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Foundations of Medicine > FOM Week 1 > Flashcards

FOM Week 1 Flashcards

1
Q

Phase Contrast Microscopy.

A

Polarized light passes through the cell. The light gets measured as it bends due to passing through cellular molecules/organelles

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2
Q

H&E Stain

A

Hematoxylin stains nucleic acids blue
Eosin stains elastic and reticular fibers pink
Lots of blue is bad

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3
Q

Osmium

A

A heavy metal that binds to lipid membranes
Myelin stains heavily because of this
Often used with electron microscopy

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4
Q

What are the two secrets to Cell life

A

Their ultimate goal is to pass along genetic info

They do so by producing energy. Once energy is stopped being produced the cell dies

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5
Q

Effects of Aspirin

A

Aspirin effects the body in three ways

  1. Inhibits COX which prevents blood clotting
  2. Intereferes with ATP synthesis by coupling with H+ ions
  3. Effects activity of brain
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6
Q

Differentiate between the genome, transcriptome, exome, and proteome; relate DNA sequence, RNA sequence, and protein primary structure.

A

Genome is complete DNA sequence of an organism
• Only 2% encodes for proteins
• Genomics will lead to individualized medicine
Transcriptome includes all types of RNA (mRNA, rRNA, tRNA..)
• Not all RNA is used for proteins
• Better source of info on proteins than genome
Exome is all of the exons that are left after splicing. These get translated into proteins usually
Proteome is all the proteins in an organism
• Gets measured by mass spectrometry
DNA–>RNA–>Protein

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7
Q

Current diagnostic limitations of genome/transcriptome/exome sequencing.

A

Genome used to take a long time and was expensive. Some ethical issues are present on rather or not this info can be stored and released to clinics or family members
Over 10,000 SNPs. Which ones matter?
Errors in sequencing machines
Duplication in the genome causes confusion
Mosaicsim and Chimerism

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8
Q

Chemical Forces Influencing Protein 3-D Structure

A 
Non Covalent forces such as:
H+ bonds
Ionic Interactions
Hydrophobicity
Vaan Der Waal Forces
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9
Q

What holds the quaternary structure together

A

Non Covalent Interactions

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10
Q

Quaternary vs Aggregation

A

Quaternary is a controlled process and is regulated

Aggregations are glumped together and unregulated

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11
Q

Protein Motion

A

Small side chains can rotate
Larger structure can act as hinges
Difficult to see

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12
Q

Moonlighting

A

One protein can have more than one function due to multiple domains

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13
Q

Fibrilar Proteins

A

Repeating globular subunits that form long twisted fibers/structures

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14
Q

Integral Membrane Proteins

A

Have an inside out structure
Hydrophobic areas will be on outside since the lipid membrane is hydrophobic
25-30% of ORFs

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15
Q

Intrinsically Disordered Proteins

A

Have lots of hydrophillicity and repeating sequences
This makes them not fold up easily and they remain fairly linear
Make up about 30% of Human Proteins

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16
Q

Homolog

A

Proteins that have a similar sequence of amino acids

Only take about 25% similarity to have a similar structure

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17
Q

Classes of Proteins

A 
Enzymatic
Structural
Transport
Signaling
Storage
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18
Q

Isoforms

A

Proteins that have a similar function but crucial differences

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19
Q

What amino acids can be phosphorylated

A

Any with an -OH R group

Ser, Thr, Tyr

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20
Q

Protein Modularity

A

The ability of proteins to have discrete areas with specific functions
Helps to increase the efficiency

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21
Q

Cytoplasm Crowding

A

When hydrophobic areas become exposed and aggregate with other hydrophobic areas

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22
Q

Factors That Influence Unfolding

A 
pH
Temp
Salt
Urea
Pressure
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23
Q

Types of Osmolytes

A

Methylamines- TMAO
Amino Acids- Pro, Ala, Tau
Polyols- Sorbitol and Glycerol

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24
Q

Heat Shock Proteins

A

Small chaperone subunits that bind to the unfolded region of proteins and assist them
Get upregulated during times of stress

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25
Q

Chaperonins

A

A large ring complex protein that can fit up to 400 amino acids in it to assist in folding

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26
Q

Ways to Degrade Proteins

A

Lysosomes

Proteosomes

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27
Q

Actin Assembly

A

Growth mostly occurs at plus end
Depolymerization mostly occurs at minus end
Requires ATP and forms a helix structure

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28
Q

Microtubule Assembly

A 
Plus end goes to periphery
Minus end is attached to centrosome
GTP cap- Growth occurs
No GTP cap- Depolymerization occurs
13 protofilaments join to form the tubule
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29
Q

Intermediate Filament Assembly

A

Not dynamic. Slow and Stable

Monomer–>Coiled Coil Dimer–>Anti-Parallel Tetramer–>8 of these form IF

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30
Q

EBS

A

Mutation in the keratin 5 an 14 genes

Causes the basal layer of skin to rip off

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31
Q

EH

A

Mutation in the keratin 1 and 10 genes

Causes the spinous and granular layer to rip off

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32
Q

EPPK

A

Mutation in the keratin 9 gene

Causes the cornified layer to rip off (keratinized layer)

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33
Q

Size of the Cytoskeleton Structures

A

Microfilaments: 6 nm
IF: 10 nm
Microtubules: 23 nm

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34
Q

Types of IF

A 
Vimentin (mesenchyme)
Glial (glia)
Keratin (epidermis)
Desmin (muscle)
Lamin (nucleus)
Neurofilaments (neurons)
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35
Q

Gamma Tubulin

A

Grows from the centrioles and stabilizes the minus end of microtubules

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36
Q

Proteins Associated with Actin

A

ARP 2 and 3: they form a dimer that bind to the minus end to help stabilize
Formin: forms a dimer and brings the filaments together
Profilin: binds to actin monomers and enhances the binding of ATP
Cofilin: shortens the distance between helices
Fimbrin: holds actin bundles close together and prevents myosin from binding
Filamin: stabilizes the actin meshwork formed by ARP

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37
Q

MAP2 vs Tau

A

MAP2 binds and allows for distance between MT
Tau binds and holds MTs close together
If Tau becomes hyperphosphorylated it will lead to tau tangles which cause CTEs

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38
Q

Apical Surface Specializations

A

Microvilli: made up of actin and used to increase absorbtion. Normally found on simple columnar
Cilia: long projections made out of MT that use ATP to move molecules
Sterocillia: abnormally long microvilli. Found in male RU

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39
Q

PCD

A

A disease where the cilia are immotile

Leads to respiratory infections and sterility

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40
Q

Basal End

A

Made up of Basal lamina and Basal membrane

Used to anchor epithelial and serves as a filter

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41
Q

Bullous Pemphigoid

A

An autoimmune disease where Abs attack the hemidesmosomes and lead to separation on the epithelium from the basement membrane

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42
Q

EMT

A

When the apical surface breaks down and creates mesenchymal cells. Can lead to cancers because it asymmetrical division of stem cells

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43
Q

Parts of the Lateral Side

A

Zonula Occludens: Tight junctions that link using actin
Zonula Adherens: Provide strength and resistance and link to actin
Desmosomes: use cadherins that link to the IFs of the cells in order to keep the cells held together
Gap Junctions: made out of connexon and allow small ions and molecules to freely diffuse from cell to cell

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44
Q

Pemphigus

A

An autoimmune disease where Abs attack desmogleins which lead to epithelial cells falling apart from each other

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45
Q

Goblet Cells

A

Unicellular glands that are found in the apical part. They secrete mucins

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46
Q

3 types of Secretion

A

Merocrine: exocytosis using membrane
Apocrine: When the apical part of cell gets excreted
Holocirne: the entire cell is lost in excretion

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47
Q

Types of Simple Epithelial

A

Squamous- capillaries, alveoli
Cuboidal- glands
Columanr- GI tract

48
Q

Types of Stratified Epithelial

A

Squamous- skin
Cuboidal- sweat ducts
Columnar- paratid gland
Transitional- bladder

49
Q

Where is psuedostratified found

A

In respiratory tract and male reproductive tract

50
Q

How does ligand binding affect protein folding

A

It alters the equilibrium by shifting it to the folded state because it limits the free space

51
Q

Protein-Ligand Binding Graph

A

In normal units it will be a curve

In log units it will be a sigmoidal shape

52
Q

How To Tell Affinities on P-L Graph

A

Lower affinities with be more to the right
Higher affinities will be more to the left
(This is for Kd, Ka will be the exact opposite)

53
Q

Allostery

A

When a protein has at least two binding sites that are different and bind to different ligands
Shifts the Kd of a ligand to either the left (enhancing) or right (inhibitory)

54
Q

Why do cells need allostery

A

REGULATION

55
Q

Cooperativity P-L Binding

A

When a protein has at least to binding sites that are identical and bind to the same ligand
Binding of one influences the binding of another
On a graph it is sigmoidal for both normal and log

56
Q

Advantages for Allosteric Drugs

A

They dont have to compete with the original ligand
More subtle affects
Expands the number of targets of specific proteins

57
Q

Benefits of Patient Centered Interviewing

A

Provides more accurate data
Increases patient and physician satisfaction
Better outcomes

58
Q

3 Core Therapeutic Behaviors

A

Respectfulness
Empathy
Genuineness

59
Q

4 Habits Model

A 
Invest in the beginning
Elicit the patient's perspective
Demonstrate empathy
Invest in the end
Everybody benefits if this is done
60
Q

4 Biomedical Ethics

A

Beneficence
Non Maleficence
Autonomy
Justice

61
Q

Deontological

A

Rule based reasoning

62
Q

Teleological

A

Values based reasoning

63
Q

Physician Patient Relationship

A

A professional, voluntary, moral, socially binding contract

64
Q

Abandonment vs Termination

A

Abandonment is when you leave the patient for no apparent cause without pointing them to a right direction
Termination occurs due to retirements, relocation, change in insurance, etc

65
Q

Evidence Based Medicine

A

Using research literature, along with you clinical expertise and patient information to make the best informed decision

66
Q

Incidence vs Prevalence

A

Incidence is the number of new cases in a period of time

Prevalence is the number of new and old cases in a population (point and period)

67
Q

Cumulative Incidence

A

Risk

New cases/Persons at risk

68
Q

Incidence Rate

A

Number of new cases/Total person-time observed

69
Q

Ways to Decrease Prevalence

A

Vaccines
People dying from disease
New treatments

70
Q

Mortality Rate

A

Number of deaths/Total person-time observed

71
Q

Case Fatality

A

Number of those who dying from disease/number of those who have contracted the disease

72
Q

What molecules can freely diffuse across membrane

A

Gasses
Small uncharged molecules
Water can slowly

73
Q

Protein Facilitated Diffusion

A

A protein helps a molecule move across membrane

Can become saturated whereas passive diffusion cant

74
Q

Types of Active Transport

A

Primary: Involves the hydrolysis of ATP
Secondary: Uses one molecule going with its gradient to drive another molecule going against its gradient (symport or antiport)

75
Q

Osmotic Pressure

A

When you move solute water will move with it to equalize the water:solute concentration
Hypertonic causes cell to shrink
Hypotonic causes cell to grow and maybe burst

76
Q

Pores

A

Both ends of the structure are always open and they allow large molecules to diffuse across
Only found in bacteria

77
Q

Channels

A

Both ends are open during activation but can be closed

They have a smaller pore size and can be specific

78
Q

Pump/Transporter

A

Only one end of the protein is open at a time

Requires energy and a conformational shape change

79
Q

GLUT1

A

Has a Km of 3-7

Found all throughout the body to help bring glucose into cells from the bloodstream

80
Q

GLUT2

A

Has a Km of 17

Found in the liver and small intestine to help bring sugar into the bloodstream and not out

81
Q

GLUT3

A

Has a Km of 1.4

Found in the brain and nerve cells so they can outcompete other tissues for glucose if need be

82
Q

GLUT4

A

Has a Km of 6
Found in fat, muscle, and heart cells and are normally inside the cells. Insulin and exercise brings them to the membranes

83
Q

SGLT Transporters

A

They use Na+ to bring glucose in from the lumen
SGLT1 has a very low Km
SGLT2 has a very high KM
Mutations in these lead to diarrhea

84
Q

Voltage K Channel

A

Specific so only dehydrated K can pass through
Hydrate K is too big to fit
Na is too small to form the proper interactions needed

85
Q

Na/K Pump

A

Uses ATP to pump 3 Na out of cell and 2 K into the cell

Important for maintaining the electrochemical gradient that drives cellular actions

86
Q

Types of ATPase Transporters

A

P Type: Used to transport ions
V Type: Used to transport H+ ions
ABC Superfamily: Used to pump peptides, drugs, and lipids

87
Q

ABC Transporters

A

Have 4 domains
2 nonconserved transmembrane
2 conserved nucleotide binding domains
Ligand binds. ATP binds and releases ligand into ECM. ATP gets hydrolyzed and protein returns back to normal

88
Q

Myoglobin

A

A single subunit with one domain that binds oxygen and stores it
Found in the muscle
Has a high affinity for oxygen

89
Q

Hemoglobin

A

A tetramer that has four binding sites for oxygen

It displays cooperative binding

90
Q

Deoxy vs Oxy State

A

Deoxy state has a lower affinity for oxygen

Oxy state has a higher affinity for oxygen

91
Q

2,3 BPG

A

Binds to the Deoxy state and helps facilitate the unloading of oxygen

92
Q

Effects of BPG, H+, and CO2 on HB Binding Curve

A

They are all allosteric inhibitors that weaken the affinity of O2 to make it easier to unload oxygen at active tissue

93
Q

Moonlighting of Hb

A

Binds and unloads oxygen
It can also bind to NO and convert it to NO3. This causes a rise in blood pressure
It can also bind to CO

94
Q

How CO Affects Hb

A

Once CO binds it changes the shape of the other three sites and locks them in the high affinity oxy state which means oxygen will not be unloaded

95
Q

Thalessemias

A

When a subunit of Hb is lost

Causes anemia

96
Q

Hemoglobinopathies

A

Point mutations in Hb

Sickle Cell Anemia

97
Q

Features of an Idea Hb Subsitute

A

The subunits are covalently attached
They can withstand high pressure
They are large and covered in PEG to prevent oxidation of NO

98
Q

Health

A

A state of physical, emotional, and spiritual well being

Allows you to live comfortably

99
Q

Public Health

A

What we do as a society to ensure and improve the health of its members

100
Q

Population Health

A

The trends and factors we observe associated with health

101
Q

Top 3 Causes of Death

A

Heart Disease
Cancer
Non health related deaths

102
Q

Goals of Healthy People 2020

A

To achieve health equity among people and to ensure high quality of life while minimizing disease and injury

103
Q

Determinants of Health

A 
Biology/Genetics
Behavior
Socioeconomic
Physical Environment
Access to Quality Care
104
Q

Immunoglobulins

A

Another word for Ab
The pre-emptive stike force against foregin substances
18% of total blood proteins

105
Q

Structure of Abs

A

They have two light chains and two heavy chains linked by S bonds
They are mostly built of beta sheets
They have two identical and independent binding sites

106
Q

Steps to Activating Insulin

A

Forms three S bonds
Cleaves the Leader Sequence
Cleaves the Connecting Sequence

107
Q

Insulin Monomer vs Insulin Hexamer

A

Monomer is active and only one subunit. It is used for quick release
Hexamer is inactive and held together by Zn. It is used for extended release

108
Q

Prions

A

Mutations in PrP proteins that cause misfolding of proteins to form amyloid plaques. Can be transmissible

109
Q

PKU

A

A genetic disorder of the enzyme responsible for lyasing Phe. This causes a build up of it which can be toxic

110
Q

Caposome

A

A modified drug used to treat PKU
Has a capsule that is resistant to the low pH in the stomach that stores the lyase inside
Phe can diffuse into it where it will get cut

111
Q

MDR Proteins

A

ABC transporter proteins that have been over expressed on cell membranes
They are characterized by having lots of hydrophobic residues that excrete the drug

112
Q

Characteristics of Membranes

A

About half lipid and half protein
Amphipathic
Sheet-like structures
Fluid

113
Q

Phospholipid Structure

A

2 Fatty Acids
Glycerol
Phosphate
Alcohol

114
Q

Importance of Cholesterol in Membranes

A

They maintain fluidity of them
In high temps they keep them from becoming too fluid
In low temps they keep them from freezing

115
Q

Types of Lipid Proteins

A

Integral
Peripheral (held by charges or ions)
Modular (extracellular proteins attached)

Foundations of Medicine (5 decks)

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