleton by binding to each other and spanning both the inner and outer membranes of the nuclear envelope.

 Nuclear plasmic portion binds to lamins, and cytoplasmic portion binds to microtubules in actin cytoskeletal elements

355
Q

Mitchondria and ER linkage

A

Ca2+ dynamics

356
Q

Nucleolus

A

A large aggregate of macromolecules including:
- rRNA genes
- precursor and mature RNA
-snoRNA
- ribosomal proteins
- partially assembled ribosomes

357
Q

Imported nuclear proteins must:

A

Bind important receptors in the presence of GDP, and dissociate in the presence of GTP

358
Q

Exported nuclear proteins must:

A

Bind export receptors in the presence of GTP and dissociate in the presence of GDP

359
Q

Bayer

A

Developed sulfonamides. First antimicrobial material

360
Q

Alexander Fleming

A

Created penicillin

361
Q

Antibacterial spectrum

A

Range of activity of an antimicrobial against bacteria

362
Q

Antimicrobial chemotherapy

A

The use of chemotherapeutic drugs to control infection

363
Q

Antimicrobials

A

All inclusive term for an antimicrobial drug, regardless of what type of microorganism it targets

364
Q

Bacteriacidal antibiotic

A

Antibiotic that kills bacteria

365
Q

Bacteriostatic antibiotic

A

Antibiotic that inhibits the growth of bacteria but does not kill

366
Q

Beta- lactamase

A

An enzyme that hydrolyzes the beta lactam ring in the beta lactam class of antibiotics, inactivating the antibiotic. Penicillincillinases, cephalosporinases, carbapenemases

367
Q

Broad spectrum

A

Antibacterial drug that can inhibit a variety of gram-positive and gram-negative bacteria

368
Q

Definitive therapy

A

Used to treat a patient where the micro organism has been identified

369
Q

Empiric therapy

A

Used to treat a symptomatic patient where are the microorganism causing infection has not been identified

370
Q

Minimum inhibitory concentration MIC

A

Determined by exposing a standardized suspension of bacteria to a series of anti-microbial delusions. The lowest antibiotic concentration that inhibits the growth of the bacteria is the MIC 

371
Q

Narrow spectrum

A

Anti-bacterial drug that is active against a limited variety of bacteria

372
Q

Prophylaxis

A

Use of a drug to prevent eminent infection of a person at risk

373
Q

Suppressive therapy

A

After initial disease is controlled, therapy is continued to prevent recurrence

374
Q

Kirby Bauer test

A

1.) inoculate plate with a liquid culture of a test organism

2.) Disks containing antimicrobial agents are placed on the surface

3.) Incubate for 24 to 48 hours

4.) Test organism shows susceptibility to some agents, indicated by inhibition of bacterial growth around discs

375
Q

Zone of inhibition

A

Zone around antimicrobial disk in a Kirby Bauer test that shows susceptibility versus resistance

376
Q

Selective toxicity

A

The ability to inhibit or kill a pathogen without affecting the host

377
Q

Drug spectrum of activity

A

The narrow or extended ranges of a drugs ability to be an antibiotic effectively

378
Q

Preemptive

A

Lab test indicate organism is present, but patient is not symptomatic

379
Q

Problems with microbiota

A

Potential pathogen resistant to drug but held in check by other microbes. Drug destroys beneficial biota, and pathogen takes over

380
Q

Two faces of drug distribution

A

1.) drug distributes to tissues with hyperfusion rates

2.) The drug later distributes to tissues with low perfusion rates. The drug is still present in the body, but it can’t be used

381
Q

Areas in the body with high perfusion

A

Liver, kidney, heart

382
Q

Areas in the body with low perfusion

A

Fat, muscle

383
Q

Biotransformation

A

The chemical modification of compounds, typically to make them more polar, in order to activate and inactivate drugs 

384
Q

Primary and secondary sources of biotransformation

A

Primary is the liver

Secondary is the G.I. tract

Third is kidney, followed by lungs and skin

385
Q

Phase 1 reactions Biotransformation

A

• Add or expose functional groups

• oxidation most common reaction

386
Q

Cytochrome P450s

A

Terminal oxidases, metabolize 75% of known drugs

Key CYPs: CYP3A, CYP2D6, CYP2C

Localized to smooth endoplasmic reticulum

387
Q

Substances that induce cytochrome P450

A

• Saint johns wort (CYP3A4)

• Ethanol (CYP2E1)

• Cigarette smoking (CYP1A1,1A2,2E1)

• Antidepressants, antipsychotics

388
Q

Substances that inhibit cytochrome P450

A

• grapefruit juice (CYP3A4)

• Drug-drug interactions

• pharmacogenomics 

389
Q

Individuals as metabolizers

A

Ultra rapid metabolizer, extensive metabolizer, intermediate metabolizer, poor metabolizer

390
Q

Biotransformation phase 2 reactions

A

Less reactive, conjugation with charged species. Glucuronidation Is most common, followed Acetylation, sulfate conjugation, methylation, glutathione conjugation causing INACTIVATION 

391
Q

Glomerular Filtration rate

A

The flow rate of filtered fluid through the kidney: specifically through glomeri

392
Q

Three modes of excretion in kidney

A

1.) filtration

2.) Reabsorption

3.) Secretion

393
Q

Kidney filtration

A

Portion of blood flow in the kidneys is filtered through glomerular capillaries to remove compounds

394
Q

Kidney reabsorption

A

Create concentration gradient in collecting tubule and compound diffuses back out. Facilitated or passive diffusion process

395
Q

Kidney secretion

A

Active transporters along tubule selectively pore compounds from plasma and dump into the urine (ex. Too large but needs to leave the body)

396
Q

Renal clearance (CIr)

A

The volume of plasma (mL) that is cleared of drug by the kidney per minute

397
Q

GFR and CLR will be the same when

A

A solute is freely filtered and not reabsorbed or secreted

398
Q

Filtered and reabsorbed in kidney

A

CLR < GFR

Many drugs have this

399
Q

Filtered and secreted in kidney

A

CLR > GFR

P aminohippurate (PAH) has this

400
Q

Biliary expression

A

Fecal excretion, process initiates in liver and passes through the gut until products are excreted along with waste. Typically avoids tissue and absorption entirely

401
Q

Respiratory excretion

A

Gases can be blown out of the lungs and removed. Example: anesthetic gases

402
Q

Where can gene expression be regulated?

A

• DNA structure
• when, where and how often a gene is transcribed
• How a transcript is spliced
• If mRNAs are transported out of the nucleus, and where in the cytosol they are localized
• which mRNAs are translated
• rate of mRNA degradation
• Control of the Pro Tien: activation or an activation, degradation, trafficking and compartmentalizing

403
Q

Gene copy number

A

There are multiple copies and normal/abnormal copy number variation creates different levels of expression.

Example: allelic imbalance, gene duplication, or gene loss 

404
Q

Translocation of genes

A

Can you put genes in a different context based on where they are located

405
Q

Local alterations in chromatin structure or directed by:

A

Eukaryotic gene activator proteins

406
Q

Cis-acting factors

A

Short stretches of DNA of defined sequences

407
Q

Trans-acting factors

A

Gene regulatory proteins 

408
Q

Transacting regulatory proteins factors

A

Act to modify activation from someplace else

409
Q

What serves as recognition sites for a wide variety of regulatory proteins?

A

Short nucleotide sequences, usually less than 20nt, most commonly found in gene promoters

Mammals: Sp1, Oct1, GATA1, MyoD, p53

410
Q

Homeobox protein NANOG

A

A key Jean regulatory proteins that helps embryonic stem cells maintain pluripotent see by suppressing self determination factors

411
Q

Homeodomain proteins

A

Special subclass of helix-turn-helix proteins, and are key regulators of animal development. Contain an identical stretch of 60 amino acids

412
Q

Zinc finger motif proteins

A

Important group of regulatory proteins that use one or more zinc atoms in their DNA finding motifs

413
Q

Leucine zipper motif

A

In leucine zipper proteins two alpha-helices, one from each monomer, are joined together to form a short coiled-coil structure

The dimer grips DNA like a close pin on a clothesline

414
Q

Helix-loop-helix motif

A

A short alpha-helix connected by a loop to a longer alpha-helix. Can create both homodimers and heterodimers

415
Q

Heterodimerization does what?

A

Increases the variety of DNA sequences recognized by regulatory proteins. They are an example of combinatorial control

416
Q

Lac operon

A

The lac operon is on when CAP is bound, but lac repressor is not bound.

+ lactose = repressor not bound

  • glucose = CAP bound 
417
Q

Enhancers

A

Regulatory sites that are distant from the promoter.

418
Q

Domains of gene regulatory proteins

A

A structural motif: recognizes specific DNA sequences

Activation domain: accelerates transcription

419
Q

Transcriptional synergy

A

Regulatory proteins when added together create MORE of an effect

420
Q

Enhanceosome

A

A group of proteins that form together on an enhancer to regulate transcription at a distance. You need ALL of the proteins to have the right effect

421
Q

Insulators

A

DNA sequences that prevent regulatory proteins from influencing distant sites. They divide the genome into independent domains

422
Q

Epigenetics

A

Heritable, reversible changes in the genome that regulate gene expression, Most often resulting in gene silencing. Can be influenced by environment.

DNA methylation is a common example 

423
Q

Mammalian X chromosome inactivation

A

Synthesis of XIST into XIC locus. Correlated with the condensation of the chromosome (bar body) 

424
Q

De novo DNA methylation

A

Causes recruitment of metal binding proteins, that in turn causes chromatin condensation, resulting in gene silencing

425
Q

Imprinting

A

Differential expression of a gene allele depending on parental origin; the purpose is to control gene dosage

Caused by 5-cytosine DNA methylation leading to chromatin condensation

426
Q

IncRNA rare mechanism for imprinting

A

IncRNA acting on chromatin, imprinting gene located on intron 11 of a non-coding RNA

427
Q

CTCF methylation rare mechanism for imprinting

A

Methylation of the CTCF insulator element activates and enhancer for the lgf2 gene 

428
Q

Fragile X syndrome

A

Silence is FMR1 and messes up regulation of translation by irregulating the shuttle between the nucleus in the cytoplasm

429
Q

Iron starvation

A

Cytosolic aconitase binds so that ferritin is NOT made, it also binds so that transferrin receptor is made

430
Q

Excess iron

A

Iron binds to cytosolic acconitase so that it cannot bind to anything, so that ferritin is made and transferrin receptor is NOT made

FOM (5 decks)

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