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FFM-1 Spring 2024 > Week 5 > Flashcards

Week 5 Flashcards

1
Q

4 Primary Ethical principles in medicine

A

1) Beneficience
2) Automony
3) Justice
4) Nonmalficence

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2
Q

What is meant by Beneficence?

A

Acting for the benefit of OTHERS

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3
Q

What is meant by Autonomy?

A

Respecting individual has the right to choose/refuse
Ability to make their own choices for their care

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4
Q

What is meant by Justice?

A

Fairness in terms of access and distribution of resources

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5
Q

What is meant by Non-maleficence?

A

DO NO HARM
Cause no unnecessary risks or needless harm to patients

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6
Q

Why is it important to develop a rapport with patients?

A

Relationship will determine QUALITY of info received and completeness of information

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7
Q

What are tenets of the Patient-centered clinical approach

A

Explore patient disease/illness experience
Understanding of WHOLE person not just the disease
Enhancing Doc/Patient relationship

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8
Q

Importance of confidentiality in healthcare?

A

Respect for patients and their privacy - don’t discuss them in public
Allows patients to discuss more sensitive topics with provider
Fosters sense of care-seeking - more willing to seek care
Prevent harm from coming to patients - lose jobs, etc.

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9
Q

Define a boundary in terms of patient-doctor relationship

A

Edge of appropriate, professional and clinical behavior

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10
Q

Why are boundaries a fine line?

A

Deciding what is considered exploitive or non-exploitive

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11
Q

What might be some instanced of boundary issues?

A

Treating family
Accepting gifts from patients
Provider ideology
Any sort of sexual conduct
Touch - necessary but ONLY WHEN necessary
Social gatherings - avoid on social media!

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12
Q

Referrals:
When to use?
When NOT to use?

A

1) ONLY if clear benefit to patient - if outside scope of practice of provider
2) NEVER to avoid death at facility (for statistical purposes)
3) If someone promises you charges/fee splitting - NOPE!

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13
Q

Ethical issues in patients refusing treatments?

A

When in doubt on treating a patient - autonomy wins out

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14
Q

Consent v. Assent

A

Consent: anyone over legal age of consent (>18yo)
Assent: more for minor to signal willingness to participate

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15
Q

Informed consent

A

Allowing patient to know all risks/benefits involved with refusal of care
Patient MUST posses proper decision making capacity in order to UNDERSTAND consequences
Consent must be obtained without coercion or manipulation

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16
Q

Define: population

A

Group of individuals who share common characteristic

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17
Q

Define: Sampling

A

Process of selecting subset group from a larger population for purpose of study

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18
Q

Define: sampling frame

A

List of individuals that are eligible for selection in research study

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19
Q

Pros to sampling frame

A

More confidence in generalized results of study as applied to a larger population

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20
Q

Sampling external validity

A

How well findings can be applied to other situations

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21
Q

Sampling Internal Validity

A

whether design, conduct, analysis of the study ITSELF answers the questions without bias

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22
Q

Subtypes of Sampling Categories:
1)
2)

A

1) Probability/Random Sampling
2) Non-probability/Nonrandom Sampling

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23
Q

Describe simple random sampling

A

Selection of individuals from population using random number generator

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24
Q

Describe Stratified random sampling

A

Divides population into SUBGROUPS based on certain characteristics
Random selection done of all subgroups

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25
Q

Describe Cluster sampling

A

Divides population into clusters (based on geography)
Randomly will select clusters to sample from

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26
Q

Describe Systematic sampling

A

Selection of every “n”th member of population at a randomized starting point

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27
Q

Describe Convenience sampling

A

Selection of individuals with easy access/willingness to participate in study

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28
Q

Describe Snowball sampling

A

Selection of few individuals from population
Those few individuals refer others who fit criteria as wel

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29
Q

Describe Purposive sampling

A

Selection of individuals who meet specific criteria FOR the study

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30
Q

Describe Quota sampling

A

Researcher has liberty to select sample based on THEIR strata
Two people cannot exist under 2 different conditions

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31
Q

Describe Self-selection

A

Specific type of people are more likely to participate in research study

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32
Q

Describe Non-response

A

Certain type of people more likely to refuse to participate in study

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33
Q

Define inclusion criteria:

A

Characteristics/features permitting someone to be eligible participant in study

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34
Q

Define exclusion criteria

A

Characteristics/features disqualifying someone from participation in research study

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35
Q

Principles of inclusion/exclusion criteria:
1)
2)
3)
4)

A

1) Relevance
2) Feasibility
3) Exclusivity
4) Representative

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36
Q

Importance for inclusion/exclusion criteria:
1)
2)
3)
4)

A

1) Enhance study validity
2) Reduce participation risk
3) Increase generalizability = include representative population
4) Facilitate feasibility

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37
Q

Define sampling error

A

Statistical error when analyst does NOT select sample representative or entire population of date

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38
Q

Types of sampling errors:
1)
2)
3)
4)

A

1) Population specific error - wrong population included for study
2) Sample frame error/coverage error - Wrong list of people to deal with
3) Selection error - Chose wrong sent of respondents
4) Non-response error - people didn’t show up or respond

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39
Q

Methods to deal with sampling errors

A

1) Choosing correct sample for study
2) Increase the sampling size
3) Ensure baseline characteristics of participants
4) Weighted sampling of participants

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40
Q

Non-sampling errors -

A

No matter what they cannot be fixed by increasing sampling size.
1) Systematic error - Selection bias
2) Chance
3) Confounding

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41
Q

Conditions of Informed Consent

A

FULL disclosure of information -
1) Procedures and purpose of study
2) Risk vs Benefits of study
3) Alternatives to research pool
4) Conditions of participation

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42
Q

What is meant by conditions of participation in informed consent?

A

Participants have right to refuse or leave study at any time without penalty
Contact info for questions concerning study, participants rights WITHIN study

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43
Q

Persons with limited decision making capacity

A

LEGALLY authorize someone to make decisions
Approach someone with intermittent incapacitation when lucid

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44
Q

Those considered part of the vulnerable population

A

Children
Pregnant women
Prisoners

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45
Q

Define coercion

A

Threats (either explicit or implicit)

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46
Q

Define undue influence

A

Excessive compensation

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47
Q

Historical Highpoints arising in medical research

A

Nuremburg Trials
Thalidomide
Tuskegee Syphilis study

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48
Q

Describe Primary Research

A

Research that has been collected BY researcher

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49
Q

Describe Applied Research

A

Use of either animal testing or cell cultures to test

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50
Q

Describe Theoretical Research

A

Usually used in test development

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51
Q

Describe Descriptive Research

A

Used in prognosis determination of certain diseases

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52
Q

Describe Interventional Research

A

Something is being tested for
Drug trials

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53
Q

Describe Epidemiological research

A

Research done at a much larger scale
Happening within a population

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54
Q

Describe Analytical Observational Studies
Cohort Studies:

A

Observation of people over time
Association of risk factors and outcomes

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55
Q

Describe Analytical Observational Studies
Case Control Studies

A

Comparison of one group to control group
Association of risk factors vs rare outcomes

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56
Q

Describe Analytical Observational Studies
Cross-sectional Studies

A

Take a group of people, gather average amount of information
Prevalence of diease!

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57
Q

Describe Analytical Interventional Studies (with RCT’s)

A

Doing research at a larger level
Exploration of cause/effect of something

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58
Q

Define Secondary Research

A

Using data collected via other people for own research purposes

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59
Q

Describe Reviews

A

Cochrane Library
Used to find reviews of medical literature for average layperson

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60
Q

Describe Meta-analyses

A

Statistical combo of various studies wo come up with overall result for studies in certain area

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61
Q

Describe Databases

A

Collection of data to be used for research purposes

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62
Q

Describe Scientific Method

A

Ask
Hypothesis
Gather
Analyze
Conclude
Recommend

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63
Q

Goals of Descriptive Research

A

Summation of characteristics of group

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64
Q

Goals Predictive Research

A

Forecast outcomes of something

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65
Q

Goals of Explanatory/Causality Inference Research

A

Establish causal link/mechanism

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66
Q

Types of Info from Research
Descriptive

A

Describe X and Y and how they relate to ones another

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67
Q

Types of Info from Research
Correlational

A

Is there a relationship between X and Y

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68
Q

Types of Info from Research
Experimental

A

Change in X will affect Y in what way?

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69
Q

Types of Info from Research
Literature Review

A

Look at all studies and find which conclusions work best for X and Y

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70
Q

Variables seen in research

A

Types of responses
Different levels observed

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71
Q

Describe Hypothesis testing

A

Formulation hypothesis based on question being asked

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72
Q

Null hypothesis

A

No difference in relationship

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73
Q

Alternate hypothesis

A

There is some difference

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74
Q

Two types of Alternate Hypotheses

A

One-sided: Directional relationship
Two Sided: Non directional; some impact occurs

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75
Q

Types of Errors

A

Type I
Type II

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76
Q

Explain Type I error

A

Rejection of the null hypothesis when it should have been accepted
Alpha error
Relationship demonstrated

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77
Q

Explain Type II Error

A

Failure to reject the null hypothesis - should have and didn’t
Beta error
No relationship demonstrated

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78
Q

Describe Case Study
Advantages?
Disadvantages?

A

Study of one patient/case
Advantage: Observe someone with unusual circumstances
Disadvantage:

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79
Q

Define power

A

Probability of NOT making a Type II error
Probability of finding a difference between groups IF one exists

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80
Q

Describe Observation
Advantages?
Disadvantages?

A

Real-life observations of patients/case
Advantage: Real-life, real-time
Disadvantage:

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81
Q

Describe Surveys
Advantages?
Disadvantages?

A

Written/oral questionnaires
Advantage: Quick, cheap, familiar
Disadvantage:

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82
Q

Describe Archival research
Advantages?
Disadvantages?

A

Using existing records/databases
Advantage: cheap, data exists already
Disadvantage: Data quality not great

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83
Q

Describe Interviews
Advantages?
Disadvantages?

A

Interview of someone
Advantage: In-depth understanding/explanation of phenomenon
Disadvantage:

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84
Q

Describe Experiments
Advantages?
Disadvantages?

A

Cause and effect
Advantage: Causality
Disadvantage: Ethical considerations

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85
Q

Calculation of power of study

A

1- beta

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86
Q

Ways/means to increase power in study

A

Increase sample size
Have marked differences between groups
Lower SD

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87
Q

Define p-value

A

How much of observed data disagrees with null hypothesis
Greater the difference = lower the p-value

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88
Q

Low p-value

A

Reject null hypothesis

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89
Q

High p-value

A

Failure to reject the null hypothesis

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90
Q

Alpha level

A

Probability of making Type I error
If less than 5% = statistically significant

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91
Q

Bias

A

Systematic error in collection/interpretation of data found in study design

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92
Q

Hierarchy of Evidence Pyramid

A
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93
Q

Stages of Mitotic Cell Division and What Occurs There:
G1

A

All Cellular contents (except DNA) replicate
Preparation of Replication proteins ramps up

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94
Q

Stages of Mitotic Cell Division and What Occurs There:
S

A

DNA replication occurs

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95
Q

Stages of Mitotic Cell Division and What Occurs There:
G2

A

More of a checkpoint to ensure everything is good before mitosis
Production of proteins to aid mitosis occurs here

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96
Q

Stages of Mitotic Cell Division and What Occurs There:
Prophase

A

Chromosomes condense
Nuclear envelope begins to disappear
Mitotic spindle assembles

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97
Q

Stages of Mitotic Cell Division and What Occurs There:
Prometaphase

A

Nuclear envelope is gone completely
Chromosomes attach to microtubules via kinetochores

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98
Q

Stages of Mitotic Cell Division and What Occurs There:
Metaphase

A

Chromosomes align along equator
Sister chromatids attached to opposite poles of mitotic spindle

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99
Q

Stages of Mitotic Cell Division and What Occurs There:
Anaphase

A

Chromatids pulled apart
Chromatids are slowly pulled to opposite poles of cell

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100
Q

Stages of Mitotic Cell Division and What Occurs There:
Telophase

A

Chromosomes arrive at opposite pole
Nuclear envelope begins to reappear
Contractile ring of myosin/actin begins to form and contract

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101
Q

Stages of Mitotic Cell Division and What Occurs There:
Cytokinesis

A

Contractile ring continues to contract until 2 new cells formed

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102
Q

Mitosos:

A

Produce 2 ID cells
Each cell has 46 chromosomes (2n)
1 S phase, 1 division phase

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103
Q

Meiosis

A

Produce 4 different cells
Each cell has 23 chromosomes within it
1 S phase, 2 divisions

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104
Q

DNA Content through different stages of Mitosis

A
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105
Q

DNA Content through different stages of Meiosis I

A
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106
Q

DNA Content through different stages of Meiosis II

A
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107
Q

Role of Actin Microfilaments in Mitosis

A

Actin with myosin form contractile ring

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108
Q

Role of Intermediate Filaments in Mitosis

A

Formation of nuclear lamina
Will dissolve due to phosphorylation of proteins

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109
Q

Role of Microtubules in Mitosis

A

Formation of mitotic spindle
Attach to kinetochores

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110
Q

Cohesions

A

Proteins that regulate separation of sister chromatids during cell division

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111
Q

Cohesions broken down via _________________ during what phase?

A

Separase enzyme
Anaphase

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112
Q

Condensins

A

Large proteins that play role in chromosomal assembly and segregation during mitosis/meiosis

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113
Q

If functionality of cohesiens/separase occurs - what is result?

A

Non-disjuction of the chromatids

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114
Q

Results of non-disjunction?

A

Trisomies or monosomies

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115
Q

When can non-disjunction occur

A

Anytime during mitosis, meiosis I or II

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116
Q

Mosaicism

A

Present of cells with differing contents within ONE person

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117
Q

Taxol and why Oncologists love it?

A

Halt spindle checkpoint between Metaphase and Anaphase
Causes minor alteration of spindle microtubules to engage apoptosis
Prevents out of control cancer cells from replicating - also prevents high traffic area cells from replicating as well.

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118
Q

Contact Inhibition

A

Where one cell meets up with another while replicating and says “Sorry neighbor, not trying to intrude on your space” and stops building their cell empire.

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119
Q

Possible origins of mitochondria

A

Aerobic cell that was engulfed by anaerobic cell

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120
Q

Special features of mitochondria

A

Own DNA and ribosomes
No need to send or receive vesicles - manufactures own items for self (can receive proteins from nucleus)

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121
Q

Structure of mitochondria

A

Membrane enclosed
0.5-1.0 micrometers in diameter
10 micrometers in length
Form ATP in ETC
Seen in greater numbers in active cells in body

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122
Q

Outer membrane function of Mitochondria

A

Contains Porins = form aqueous channels in membrane
Molecules up to 5000 daltons allowed to pass through
Needed for release of newly synthesized ATP

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123
Q

Inner membrane function of Mitochondria

A
  • Form folds known as cristae
  • Cristae used to increase surface area of inner membrane
  • Impermeably to ions - only allow molecules needed for ETC to pass thru
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124
Q

Transmembrane proteins of the Inner membrane of Mitochondria

A

Cytochrome C oxidase (Complex IV)
ATP Synthase
ADP/ATP Carriers (antiporters)

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125
Q

Mitochondrial Matrix function of Mitochondria

A

Mix of enzymes for various metabolic functions
Contains matrix granules
Contains several copies of mtDNA, tRNA and ribosomes

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126
Q

Function of Matrix granules

A

Storage of extra Ca2+

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127
Q

Metabolic processes that involve mitochondrial enzymes

A

1) Oxidation of pyruvate
2) Oxidation of FA’s
3) TCA Cycle

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128
Q

Structure of mtDNA (Mitochondrial DNA)

A

Circular dsDNA
NOT packaged by histones

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129
Q

mtDNA codes for how many genes?

A

37
13 proteins, 22 tRNA, 2 rRNA

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130
Q

Function of Mitochondrial Protein Targeting Sequence

A

Proteins tagged to be transported to mitochondria

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131
Q

Target sequence for tagging proteins for mitochondria

A

5-10 AA sequence

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132
Q

Where are these sequences translated at

A

Free Ribosomes within cytoplasm

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133
Q

What allows for transport of protein into matrix?

A

Mitochondrial Matrix Targeting Sequence

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134
Q

Transmembrane proteins involved with transportation

A

TOM (Translocase protein of Outer Matrix)
TIM (Translocase protein of Inner Matrix)

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135
Q

Inheritance of mitochondrial DNA

A

Maternal ONLY

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136
Q

Why only maternal inheritance of mtDNA?

A

Paternal mitochondria is tagged with ubiquitin to be degraded by proteosomes

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137
Q

What is Oxidative Phosphorylation

A

Breakdown of food molecules into ATP using O2 as final acceptor molecule

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138
Q

Why is Carbon Monoxide so dangerous for OxPhos?

A

Will bind to heme moiety in Complex IV and inhibit respiration and ATP formation

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139
Q

What other areas does Mitochondria participate in?

A

Apoptosis
Steroidogenesis (seen as tubular structures called tubular cristae)
Thermogenesis

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140
Q

Structure of Peroxisomes

A

Spherical organelles
Enclosed via SINGLE membrane
Contain NO DNA
Can contain up to 37 different enzymes (peroxins)

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141
Q

Peroxin proteins are encoded by?

A

PEX genes

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142
Q

How to peroxisomes appear on TEM

A

Electron dense area

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143
Q

Formation of peroxisomes:
2 ways

A

Fission
De Novo synthesis

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144
Q

Describe Fission formation of peroxisomes

A

Pre-existing peroxisome divided in 2
Slower process for formation

145
Q

Describe de novo synthesis of peroxisomes

A

Pre-peroxisome vesicle buds off sER
Will contain specific proteins that will import PTS-containing proteins
Become functional peroxisome

146
Q

Functions of Peroxisomes:
Breakdown of VLCFA’s

A

Done via beta-oxidation of FA’s
VLCFA undergo initial oxidation in peroxisomes
Oxidation in peroxisomes NOT COUPLED to ATP production
Yields H2O2

147
Q

Functions of Peroxisomes:
Breakdown of H2O2

A

H2O2 accumulates in cell
H2O2 is harmful ROS
Catalase will breakdown H2O2 into H2O and O2

148
Q

Functions of Peroxisomes:
Formation of Bile Acids

A

Formed in LIVER ONLY
Formed from cholesterol from sER
H2O2 used to convert cholesterol into bile acids

149
Q

Function of Bile Acids

A

Emulsify gastric contents into substances that can be absorbed

150
Q

Functions of Peroxisomes:
Detoxification

A

Rid body of toxins
Number of peroxisomes in liver/kidneys is usually high because of this

151
Q

Functions of Peroxisomes:
Formation of myelin

A

Myelin - lipid/protein sheath surrounding nerve
Seen in CNS/PNS
Formation of special phopholipid = plasmologen

152
Q

Zellwegers Syndrome

A

Affects plasmologen synthesis in peroxisomes
Mutation of receptors of Peroxisomal Targeting Signal
Patients cannot import proteins into peroxisomes

153
Q

Adrenoleukodystrophy (ADL)

A

Mutation in member of ATP-binding cassette transporter family of proteins (ABCD1)
Breakdown/loss of myelin; progressive loss of function of adrenal glands
Inability of peroxisomes to import VLCFA’s inside - VLCFA’s will accumulate in serum

154
Q

Concerning metabolism, what occurs during hypoxia?

A

Glycolysis increases
TCA/OxPhos decreased
Lactic Acid begins to form and accumulate
Increased concentrations of NADH

155
Q

What is hypoxia-inducible factor?

A

Under hypoxic conditions, will begin to transcribe proteins needed to increase O2 flow to areas under hypoxic stress

156
Q

Under normal conditions - what is function of hypoxic inducible factor?

A

Usually Hydroxylated via HIF-prolyl hydroxylase - not active
Tags it with ubiquitin for degradation in proteosome

157
Q

Enzyme preventing activation of HIF?

A

HIF-prolyl hydroxylase

158
Q

Mutations in mtDNA - classified as?

A

1) Homoplasmic - seen in all mtDNA
2) Heteroplasmic - seen in some mtDNA, not in others

159
Q

Effects of Hypoxia:
1)
2)
3)
4)
5)
6)

A

1) Loss of ATP generation
2) Failure of ion pumps - build up of oxidative stress
3) Glycolysis ramped up
4) Formation and accumulation of lactic acid - tissues become acidic
5) Membranes begin to leak
6) Lysosomal enzymes become active

160
Q

Type of free radicals

A

Superoxide
Hydrogen Peroxide
Hydroxyl radical

161
Q

Describe superoxide radical

A

Reactive but not the worst
Cannot cross membrane due to charge (anion)
Converted to H2O2 by Superoxide dismutase

162
Q

Enzyme that denatures superoxide radicals

A

Superoxide dismutase

163
Q

Describe Hydrogen peroxide radical

A

Conversion of Superoxide into H2O2
Can convert into a hydroxyl radical

164
Q

Enzyme that denatures H2O2

165
Q

Describe Hydroxyl radical

A

Can be catalyzed in blood by free iron within blood

166
Q

Enzyme that denatures hydroxyl radical

A

Glutathione peroxidase

167
Q

Other ways for ROS to collect extra electrons?

A

Stray electrons from ETC (Complex I, II, III)
Ionizing radation
Flavoproteins (Fava beans)
NADPH oxidase/xanthine oxidase

168
Q

What is the Haber-Weiss Rxn?

A

Equation showing how ferrous/ferric iron can catalyze formation of hydroxyl radial from H2O2

169
Q

Examples of non radical oxidants

A

Ozone
Singlet Oxygen
Hypochlorus acid
Peroxynitrite

170
Q

Examples of Free Radical Oxidants

A

Peroxyl
Alkoxyl
Hydroperoxyl
NO

171
Q

Effects of ROS on Proteins:

A

Oxidize Cysteine and Methionine
Disturb iron-sulfur centers of cysteine and methionine
Will break peptide bonds between proteins

172
Q

Effects of ROS on DNA:

A

Oxidation of nucleotide bases
Most common - 8-oxoguanine (removed via BER)
Will form double strand breaks in DNA

173
Q

Effects of ROS on Lipids:

A

Oxidation of POLYUNSATURATED FA’s
Usually caused by free radical propagation

174
Q

Do ROS oxidize saturated FA’s or monounsaturated FA’s

175
Q

Steps for Free radical propagation in FA’s

A

1) Peroxide reacts with polyunsaturated lipid = forms free radical
2) Free radical interacts with O2 = forms lipid peroxyl radical
3) Lipid peroxyl radical moves on to another molecule to do it’s thing = leaves behind peroxide lipid

176
Q

What vitamin breaks free radical propagation of lipids?

177
Q

Structure/Function of superoxide dismutase:

A

Will convert superoxide radical into H2O2
Is a manganese containing enzyme within the mitochondria
Contains zinc-copper if enzyme is present in cytoplasm

178
Q

Structure/Function of Catalase:

A

Destroys H2O2
Is a heme-containing enzyme that is widespread throughout all body fluids
(Greatest concentration found in peroxisomes)

179
Q

Structure/Function of glutathione peroxidase:

A

Destroys hydroxyl radical and hydrogen peroxide
Is present in cytoplasm and in mitochondria

180
Q

Reduced glutathione

181
Q

Oxidized Glutathione

182
Q

What does glutathione do?

A

Maintain redox state of cytoplasm

183
Q

Where is the reducing environment for glutathione?

184
Q

How is G-SH regenerated?

A

From GS-SH using NADPH reducing equivalents

185
Q

Where do NADPH reducing equivalents come from?

186
Q

Role of dietary antioxidants and ROS:

A

Roam around and scavenge free radicals
Will end up forming STABLE free radical that can do no other damage to cells
It will destroy other free radicals in the process

187
Q

Examples of Water Soluble antioxidants

A

Vit C
Uric acid
Phytochemicals

188
Q

Examples of Fat-soluble antioxidants

A

Vit E
Vit A
Reduced CoQ

189
Q

How does NADPH oxidase function in phagocytosis?

A

It is a plasma membrane bound enzyme specifically for making ROS
Used to kill phagocytosed bacteria in cells

190
Q

NRF2-KEAP1 system function?

A

Protection against oxidative stress

191
Q

Under oxidative stress, how does NRF2-KEAP1 function?

A

NRF: is a transcription factor; will stimulate transcription of antioxidant genes
KEAP1: Will bind to antioxidant response element on DNA

192
Q

Under normal conditions, how does NRF2-KEAP1 function:

A

NRF2 is kept within cytoplasm as the master regulator of cell redox state
NRF2 inevitably sent to proteosome via KEAP1 (senses oxidation within cells)

193
Q

Primary storage site of glycogen

A

Liver and Muscle cells

194
Q

Composition of glycogen:

A

alpha 1,4 chains of glucose
alpha 1.6 branches of glucose

195
Q

Storage of glycogen in liver:
Function of?

A

Maintain blood glucose levels during times of fasting/between meals

196
Q

How long does glycogen reserve in liver last for?

A

Approx 12 hrs

197
Q

Muscle glycogen:
Function of?

A

Direct source of glucose for muscles

198
Q

What enzyme do muscles lack for conversion of glucose?

A

Glucose-6-Phosphate

199
Q

When released from muscle, where does glucose go?

A

Remains in muscle

200
Q

What does glucagon stimulate?

A

Breakdown of glycolysis

201
Q

What does epinephrine signal in muscle cells?

A

Glycogen breakdown in muscle cells

202
Q

What is glycogen broken down into in muscle?

A

Glucose-1-phosphate

203
Q

What it glycogen broken down into in the liver?

A

Immediate glucose to be released and utilized by bloodstream

204
Q

Where does gluconeogenesis insert itself in glycolysis?

A

Glucose-6-Phosphate

205
Q

Excess glucose in blood triggers?

A

Insulin and GLUT4

206
Q

As glucose concentration increases, what will happen to hexokinase velocity?

A

Will increase sharply and become saturated in tissues OTHER than the liver

207
Q

As glucose concentration increases, what will happen to Glucokinase velocity?

A

Will increase steadily over time in the liver

208
Q

What are GLUT4 proteins

A

Transport proteins enabling glucose to enter muscle and adipose cells

209
Q

What enzyme interconverts glucose-1-phosphate into Glucose-6-phosphate?

A

Phosphoglucomutase

210
Q

What is glycogenin?

A

Protein core of glycogen that is surrounded by 10,000 molecules of glucose

211
Q

What enzyme adds glucose units to non-reducing ends of glycogenin?

A

Glycogen synthase

212
Q

What is the function of glycogenin?

A

Primer upon which other glucose molecules can attach to.

213
Q

How does glycogenin add glucose molecules to itself?

A

Will autocatalyze glucose molecules to self til certain point.

214
Q

What is the primary enzyme that allows glycogenin to add UDP-glucose to itself?

A

Glucosyltransferase

215
Q

Once sufficient moieties added to glycogenin, what enzyme takes over additon of UDP-glucose?

A

Glycogen synthase

216
Q

How often to brand points appear in glycogen molecules?

A

Every 8-10 glucose residues

217
Q

What enzyme transfers glucose molecules from main chain (1,4) to branch chain (1,6)?

A

Glycosyl 4:6 transferase
(Branching enzyme)

218
Q

What enzymes break down glycogen?

A

Alpha-amylase either in pancreas and salivary glands

219
Q

Why do glycogen synthesis and breakdown have different enzymes?

A

Allow for activation of ONE pathway at a time (one active, other inhibited)

220
Q

Breakdown of glycogen in liver:
Reason?

A

Regulate blood sugar

221
Q

Breakdown of glycogen in muscles:
Reason?

A

Provide substrate for ATP production

222
Q

Primary enzyme responsible for glycogen breakdown?

A

Glycogen phosphorylase

223
Q

How does Glycogen phosphorylase function?

A

Start with non-reducing ends and cleave alpha (1,4) bonds
Will cease when 4 glucose moieties left

224
Q

How are terminal 3 glucose molecules removed from branches?

A

Debranching enzyme
4:4 transferase and alpha (1,6) glucosidase

225
Q

Function of alpha 1,6 glucosidase?

A

Remove remaining single glucose at branching point

226
Q

Glycogen synthase stimulated via?

A

Increased G6P levels

227
Q

Glycogen phosphorylase inhibited by?

A

Increased energy levels (ATP)

228
Q

Glycogen phosphorylase activated by?

A

Activated by low-energy signals
Increased Ca2+ and AMP

229
Q

Signals activate glycogenolysis in liver and muscle?

A

Liver: Glucagon
Muscle: Epinephrine

230
Q

Mechanism of action of glycogenolysis?

A

Phosphorylating and activation of phosphoylase (via cAMP)

231
Q

Increased Ca2+ leads to in muscle?

A

Activation of phosphorylase kinase
Triggers activation of glycogen phosphorylase

232
Q

Increased AMP in muscle?

A

Can activate glycogen phosphorylase B

233
Q

Glycogen synthase:
Activated by?
Inhibited by?

A

Activated by: Insulin
Inhibited by: Glucagon/epinephrine via cAMP/PKA pathway

234
Q

Activation of glycogen synthase via:
1)
2)

A

1) Activation of phosphatase-1 (dephosphorylates glycogen synthase)
2) Activation of PKB (phosphorylates GSK-3; inactivates)

235
Q

Example of dietary lipids

A

Triglycerides
Cholesterol
Phospholipids
Fat-soluble vitamins (A, D, E, K)

236
Q

Detergents made from?

A

Cholesterols

237
Q

Where are detergents formed?

238
Q

Where do further modifications of detergents occur?

A

In GI tract

239
Q

Types of bonds that join -COOH end of FA to other molecules?

A

Ester bonds

240
Q

Types of detergents?

A

Cholate
Deoxycholate
MAG
Lyso-phosphotidylcholine

241
Q

One of the functions of detergents?

A

Provide access for lipases to cleave FA’s form TG’s, cholesterols, phospholipids

242
Q

How are FA’s removed from TG’s?

A

Via lipases in the intestines

243
Q

Which FA is cleaved in the intestines?

244
Q

Function of bile acids?

A

Emulsify insolubile TG’s and break them down to where intestines can absorb them

245
Q

FA’s that can penetrate the membrane and be readily absorbed?

A

Small FA’s
Short chain FA’s
Medium chain FA’s

246
Q

What is a chylomicron?

A

Lipoproteins that are TG rich
Contain specific apo-proteins to mediate uptake in liver and adipose tissue

247
Q

Function of chylomicrons?

A

Transport dietary lipids to destination

248
Q

TG’s sent to liver via chylomicrons are repackages into what?

249
Q

In terms of fat storage:
Insulin

A

Stimulates uptake of fat storage in adipose tissue

250
Q

How does insulin stimulate uptake of fat?
1)
2)
3)

A

1) Suppress FA release from existing FA’s
2) Acceleration of glycolysis (increased DHAP for TG synthesis)
3) Enhance lipoprotein lipase in adipose capillaries

251
Q

Role of Lipoprotein lipase

A

Digest TG’s into FFA’s and release those free fatty acids for uptake

252
Q

Regulation of Lipoprotein Lipase: Fed State
Adipose
Muscle

A

Upregulated in adipose tissue
Downregulated in muscle
Cardiac muscle has higher LPL than skeletal muscle

253
Q

Regulation of Lipoprotein Lipase: Fasted State
Adipose
Muscle

A

Upregulated in muscle via epinephrine
Downregulated in adipose tissue

254
Q

Where is Lipoprotein lipase found in body?

A

Endothelial cells of capillary walls (in lumen of capillaries)

254
Q

How is lipoprotein lipase anchored to endothelial walls?

A

Heparan sulfate

256
Q

Fatty Acid Synthesis:
Location?

257
Q

What product of glycolysis must be increased to form FA’s?

A

Acetyl CoA

258
Q

What is Acetyl-CoA combined with to form TG’s?

A

Glycerol Phosphate

259
Q

Define beta oxidation

A

Fatty acid degradation

260
Q

FA Substrate Formation:
Formed where?

A

Cytosol of cells

261
Q

FA Substrate Formation:
Acetyl CoA formed where?

A

Mitochondria

262
Q

FA Substrate Formation:
How is AceCoA moved BACK to cytosol?

A

Citrate/Pyruvate Shuttle

263
Q

Steps in Citrate/Pyruvate Shuttle
1)
2)
3)
4)
5)
6)

A

1) Pyruvate enters mitochondria
2) Pyruvate becomes oxaloacetate (first step of gluconeogenesis)
(via Pyruvate Carboxylase)
3) AceCoA formed and combines with Oxaloacetate = forms citrate
4) Citrate leave mitochondria - cleaved BACK to AceCoA
5) Reducing agents form Palmitoyl CoA
6) AceCoA used to synthesize Palmitate

264
Q

AceCoA is converted into?

A

Malonyl CoA

265
Q

What enzyme converts AceCoA into Malonyl CoA?

A

Acetyl CoA Carboxylase

266
Q

Acetyl CoA Carboxylase inhibited by?

A

Palmitoyl CoA

267
Q

Acetyl CoA Carboxylase activated by?

268
Q

Main enzyme to grow FA chain?

A

Fatty Acid synthase

269
Q

What is attached to FA chains to transport around during synthesis?

A

Phosphopantetheine

270
Q

Phosphopantetheine enzymatically bound to?

A

Acyl Carrier Protein (ACP) domain

271
Q

Pantothenic acid is which Vitamin?

A

Vitamin B5

272
Q

Fatty Acid Synthase typically makes?

A

Saturated FA’s

273
Q

Enzyme to introduce double bonds to make unsaturated FA’s

A

Desaturases

274
Q

Overall types of reactions in FA synthesis

A

Reduction
Dehydration
Reduction
Condensation
Translocation

275
Q

TG’s synthesized from?

276
Q

Where is glycerol phosphate made?

277
Q

What is glycerol derived from?

A

Breakdown of TG’s in chylomicrons and VLDL particles

278
Q

Glycerol used as precursor for which metabolic pathway?

A

Gluconeogenic pathways

280
Q

FA’s are released for usage by?

A

Hormone Sensitive Lipase

281
Q

Where does FA go once released from adipose tissue?

A

Binds to serum albumin in bloodstream for transport

282
Q

TG’s are converted to FA via?

A

Lipoprotein Lipase

283
Q

TAG turned into DAG by?

A

Adipose TriGlyceride Lipase

284
Q

Hormone Sensitive Lipase regulated by

A

Epinephrine
cAMP/PKA messaging

285
Q

Rate limiting enzyme of FA release

A

Hormone Sensitive Lipase

286
Q

MAG is further broken down by?

A

Monoglyceride Lipase

287
Q

FA release from adipose tissue is inhibited by?

288
Q

Increased TG breakdown via removal of insulin
1)
2)

A

1) Decrease rate of phosphate removal from HSL
2) Decreasing DHAP

289
Q

Importance of FFA’s being bound to albumin in serum?

A

Otherwise FFA’s insert themselves into membranes and disrupt/compromise membrane function

289
Q

How are FA’s brought into mitochondrial matrix of cells?

A

Carnitine shuttle

289
Q

Define β-oxidation

A

Breakdown of FA’s to AceCoA
Makes energy from fat reserves

290
Q

Which carnitine shuttle adds carnitine to FA?

A

Carnitine Palmitoyl Transferase I (CPT1)

291
Q

Which carnitine shuttle removes carnitine from FA?

A

Carnitine Palmitoyl Transferase II (CPT II)

292
Q

What inhibits Carnitine Shuttle?

A

Malonyl CoA

293
Q

Function of β-oxidation?

A

Use of FA directly for energy

294
Q

Fatty Acid CoA:
Broken down to
Via enzyme?

A

Enoyl CoA
Acyl CoA Dehydrogenase

295
Q

Enoyl CoA:
Broken down to
Via enzyme?

A

3-hydroxyacyl CoA
Enoyl CoA Hydratase

296
Q

3-Hydroxyacyl CoA:
Broken down to
Via enzyme?

A

3-Ketoacyl CoA
3-hydroxyacyl CoA dehydrogenase

297
Q

3-ketoacyl CoA:
Broken down to
Via enzyme?

A

Acetyl CoA
β-Ketoacyl-CoA thiolase
(exchange)

298
Q

How does acyl CoA dehydrogenase act?

A

Oxidizes double bond between 𝛼 and β carbons

299
Q

Result of Acyl CoA Dehydrogenase

A

Double bond formed
FADH2

300
Q

Variants of Acyl-CoA Dehydrogenase

A

VLC acyl-CoA Dehydrogenase
LC acyl-CoA Dehydrogenase
MC acyl-CoA Dehydrogenase
SC acyl-CoA Dehydrogenase

301
Q

Function of Enoyl CoA Hydratase

A

Hydrate across double bonds

302
Q

Function of 2-hydroxyacyl CoA Dehydrogenase

A

Oxidation of β-carbon hydroxyl

303
Q

β-Ketoacyl CoA Thiolase

A

Produces AceCoA

304
Q

Where are VLCFA’s initially broken down

A

Peroxisomes

305
Q

Enzyme that allows odd double bonds (odd chain FA’s) to be oxidized?

A

cis Δ3 enoyl CoA isomerase

306
Q

Function of cis Δ3 enoyl CoA isomerase?

A

Moves double bond in odd chain FA to 2-position

307
Q

Even chain FA’s - double bonds at even positions:
Enzymes that reduce double bonds

A

2,4 dienoyl-CoA Isomerase

308
Q

Function of 2,4 dienoyl-CoA Isomerase?

A

Reduce double bonds to one
Isomerase moves it into position to be handled by β-oxidation

309
Q

Regulation of Acetyl CoA Carboxylase

A

Activated by citrate
Inhibited by Palmitoyl CoA

310
Q

Function of Insulin in regulation of AceCoA Carboyxlase

A

Will activate it via protein phosphatase (removed phosphate from phosphorylated Carboxylase)

311
Q

Function of Glucagon and Epinephrine on regulation of AceCoA Carboxylase

A

Will activate AMPK Kinase - phosphorylates Carboxylase to inactivate it

312
Q

Function of AMP on regulation of AceCoA Carboxylase

A

Allosteric activator of AMP-activated protein kinase
Phosphorylates AceCoA Carboxylase

313
Q

Regulation of FA Synthesis/Oxidation via Malonyl CoA

A

Blocks Carnitine Shuttle in Mitochondria
Prevents LCFA from entering Mitochondrial Matrix

314
Q

FA Synthesis active

A

β-oxidation inhibited

315
Q

FA Synthesis inactive

A

β-oxidation active

316
Q

Acetyl CoA Carboxylase 1

A

Regulates FA Synthesis

317
Q

Acetyl CoA Carboxylase 2

A

Regulates β-oxidation

318
Q

NEFA

A

Non-Esterified FA’s

319
Q

Ketone bodies made in response to?

A

Long increase in FA’s for prolonged period of time

320
Q

Known Ketone bodies

A

3-Hydroxy butyrate
Acetoacetate

321
Q

Function of ketone bodies

A

Alternate way to move energy among organs during prolonged fast

322
Q

Ketone bodies formed?

323
Q

Amount of time for ketone bodies to fully ramped up for production in liver

324
Q

Rate limiting enzyme in Ketone body synthesis

A

HMG-CoA Synthase

325
Q

Formation of Ketone bodies

A

2 AceCoA condensed to make Acetoacetyl CoA
3rd molecule of AceCoA used to make 3-hydroxymethylglutaryl-CoA

326
Q

Formation of 3-hydroxymethylglutaryl CoA by which enzyme?

A

HMG-CoA synthase in mitochondria

327
Q

Enzyme to catalyze HMG-CoA to AceCoA and Acetoacetate

A

HMG-CoA Lyase

328
Q

Acetoacetate converted to?

A

Reduced to 3-Hydroxybutyrate

329
Q

When ketone bodies taken up in cells - what enzymes converts hydroxybutyrate and acetoacetate into Acetoacyl-CoA?

A

CoA transferase
Thiophorase

330
Q

In blood, acetoacetate forms?

331
Q

How is acetate in blood formed?

A

Spontaneous decarboxylation of acetoacetate

332
Q

Signs of high ketone body production in body

A

Sweet smell on breath

333
Q

Key enzymes of glycolysis

A

1) Hexokinase (muscle/other)/Glucokinase (liver pancreas)
2) PFK1
3) Pyruvate dehydrogenase

334
Q

Function of hexokinase

A

Phosphorylate glucose to G6P

335
Q

Function of phosphofructokinase-1

A

Phosphorylates Fructose-6-Phosphate to Fructose-1,6-Phosphate

336
Q

Function of Pyruvate kinase

A

Convert Phosphoenolpyruvate to Pyruvate

337
Q

Enzyme in glycolysis that controls flux of glucose through glycolysis

338
Q

Enzyme that maintains balance between glycolytic flux and other metabolic pathways

A

Pyruvate Kinase

339
Q

Define: Glycogenolysis

A

Glycogen breakdown into glucose

340
Q

Define: Gluconeogenesis

A

Synthesis of glucose in liver (and kidney)

341
Q

During fasting, what is primary source of energy

342
Q

RBC’s dependent on which metabolic pathway to funtion

A

Glycolysis - unable to function without it
No mitochondria = unable to undergo β-oxidation

343
Q

Possible fates of pyruvate

A

Lactate
Acetyl-CoA
Oxaloacetate
Ethanol
Alanine

344
Q

Function of TCA cycle

A

Breakdown acetate to CO2 for energy
Produce reducing equivalents (NADP or FADH2)

345
Q

Sources of AceCoA

A

Glycolysis
β-oxidation
Ketone bodies

346
Q

FA’s enter mitochondria for oxidation via

A

Carnitine Shuttle

347
Q

Vitamins needed for Pyruvate Dehydrogenase

A

Vit B1, B2, B3, B5

348
Q

Other cofactors needed for Pyruvate Dehydrogenase

A

Lipoic Acid

349
Q

If deficiencies in Vitamins, results on oxidative metabolism

A

Reduced OxPhos and reduced energy to cells

350
Q

Structure of CoA

A

Coenzyme A
Pantothenic Acid

351
Q

Enzymatic Activities of Pyruvate Dehydrogenase:
Decarboxylase

A

Pyruvate reacted with TPP
Loss of CO2

352
Q

Enzymatic Activities of Pyruvate Dehydrogenase:
Lipoaminde Reductase/Transacetylase

A

TPP donates bound hydroxyethyl to lipoyl moiety
Coenzyme A replaces sulfur for lipoyl sulfur = Reduced lipoyl/AceCoA

353
Q

Enzymatic Activities of Pyruvate Dehydrogenase:
Dihydro-lipoyl Dehydrogenase

354
Q

Cofactors needed for Pyruvate Dehydrogenase

A

Thiamine Pyrophosphate
Lipoic Acid
CoA
FAD/FADH2
NAD+/NADH

FFM-1 Spring 2024 (11 decks)

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