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Applied Medical Sciences > Test 1 Lecture 1 > Flashcards

Test 1 Lecture 1 Flashcards

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USMLE® Step 1 flashcards
1
Q

chemical reactions and enzymes that convert glucose to pyruvate (glycolysis) to ethanol and CO2 (frementation)

A

Phosphorylated sugars

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2
Q

What are coenzymes?

A

vitamin-derived cofactors

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3
Q

What are the types of coenzymes?

A

thiamine pyrophosphate, riboflavin, coenzyme A, coenzyme Q (lowers statins), cobamide coenzyme

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4
Q

What is the importance of biochem for healthcare?

A
  1. understanding and maintenance of health
  2. effective treatment of disease
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5
Q

all chemical processes that occur in an organism

A

metabolism

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6
Q

What are examples of metabolism?

A
  1. glucose homeostasis
  2. DNA replication, RNA splicing
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7
Q

glycolytic enzyme, glucose transporters, glycogen synthetases, disaccharidases, gluconeogenic enzymes

A

glucose homeostasis

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8
Q

What are the types of error that can occur in genetic metabolic processes?

A
  • gene deletion
  • frameshifts
  • sequence mutations
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9
Q

termed inborn errors of metabolism

A

inherited or congenital disorders that are due to a defective enzyme causing a disruption in a specific metabolic pathway, the way that DNA or the genes communicate

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10
Q

What is the central dogma?

A
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11
Q

What is sickle cell anemia

A
  • autosomal recessive homozygous
  • Glutamic acid codon (GAG) to a valine codon (GTG)
  • mutated gene is hemoglobin beta (HBB), located on chromosome 11
  • causes the body to produce a new hemoglobin HbS which behaves differently than HbA
  • Causes the cell to sickle
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12
Q

What is familial hypercholesterolemia?

A
  • very high levels of low- density lipoprotein (bad cholestrol)
  • common
  • mutation in the LDLR gene encodes LDL receptor protein which removes LDL from circulation
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13
Q

Who does Familial hypercholesterolemia affect?

A

-heterozygote (recessive) for LDLR gene can lead to cardiovascular disease by the age of 30 to 40
- Homozygotes ( dominant) causes severe cardiovascular disease in childhood may lead to heart attack or death by 30

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14
Q

unrestrained, uncontrolled growth of cells, failure of cell cycle control

A

cancer

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15
Q

What are the two kinds of genes that disturb the cell cycle when mutated?

A
  1. tumor-suppressor genes
  2. Proto-oncogenes
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16
Q

What are the tumor suppressor genes?

A

P53 protein
retinoblastoma susceptibility gene (first tumor suppressor identified)

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17
Q

protein that monitors integrity of DNA

A

p53 protein

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18
Q

If DNA is damaged what do enzymes and p53 do to the DNA?

A

-repair enzymes are stimulated
- if DNA damage is irreparable, p52 directs cell to kill itself

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19
Q

What must occur for the cancerous phenotype to develop?

A

both copies of the tumor-suppressor gene must lose function

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20
Q

_ is absent or damaged in many cancerous cells

A

p53

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21
Q

predisposes individuals for a rare form of cancer that affects the retina of the eye

A

Retinoblastoma susceptibility gene

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22
Q

normal cellular genes that become oncogenes when mutated

A

proto-oncogenes

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23
Q

What can oncogenes cause?

A

cancer

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24
Q

Proto-oncogenes can encode for?

A
  • receptors for growth factors
  • signal transduction proteins
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25
Q

Only one copy of a proto-oncogene is needed for?

A
  • mutation of cell no longer depending on growth factors
  • uncontrolled division
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26
Q

Diseases are manifestations of abnormailities in?

A

genes, proteins, chemical reactions, or biochemical processes

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27
Q

What are examples of biochemical processes involved in disease?

A

electrolyte imbalance, defective nutrient ingestion or absorption, hormonal imbalances, toxic chemicals or biologic agents, and DNA based genetic disorders

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28
Q

building substances (molecules)

A

anabolism

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29
Q

breaking substances (molecules)

A

catabolism

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30
Q

What serves as a catalyst to speed up anabolism and catabolsim?

A

enzymes

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31
Q

What are anabolic reactions?

A
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32
Q

What are catablic reactions?

A
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33
Q

predominant chemical component of living organisms

A

water

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34
Q

What are the physical properties of water?

A
  • excellent solvent or organic and inorganic molecules
  • electrically neutral (due to waters dipolar sructures and exceptional capacity for forming hyrogen bonds)
  • polar
  • multipurpose
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35
Q

What does hydrophilic ad hydrophobic mean?

A
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36
Q

any substance that dissociates in water to increase the (H+) and lower the pH

A

acid

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37
Q

What happens as acids get stronger?

A

the more hydrogen ions it produces and the lower its pH

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38
Q

substance that combines with H+ dissolved in water and thus lowers the H+

A

Base

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39
Q

What dissociates into hydroxide ions, extra proton (-) and hydrogen ions, proton donor (+)?

A

water

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40
Q

measures the concentration of hydroxine ions (protons) in a solution (acidity)

A

pH

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41
Q

What maintains the pH of extracellular fluid and to what pH?

A

bicarbonate and other buffers
7.35 to 7.45

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42
Q

Suspected disturbances of acid-base balance are verified by measuring what?

A

-pH of arterial blood
-CO2 content of venous blood

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43
Q

What causes acidosis?

A

pH of <7.35
diabetic ketosis and lactic acidosis

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44
Q

What causes alkalosis?

A

pH> 7.45
vomiting of acidic gastric contents

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45
Q

What is a carbonic anhydrases?

A
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46
Q

resist a change in pH following addition of strong acid or base

A

buffering

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47
Q

What does oxidative metabolism produce?

A

CO2, the anhydride of carbonic acid, which if not buffered would produce severe acidosis

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48
Q

Biologic maintenance of a constant pH involves buffering by?

A

phosphate, bicarbonate, proteins (which accept or release protons to resist a change in pH)

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49
Q

What are the arterial blood gas levels?

A
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50
Q

Which organs keep the acid base balance normal in the body?

A

lungs and kidneys

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51
Q

this measure how much oxygen your blood cells are carrying

A

oxygen saturation (O2Sat)

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52
Q

this measures the pressure of oxygen thats dissolved in your blood. it helps show how well oxygen moves from lungs to your bloodstream

A

partial pressure of oxygen (PaO2)

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53
Q

This measures the amount of carbon dioxide in your blood. it also shows how easily carbon dioxide can move out of your body

A

Partial pressure of carbon dioxide (PaCO2)

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54
Q

this measures the acidity of your blood

A

acid base balance (ph level)

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55
Q

PH<7.35, respiratory CO2 normal, bicarb low (<24mEq/L), split into anion and non anion gap

A

Metabolic acidosis

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56
Q

pH >7.45, respiratory CO2 normal, bicarb level high

A

Metabolic Alkalosis

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57
Q

pH <7.35, CO2 elevated >45, elevated HCO3
(bicarb)

A

Respiratory acidosis

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58
Q

pH >7.45, respiratory CO2 <35

A

Respiratory alkalosis

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59
Q

What is an example of respirtory alkalosis?

A

hyperventilation (blowing off CO2) due to fever, pain, or anxiety

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60
Q

What are the primary processes of ABG?

A
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61
Q

Wha are the steps to exaluating an ABG?

A

There are 5 steps

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62
Q

is primarily due to the loss of bicarbonate

A

Non-gap metabolic acidosis

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63
Q

What are examples of non-gap metabolic acidosis?

A
64
Q

What are the differentials for anion gap metabolic acidosis?

A

CAT MUDPILES

65
Q

What do these lab values show?

A

metabolic acidosis

66
Q

How many and what are the essential amino acids

A

there are 9 amino acids that human diet must include and can not be synthesized

67
Q

Where are free amino acids found?

A

flitered in the kidney form the arterial renal blood and traces of free amino acids in urine

68
Q

What are important components of amino acids?

A
69
Q

What are the three amino acid enantiomers?

A

-thalidomine
-warfarin
-ibuprofem

70
Q

contains teratogenic S-enantiomer in addition to the therapeutic (anti-morning sickness) R-enantiomer

A

Thalidomide

71
Q

The S-enantiomer is five times more potent than the R-enantiomer

A

Warfarin

72
Q

S-enantiomer three times more potent than the other

A

Ibuprofen

73
Q

Where does protein folding begin?

A

the polypeptide chein and continues after translation

74
Q

protein binding polypetides stabilize unfolded protein intermediates

A

molecular chaperones

75
Q

What do molecular chaperones do?

A

prevent aggregation and facilitates trafficking of newly formed proteins

76
Q

What are the diferent structures of proteins?

A
77
Q

Human genes are transcribed and translated to form?

A

proteins

78
Q

proteins with fewer than 50 amino acids

A

peptide

79
Q

proteins with more than 50 amino acids

A

polypeptide

80
Q

Proteins can be what 2 kinds of molecules?

A

structural or functional molecules

81
Q

What are structural molecules?

A
82
Q

What are functional molecules?

A
83
Q

Amino acids can be __ or ___

A

hydrophilic or hydrophobic

84
Q

the influence of hydrophilic and hydrophobic interactions on structure of protein

A

hydrophobic effect

85
Q

Where are hydrophobic and hydrophilic residues located?

A
86
Q

replacement of a hydrophobic by a hydrophilic amino acid or vice versa

A

missense mutation

87
Q

What are the two examples of missense mutations?

A
88
Q

stop codon that result in chain termination- severity depends on the extent of protein truncation

A

nonsense mutations

89
Q

contain chemically reactive sites termed catalytic subunits

A

enzymes

90
Q

what occurs in enzyme activation?

A
91
Q

What are the drugs that use cellular enzymes?

A
92
Q

What is allosteric inhibition and allosetric activation?

A
93
Q

Explain and catabolic enzyme reaction

A
94
Q

Explain the anabolic enzyme reaction

A
95
Q

Explain the feedback loop

A

It causes a stimulus to produce the enzyme but when there is enough enzymes it will inhibit the production so no more enzymes are produced.

96
Q

What is a rate limiting reaction?

A
97
Q

enzyme that acts as a proteases that is activated by the complement cascade

A

zymogen

98
Q

What do zymogens contain?

A
99
Q

What are the advantages to zymogen?

A

enzymes remain inactive until the appropriate tissues destinatin is reached

100
Q

Explain the Renin-Angiotensin system

A
101
Q

How do enzymes aid in diagnosis?

A
102
Q

How are enzymes used to diagnose MIs?

A
103
Q

sugars that cannot be hydrolyzed into simpler carbohydrates

A

monosaccharides

104
Q

What are Polyhydric alcohols?

A
105
Q

are condensation products of two monosaccharide units

A

disaccharides

106
Q

What are examples of disaccharides?

A

lactose, maltose, isomaltose, sucrose, and trehalose

107
Q

are condensation products of 3 to 20 monosaccarhides- indigestible ( act as soluble fiber, may help prevent constipation)

A

oligosaccharides

108
Q

> 10 sugars, starch molecules (rice, wheat), such as glycogen

A

plysaccharides

109
Q

Where is glycogen stored?

A

skeletal muscle so it is readily available source for glycolysis

110
Q

What is the breakdown of carbohydrates?

A
111
Q

responsible for transporting glucose and galactose by atp dependent active transport against and concentration gradient

A

sodium glucose co-transporter

112
Q

what are the downsides and plus sides to sodium-glucose co-transporter?

A
113
Q

What are the location and function of glucose transporters?

A
114
Q

What is the sodium-dependent unidirectional transporter?

A
115
Q

process of forming glycogen molecules from glucose in order to store it

A

glycogenesis

116
Q

The process of breakdown of glycogen to yield glucose residues. a breakdown of molecules to fuel (catabolic mechanism)

A

glycoogenolysis

117
Q

Provides glucose when dietary intake is insufficient or absent

A

gluconeogenesis

118
Q

This is the process of obtaining energy from glucose molecules. The process takes place in the cytosol. It is an oxygen-independent process and can occur in aerobic as well as non- aerobic conditions.

A

glycolysis

119
Q

What catalyzes the hydrolysis of glycogen to glucose

A

maltase

120
Q

Where and when does gluconeogenesis occur?

A

in the liver (hepatocytes) and celluarly in the cytoplasm, mitochondira, and ER
begins 8 hours after fastig begins

121
Q

What are the products of glycolysis?

A

2 ATP
2 NADH
2 Pyruvate

122
Q

a hormone produced during a period of fasting, made by the islets of langerhan, pancreatic alpha cells

A

glucagon

123
Q

What is the main mediatory of glycogen breakdown in skeletal muscle?

A

epinephrine

124
Q

What produces insulin?

A

Beta cells of the islets of langerhan in the pancreas

125
Q

Explain how insulin and glucagon affect the regulation of blood glucose?

A
126
Q

How does glycolysis affect muscle?

A
127
Q

What is the concentration of blood glucose?

A

4.5 and 5.5 mmol/L

128
Q

A sudden decrease in blood glucose in response to insulin overdose causes?

A

convulsions, because of the dependence of the brain on a supply of glucose

129
Q

What is insulin?

A
130
Q

secreted by the adrenal medulla as a result of stressful stimuli -”Fight or Flight” leads to glycogenolysis in liver and muscle – stimulates phosphorylase via generation of cAMP. Inhibits insulin, you need all the glucose you can get!

A

Epinephrine

131
Q

acts in response to hypoglycemia, stimulates glycogenolysis by activating glycogen phosphorylase (liver) – does not act in the muscle

A

glucagon

132
Q

What is diabetes mellitus?

A
133
Q

Explain DM type 1

A
134
Q

Explain DM Type 2

A
135
Q

What is the importance of lipids?

A
136
Q

loosely defined group of molecules with one main chemical characteristic, insoluble, hydrophobic

A

lipids

137
Q

What are the three types of lipids?

A
138
Q

What are the different types of fat?

A

4

139
Q

the major form of dietary lipid in fats and oils, whether derived from plants or animals

A

triacylglycerols (triglycerol)

140
Q

What are fatty acids classified as?

A

saturated (full of single bonds)
unsaturated (containing double or triple bonds)

141
Q

What is the difference between saturated and unsaturated?

A

unsaturated are essential fatty acids such as monunsaturated and polyunsaturated, found in plant oils
saturated are fatty acids are found in animal fats, may be elongated, can predisopse to vascular disease when consumed in excess

142
Q

process of adding hydrogen atoms to unsaturated fat to make it a solid

A

hydrogenation

143
Q

incomplete “partially” hydrogenation, bad for you

A

trans fat

144
Q

breakdown of lipids used to mobilize stored energy, usually occurs in fat adipocytes

A

lipolysis

145
Q

What is the most important regulatory hormone in lipolysis?

A

insulin

146
Q

lipoproteins transport lipids from the intestine as _ and from the liver as _

A

chylomicrons
very-low density lipoproteins

146
Q

lipid molecules orient with polar (hydrophilic) head toward water and nonpolar (hydrophobic) tails away from water

A

micelles

146
Q

What are the four major lipid classes?

A
147
Q

derived from intestinal absorption of triacylglycerol and
other lipids

A

chylomicrons

147
Q

derived from the liver for the export of triacylglycerol

A

VLDL

148
Q

essential for carrying lipids that keep the human body alive, including in those small vessels.

A

LDL

149
Q

involved in cholesterol transport
* absorbs cholesterol in the blood and carries it back to the liver.

A

HDL

150
Q

What is the predominant lipid in chylomicrons and VLDL?

A

Triaglycerol

151
Q

What are the predominant lipids in LDL and HDL?

A

cholestrol and phospholipid

152
Q

What are the two main etiolgies of lipids?

A
153
Q

What is alcohol and liver disease?

A

Applied Medical Sciences (3 decks)

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