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Foundations of Medicine > FOM Week 2 > Flashcards

FOM Week 2 Flashcards

1
Q

Factors Affecting Observed Rxn Rates

A

Energy/Temperature
Encounters/Concentration
Orientation

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2
Q

Transient State

A

The beginning of a rxn

All reactants and products are being changed

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3
Q

Equilibrium

A

When the rate of the forward rxn equals the rate of the reverse rxn. Occurs at the end of a rxn
Cells are never in equilibrium

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4
Q

Steady State

A

Occurs at intermediate time points

It is when one part of the rxn/cell is constant while everything else is changing

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5
Q

Examples of Irreversible Rxns

A

When a product is a gas

Proteolysis (they diffuse away from each other)

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6
Q

Properties of Catalysts/Enzymes

A 
Lower the Ea to make rxns occur quicker
Specific for certain rxns
They are unchanged by the rxn
Do not alter G or equilibrium
Speed up both the forward and reverse rxn
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7
Q

Advantages of Enzymes

A

They increase the rate of rxns
They allow rxns to occur in gentle conditions
They can couple to drive non-spontaneous rxns by using the energy released from another rxn (hydrolysis of ATP)
They control the release of energy

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8
Q

What is included in the patient history interview

A 
CC
HPI
PMH
Meds
All
FH
SH
ROS
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9
Q

7 Characteristics of HPI

A 
Where is it
When did it start
How bad
What is it like
When does it happen
What helps
What else
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10
Q

IHELLP for SH

A 
Income
Housing
Education
Legal Status
Literacy
Personal Safety
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11
Q

Fdel508 Mutation

A

Causes CF

A Phe gets deleted and this slows down protein folding which causes it to get degraded

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12
Q

Symptoms of CF

A

Causes a thick mucus build up in respiratory system
Malnutrition
Sometimes sterility

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13
Q

Kalydeco

A 
A drug used to treat CF class 3
Will not work with Fdel508 because that is class 2
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14
Q

Pharmocogenetics

A

An individuals response to a drug may be different due to genetic differences

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15
Q

Peroxisome

A

Responsible for the metabolism of very long fatty acid chains through beta oxidation
Also responsible for the synthesis of plasmalogen

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16
Q

How are peroxisomes identified on EM

A

They have a crystalloid core in the center region

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17
Q

How are peroxisomes formed

A

Pre-perox proteins are made and then sent from the ER to fuse with other pre perox proteins or to join with existing peroxisomes. They then split in half

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18
Q

How are items transported into peroxisomes

A

The cargo gets tagged with PTS1 (c terminus) or PTS2 (n terminus)
The PTS protein then binds to PEX5 which will go into the peroxisome and then drop off the cargo
PEX5 then goes back into the cytosol and repeats

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19
Q

PPARs

A

Proteins that induce the transcription of pre perox proteins
They get very active when there are lots of FAs present in the cell or ECM
Skeletal muscle has lots of them. How exercise burns fat

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20
Q

X-ALD

A

An X linked disease
ALD is a transporter that allows FAs into the perox
The disease causes a build up of FAs
Treatment is diet plus Lorenzo’s oil

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21
Q

How are mitochondria identified on EM

A

They are long doubled membrane structures

Also by the cristae

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22
Q

Mitochondria Outer Membrane

A

It is very permeable and allows diffusion of many molecules
It causes the IM space to resemble the cytosol
Very important when it comes to lysosomes and oxidative phosphorylation

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23
Q

ATP Synthase

A

Is responsible for creating ATP through the H+ electrochemical gradient created by the ETC
Can also work backwards and pump H+ into the cytosol

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24
Q

Lysosomes

A

The recycling centers of the cells

Have a very low pH

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25
Q

How are lysosomes identified on EM

A

They are round and have lots of vesicles

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26
Q

How do lysosomes maintain their low pH

A

They have a V type ATPase that pumps H+ ions from the cytosol into the matrix (pH is around 5)

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27
Q

How are lysosome enzymes tagged for transport

A

A phosphototransferase places a P onto the oligosaccharide attached to the enzyme. This creates a M6P
Any enzyme tagged with M6P will bind to the trans golgi receptors and be shipped off to the lysosome
The receptor is then shipped back so it can be reused

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28
Q

I Cell Disease

A

Defective phosphototransferase so nothing gets tagged with M6P and the lysosomes cannot function

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29
Q

6 Classes of Enzymes

A

Oxidoreductase (involved in transfer of electrons)
Transferase (transfers functional groups)
Hydrolase (breas bonds by the addition of water)
Lyase (cleaves C-C, C-O, or C-N bonds w/o water)
Isomerase (rearrangement of atoms)
Ligase (forms C-C, C-O, or C-N bonds by ATP)

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30
Q

Oxidoreductase

A

Involved in transfer of electrons
Co enzymes involved are NADH, NADPH, FADH2
Common names are dehydrogenase, reductase, oxidase, peroxidase, CYP450

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31
Q

Transferase

A

Transfers functional groups

Common names are aminotransferase or kinase

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32
Q

Hydrolase

A

Breaks bonds by the addition of water

Common names are peptidase, esterase, protease, phosphatase, urease

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33
Q

Lyase

A

Cleaves C-C, C-O, C-N bonds
Common names are decarboxylase and aldolase
Enzymes that do the reverse are called synthases

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34
Q

Isomerase

A

Rearranges atoms

Common names are epimerase, racemase, and mutase

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35
Q

Ligase

A

Forms C-C, C-O, or C-N bonds by ATP

Common names are synthetases (not same as synthase)

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36
Q

CoFactors

A

Small metals that attach to the enzyme

Help to stabilize and also have a catalytic role

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37
Q

CoEnzymes

A

Vitamins that are essential for the enzyme to function

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38
Q 
What groups do each of these molecules carry:
ATP
NADH/NAD+
NADPH/NADP+
FADH2/FAD
A

Carries phosphate groups which are high energy
Shuttles electrons used for fuel
Shuttles electrons used for biosynthesis and redox rxns
Shuttles elctectrons used for fuel (more powerful than NADs and work as prosthetic groups)

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39
Q 
What groups do each of these molecules carry:
Coenzyme A
Biotin
Tetrahydrofolate
Adenosylmethionine
A

Acyl groups
CO2
1 C unit to another C or S
Methyl group to O or N

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40
Q

What groups do each of these molecules carry:
Pyridoxal Phosphate
Thiamine Pyrophosphate

A 
Amine groups (NH2/NH) for a.a metabolism
Aldehydes/ketones for decarboxylation
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41
Q

Cysteine Protease

A

Has an active SH residue
Ex are palpain and calpain
Inhibited when SH is modified (ex iodoacetamide)

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42
Q

Aspartate Protease

A

Active site requires a deprotonated Asp
Active at low pH
Ex are pepsin and HIV protease
Inhibited by pepstatin

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43
Q

Metalloprotease

A

Active site requires Zn or Co
Ca is sometimes needed for structure
Inhibited by EDTA which binds onto the Zn or Co

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44
Q

Serine Protease

A

Active site has a catalytic triad (Asp-His-Ser)
Threonine can substitute for Ser
Ex are trypsin, chymotrypsin, thrombin

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45
Q

Explain how the catalytic triad works

A

The OH on the serine attacks a carbonyl group forming a covalent intermediate
Water comes in to hydrolyze it and the enzyme goes back to normal

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46
Q

Assumptions of MM Equation

A

[Substrate]&raquo_space;»»» [Et]
The rxn is in steady state
Rxn is irreversible once product is made

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47
Q

What will the rate equation be at very high [substrate]

A

V = K3 x [Et} = Vmax

Because the enzyme will be at Vmax

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48
Q

Kcat

A

The turnover rate of an enzyme

Kcat = Vmax / [Et]

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49
Q

MM Equation

A

V = (Vmax x [S]) / (Km + [S])

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50
Q

Km

A

The substrate concentration that gives you 1/2 Vmax

Km= (K3 + K2) / K1

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51
Q

Ways to Change Km

A

Temp
pH
Salt
Mutations

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52
Q

Way to Change Vmax

A

Add more enzyme

Change the Kcat

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53
Q

Why is it important to measure at the right time when doing a glucose test

A

If you wait too long you will get an artificially high reading
If you dont wait long enough you will get an artificially low reading

54
Q

Types of Cell Adhesion Molecules

A

They are membrane spanning proteins that hold cells together and also are involved in cell signaling
They attach to the cytoskeleton using linker proteins
Integrins
Cadherins
Immunoglobulin

55
Q

Zonula Occludens

A

A very tight junction that wraps around the entire cell
Prevents transport of all material
Cholera has a toxin that disassembles this

56
Q

Proteins that Make Up the Zonula Occludens

A

Transmembrane linker proteins are Claudin, Occlaudin, and JAM-1
Plaque Proteins are ZO1, ZO2, ZO3
Filament it links to is actin

57
Q

Zonula Adherens

A

Their purpose it to hold the cells together by providing structure and shape
They wrap all the way around the cell

58
Q

Proteins that Make Up the Zonula Adherens

A

Transmembrane linker protein is cadherin
Plaque Proteins are alpha, beta, and gamma catenin, vinculin, and alpha actinin
Filament it links to is actin

59
Q

Desmosomes

A

Their purpose is to give the cell extra strength to withstand friction
They have very thick plaque proteins
Dont wrap around the cell. Instead have spot welds

60
Q

Proteins that Make Up the Desmosomes

A

Transmembrane linker protein is cadherin (desmoglein)
Plaque Proteins are plakoglobin (gamma catenin), desmoplankin, and plakophillin
Filament it links to is keratin (IF)

61
Q

Gap Junctions

A

They are used for cell communication
Allow the diffusion of all molecules less than 1400 daltons
They have no link to the cytoskeleton
They are made up of connexins which form a hemi-pore

62
Q

Hemidesmosome

A

A spot wield that links the epithelial to the BM

Autoimmune disease is called bullous pemphigoid

63
Q

Proteins that Make Up the HemiDesmosome

A

Transmembrane linker protein is integrin and BP 180
Plaque Proteins are plectin and BP230
Filament it links to is keratin (IF)

64
Q

Focal Adhesion

A

On the basal end of the epithelial

They are important for cell motility and signaling

65
Q

Proteins that Make Up the Focal Adhesions

A

Transmembrane linker protein is integrin
Plaque proteins are vinculin, alpha actinin, FAK, SRC Kinase, Ras, Raf, GRB2, and SoS
Filament it links to is actin

66
Q

3 Modifiable Determinant of Health

A

Socioeconomic environment
Physical Environment
Individual Behavior

67
Q

Effects of Distress

A

Has a negative affect on health and behavior in most cases

68
Q

Downward Drift Hypothesis

A

Mental disorders lead to reduced income and employment which in turn leads to more increased symptoms of mental disorders

69
Q

Fundamental Attribution Error

A

An automatic way of thinking

We blame others wrong doing on internal behavior while our wrong doing due to external influences

70
Q

Just World Hypothesis

A

People get what they deserve

71
Q

Factors that Effect a Persons Pysche

A 
Early trauma and stress
Relationships
Support
Mental Disorders
Behavior
72
Q

Biopsychosocial Perspective

A

Seeing patients as whole persons
Not blaming the patient for what is wrong
Identifying which of the three will most help improve the patients health

73
Q

Stages of Change

A
  1. Precontemplation
  2. Contemplation
  3. Preparation
  4. Action
  5. Maintenance
    Relapse happens about 7-8 times and brings you back to steps 1-4
74
Q

Etiology

A

The cause of a disease

75
Q

Pathogenesis

A

The sequence of cellular, biochemical, and molecular events that follow the exposure of cells or tissues to an injurious agent

76
Q

Morphological Change

A

Structural alterations in cells or tissues that are either characteristic of a disease or diagnostic of an etiologic process

77
Q

Central Dogma of Pathology

A

Molecular damage–> Cellular damage–> Tissue damage–> Organ damage–> Clinical symptoms

78
Q

VINDICATES

A 
Vascular
Infection/Idiopathic
Neoplasia
Drugs/Toxins
Inflammation
Congenital
Allergies/Auto immune
Trauma
Endocrine
Something else
79
Q

Hypertrophy

A

Increase in cell size
Due to increased protein and organelle synthesis
Caused when the tissue is overworked
Ex is systematic hypertension
Treated with diuretics and ACE inhibitors

80
Q

Hyperplasia

A

Increase in the cell number
Due to hormones and GFs
Ex is the breast and mammary glands during pregnancy

81
Q

Atrophy

A

Decrease in both cell size and cell number
Caused when there is a lack of food/oxygen or when tissue is not active and an increase in protein degradation by proteosomes
Ex is Atherosclerosis

82
Q

Metaplasia

A

When a differentiated cell type gets replaced by another cell type
Most common is columnar to squamous
Caused by a change in the stem cells below
Ex is Barret Esophagus

83
Q

Dysplasia

A

Disordered growth of cells
Commonly seen in squamous epithelial
Is pre-malignant and needs treatment

84
Q

Types of Loose CT

A

Aeriolar
Reticular
Adipose

85
Q

Types of Dense CT

A

Regular
Irregular
Elastic

86
Q

Types of Specialized CT

A

Bone (compact and spongy)
Blood
Cartilage (elastic and hyaline)

87
Q

Types of Resident Cells

A

Fibroblasts
Chondroblasts
Osteoblasts
Ondontoblasts

88
Q

Major Types of Collagen

A

Type 1 is found in skin and bone (most common)
Type 2 is found in cartilage
Type 3 is found in reticular fibers (liver, spleen, lymph nodes)
Type 4 is found in the basement membrane

89
Q

Assembly of Collagen

A

The alpha chain is inserted into the lumen of the ER and the predomain is removed
Three precursors will then assemble into pro collagen where the NC1 domains are still present
The Procollagen peptidase then cleaves the NC1 domains from the collagen. This happens in the extracellular domain
The collagen molecules are then linked together to form collagen fibrils by the activity of LOX
The collagen fibrils then join together to form a collagen fiber

90
Q

Ground Substance

A

The space between the loose CT

Is composed of water, proteoglycans, glycoproteins, and GAGs

91
Q

Elastic Fibers

A

Made out of elastin and fibrillin
They are stetchy and return to normal shape
Found in organs that need to be flexible

92
Q

Three Layers of BM

A 
Lamina rara/lucida (made up of laminin)
Lamina Densa (made up collagen 4)
Lamina reticularis (made up of collagen 3)
93
Q

Laminin

A

A protein secreted by the epithelial cells and binds to integrin on the basal side

94
Q

Entactin

A

Joins the laminin to the collagen 4 in the lamina densa region of the BM

95
Q

Proteoglycans

A

Bind to the laminin network and have sugars on them that hold signals to the underlying cell receptors

96
Q

Isozymes

A

Enzymes that have similar functions but discrete differences
A way of enzyme regulation
Drugs can target multiple isozymes

97
Q

COX1 and COX2

A

Inhibited by aspirin and ibuprofen

Inhibiting COX1 gives you the GI side effects

98
Q

Ways to Change Enzyme Concentration

A

Synthesis
Degradation
Compartmentalization

99
Q

Covalent Modifications to Enzymes

A

Phosphorylation (reversible)

Proteolysis (irreversible)

100
Q

ATCase

A

An enzyme resonsible for synthesis of pyramidines
Activated by ATP and GTP
Inhibited by CTP and UTP

101
Q

Ways to Regulate Enzymes

A 
Isozymes
Concentration
Covalent Modification
Cooperative/Allostery
Co-Factors Availability
Inhibition
102
Q

Cross Sectional Study

A

A prevalence study that involves analysis of two data sets

It is convenient and cheap

103
Q

Ecological Study

A

Monitoring data from cross sectional studies and placing them in populations or groups
Data is easily collected but gives rise to the ecological fallacy

104
Q

Case Control Study

A

Starting with people who have the disease and working backwards in order to find the risk factors/cause
Is cheap and quick but you cannot determine prevalence or incidence from it

105
Q

Cohort Study

A

Starting with people who are disease free and monitoring them when they are exposed to see who gets the disease
Costly and time consuming but gives you incidence

106
Q

Randomized Control Clinical Trials

A

Planned experiments that assess the efficacy of treatments by comparing those with the treatment to those in the control group

107
Q

Systematic Reviews

A

Combine and assess multiple studies in order to gain qualitative data
The most supported studies

108
Q

Use Aspirin and Ibuprofen to Explain Reversible and Irreversible Inhibition

A

Ibuprofen is reversible from COX and readily dissociates

Aspirin is irreversible because it doesnt let go of COX and outlasts the life of RBCs

109
Q

Categories of Irreversible Inhibitors

A

Drugs (penicillin)
Naturally occurring (serpins)
Heavy metals (mercury and lead)
Pathology (glycation of enzymes from diabetes)

110
Q

Lineweaver-Burke Plots

A

Originally created before computers because quantifying date from curved plots was difficult
X axis is 1/[S]
Y axis is 1/Vo
Slope is Km/Vmax

111
Q

How to Determine Km and Vmax from LB Plot

A

Where the line crosses x axis is 1/Km

Where the line crosses y axis is 1/Vmax

112
Q

Competitive Inhibition

A

When the inhibitor competes with the substrate for the active site
Enzyme can bind one OR the other
Raises the Km but no effect on the Vmax

113
Q

Non Competitive Inhibition

A

When the inhibitor allosterically binds to the enzyme or the ES complex and prevents the rxn from occuring
Lowers the Vmax but no effect on the Km

114
Q

Uncompetitive Inhibiton

A

Affects both the Km and Vmax

Causes the lines to be parallel on the plot

115
Q

AChase

A

Enzyme in the synapse that is responsible for hydrolyzing ACh so neurons arent always firing

116
Q

Inhibitors of AChase

A

Carbomates are reversible

Sarin and malathion are irreversible

117
Q

Myesthenia Gravis

A

A condition where the dendrites have too few of ACh receptors so the signals dont last long enough
Treat by adding carbomates to slow down degradation

118
Q

Metabolism

A

All the chemical rxns that occur in a cell in order to maintain life
They involve a series of enzymatic processes

119
Q

4 Building Blocks of Macromolecules

A

Sugars
Fatty Acids
Nucleotides
Amino Acids

120
Q

What is the preferred energy source for most cells

A

Fatty Acids

Not ATP

121
Q

Why is ATP the main currency of energy

A

It contains just the right amount of energy
It is stable
It is relatively small

122
Q

Anemia

A

A disease caused from a patient having too few of RBCs

123
Q

Erythrocytes

A

Red Blood Cells and are very short lived
They have no organelles and no nucleus
They are bio concave shape which is essential for flexibility

124
Q

4 Major Steps to Tissue Preparation

A

Fixation (kills the cell but retains their shape)
Dehydration (all fixation and tissue fluid is removed)
Embedding
Staining

125
Q

H&E Stain

A

The most common histological stain
H stains nuclei and ribosomes blue/purple
E stains collagen fibers red

126
Q

PAS Stain

A

Stains a magenta color

Useful for observing mucins and glycogen

127
Q

Trichrome Stain

A

Stains connective tissue a blue or green depending on the type used

128
Q

Giemsa Stain

A

Stains a dark purple

Useful for observing blood cells and bone marrow

129
Q

Toluldin Blue Stain

A

Stains mast cells a dark blue

130
Q

Osmium Staining

A

Stains lipid rich areas such as myelin a dark black

Is also used for EM

Foundations of Medicine (5 decks)

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