Study Guide Flashcards
(164 cards)
1
Q
Physiology
A
This is the study of normal functioning of a living organism and its component parts, including all it chemical and physical processes.
2
Q
Pathophysiology
A
the study of body functions in a disease state
3
Q
Mechanistic Approach
A
this kind of explanation of a physiological process focuses on “how” it occurs, or the mechanism by which it occurs.
4
Q
Teleological Approach
A
this kind of approach to physiology focuses on “why” a process exists, or what is its adaptive significance for the organism.
5
Q
if you were to talk about blood flow in terms a way to get oxygen and nutrients to body cells and remove waster would be this kind of approach to physiology
A
teleological approach
6
Q
if you explained blood flow as resulting from rhythmic contractions of the heart’s ventricles that create a pressure differential in blood vessels, then you would be using what kind of approach to physiology?
A
mechanistic approach
7
Q
Homeostasis
A
the ability to keep one’s internal environment relatively stable, despite an ever changing external environment.
8
Q
Law of mass balance
A
say that if the amount of a substance in the body is to remain constant, any gain must by offset by an equal loss.
9
Q
equilibrium(state of)
A
when the molecular composition of two body or cellular compartments is identical
10
Q
disequilibrium(and an ex.)
A
is when sometimes the concentration of molecules or ions is very different in one compartment versus an adjacent one. For example sodium is much more concentrated outside cells than inside.
11
Q
setpoint
A
the optimal value for a physiological parameter or variable
12
Q
hypothesis
A
this is a logical guess about how events will take place in an experiment.
13
Q
independent variable
A
this is a factor in an experiment that the scientist actually manipulates.
14
Q
dependent variable
A
this is a factor in an experiment that is observed or measured.
15
Q
control group(or sample)
A
this part of an experiment is included so that the scientist can be confident that any observed changes were due to the experimental manipulation, and not some outside factor.
16
Q
Arrows
A
Indicate associations in maps between terms or phrases
17
Q
explanatory phrases
A
connections between two terms are labeled with explanatory phrases to indicate more specifically how they are associated.
18
Q
Structure/function map
A
is a kind of concept map that shows the relationship between different vocabulary terms, usually from general to specific in a top-to-bottom progression.
19
Q
Be able to draw a feedback loop in the specific format shown in the Chapter 1 lecture. Do you know the definition of each component (stimulus, sensor, etc.)? Could you identify each component in a physiological scenario given on an exam?
Much more on this later in the course!
A
stimulus- any physiological change that deviates from the body’s preferred setpoint, ex. change in blood pressure
sensor- the structure the specifically detects the change from the setpoint, ex. chemoreceptors
integrating center- the anatomical location/structure where the information from the sensor is interpreted or compared to a stored setpoint, receieves info. from afferent pathway, ex. individual cells or proteins
effector- the specific anatomical structure that can counteract the stimulus and return the affected body parameter to its setpoint, cued into action by efferent pathway, ex. individual proteins, organelles
effector’s action- the the effector does to restore homeostasis, ex. sweat gland secretion of sweat
response- the outcome of the effector’s action, in negative feedback look the outcome is opposite of stimulus, in positive feedback the respone pushes stimulus further from the setpoint.(requres outside force to stop)
20
Q
describe the steps of the scientific method and understand basic experimental design (control group/sample,
experimental group/sample, dependent variable, independent variable, etc.).
A
- make an observation
- ask a question
- form a hypothesis, or testable explanation
- make a prediction based on the hypothesis
- Test the prediction
- record results and formulate theories and test again
Independent variable- is the factor manipulated by the investigator
dependent variable- the observed factor
control group-help to ensure that observed changes are due to the experimental manipulation and not to some outside factor.
21
Q
process map(or flow chart)
A
is another kind of concept map that links events or structures in a cascade that occur in a specific temporal sequence.
22
Q
Stimulus
A
is a change in a regulated variable or physiological parameter that is outside of its desirable range.
23
Q
Be able to identify and explain the function of all cellular features and organelles discussed in the Chapter 3 lecture.
Motor proteins
proteasomes
A
motor proteins- proteins move organelles around the cell using the cytoskeleton
proteasomes- enzyme that breaks down proteins
24
Q
- nucleus
- cytoskeleton
- mitochondria
- Rough ER-
- Smooth ER-
- Golgi Complex-
- Cytoplasmic vesicles-
- Ribosomes-
A
- nucleus- houses the genetic material of the cell
- cytoskeleton- gives cell structure and enables membrane movement
- mitochondria- site of aerobic respiration
- Rough ER- post translational modification of proteins
- Smooth ER- synthesis of lipids
- Golgi Complex- packaging and transport of proteins
- Cytoplasmic vesicles- filled with molecules for secreation or storage
- Ribosomes- synthesis of proteins
25
sensor
monitors that level of the variable in the previous question or detects changes in its level.
26
Understand the four metabolic pathways of the cell discussed in the Chapter 4 lecture. Which ones are aerobic or anaerobic? Where does each take place in the cell? What are the substrates and what are the products of each pathway? What is the rate-limiting enzyme of each pathway?
2 anaerobic systems are ATP-CP system and Glycolysis both happen in cytosol,
ATP-CP system- substrates are creatine phosphate (phosphocreatine), products are ATP and Creatine, rate limiting enzyme is creatine kinase, time to fatigue 10-15 seconds
Glycolysis- primary substrate is glucose, products are 2 ATP(net), 2 Pyruvate, 2 NADH, rate limiting enzyme phosphfructokinase, time to fatigue 60 to 90 seconds
2 aerobic systems are Citric Acid Cycle and Electron Transport System both take place in mitchondria of cells,
Citric acid cycle- primary substrate is acetyl CoA, products per round 1 ATP, 1 CO2, 1 FADH2, 3 NADH, rate limiting enzyme isocitrate dehydrogenase, time to fatigue a few hours.
electron transport system- cashes in NAD for 2.5 ATP each and FADfor 1.5 ATP each, products are 6 water molecues per glucose made and 26-28 ATP, primary substrates hydrogen ions and high energy electrons dropped off by FADH and NADH, rate limiting enzyme cytochrome oxidase, time to fatigue hours
27
Know the specific names of reactions that create complex carbohydrates or triglycerides? What reactions break down these biomolecules? What reactions convert biomolecules other than glucose into fuels/substrates for the cellular metabolic cycles?
gluconeogenesis-amino acids and lactic acids to glucose
glycogenesis- glucose to glycogen
glycogenolysis- breaksdown glycogen energy storage molecules to glucose,
proteolysis- breaksdown proteins into amino acids
protein synthesis- amino acids to proteins
lipolysis- triglycerides to fatty acids
lipogenesis- fatty acids to triglycerides
What reactions convert biomolecules other than glucose into fuels/substrates for the cellular metabolic cycles? beta oxidation and deanimation
28
integrating center
information about a physiological parameter is sent to an integrating center which evaluates the information relative to a preferred setpoint.
29
afferent pathway(also called input signal)
information coming into an integration center
30
If oxygen is available what is pyruvate(pyruvic acid) converted into? and then what happens?
Acetyl CoA, which then enters the Citric Acid Cycle, or Krebs cycle
31
efferent pathway(output signal)
information that is transmitted away from an integrating center.
32
Understand the difference between the mechanistic and teleological perspective when studying physiology.
Mechanistic perspecitve of physiology is
1. "how" a system work
2. What are the steps of a physiological process to accomplish a goal.
Teleological perspective of physiology is
1. "why" a system exists
2. What survival benefits does it help with? example why does heart rate increase during exercise? To pump more blood to muscles
33
Know the function of each subatomic particle, how ions are formed, the different types of chemical bonds, and different functional groups important to physiology.
electrons- play 4 important roles in physiology
1. covalent bonds- electrons shared between atoms form strong covalent bonds
2. Ions- if an atom or molecule gains or loses one or more electron, it acquires a charge and become an ion.( ions are basis for electrical signaling in the body)
3. High energy electrons- electrons in certain atoms can capture energy from their environment and transfer it to other atoms.
4. Free Radicals- unstable molecules with an unpaired electron. The contribute to aging, certain diseases,
Ions- are formed when an atom or molecule gains or loses one or more electron, acquiring an electrical charge.
covalent bonds-share electrons, one electron from each atom, strong bonds requre input of energy to break apart,
Polar and non polar molecules- polar molecules share electrons unevenly making atoms with a slightly more negative and slightly more positive charge, nonpolar molecules are distributed so evenly that there are no regions of partial positive or negative charge.
Ionic bonds- are the result of taking an electron, held together by electrostatic forces, negative charge ions are anions and positive charge ions are cations.
hydrogen bond- weak attractive bond between hydrogen and nearby oxygen, fluorine, or nitrogen atom.
van der waals forces- weak non specific attractions between the nucleus of any atom and the electrons of nearby atoms.
Main functional groups are amino, carboxyl, hydroxyl, phosphate.
amino NH2- signature of amino acids
carboxyl COOH-
hydroxyl OH-added and removed as a group in may biological molecules
phosphate- important role in many cellular processes, energy transfer, protein regulation
34
effector
this is a physiological structure(such as a sweat gland, or the diaphragm muscle) that has the ability to make a change in the body condition.
35
effector's action
this is the term we will use for what a structure like a sweat gland or the diaphragm muscle actually DOES(like secretes sweat, or contracts)
36
Define homeostasis, discuss generally how the body maintains it, and understand the consequences of not maintaining homeostasis.
Homeostasis is the body's ability to maintain a stable internal environment despite changes inside or outside the body, the body maintains homeostasis by adapting to changing environmental demands(additions must equal subtractions and vice versa law of mass balance), organ systems work synergistically to maintain constancy throughout the body, at the cellular level homeostasis is maintained by exchanges between the intracellular fluid and extracellular fluid. (3 steps: change in internal conditions, attempt to reestablish, succeeds= wellness, failure= disease. the consequences of not maintaining homeostasis are health deficits and even death.
37
response
this change brings the stimulus back toward its desirable range through a feedback loop.
38
Protons
subatomic particles with a positive charge
39
electrons
subatomic particles with a negative charge
40
Be able to differentiate between the four basic types of biomolecules discussed in the Chapter 2 lecture. What are the monomer and polymer forms of each? What are their typical functions in the human body?
carbohydrates- most abundant, mostly used to make ATP, monomer-monosaccharides =glucose, polymer- polysaccharides= glycogen, or starch in plans
lipids- can serve as an energy source, structural component of cells, or as signal molecules, nonpolar(do not dissolve in water), monomer= fatty acids(saturated or unsaturated), polymer= mostly triglycerides(formed with glycerol and monomer) 3 types phospholipids, eicosanoids, steroid hormones
nucleotides/ nucleic acids- composed of nitrogenous base, a sugar, and a phosphate group, adenine, thymine(DNA only), guanine, cytosine, uracil(RNA only); polymer form is DNA and RNA, functions for energy transfer and signaling as monomers and information storage and transfer in polymers
proteins- monomer=amino acids, polymer=proteins/peptides, workers of the cell,
41
ion
an atom or molecule that is charged
42
chemical bonds
hold atoms together in molecules
43
Know the four levels of protein structure and the seven different functional categories of proteins. What are the ways that protein function can be modulated as discussed in Chapter 2?
primary- specific sequence of amino acids in a peptide
secondary- different regions of peptide chain are attracted to each other(alpha helix or beta pleated sheets)
tertiary- bonding and folding forming 3D structure
quarternary- formed when two or more tertiary structures are attached to form a unique molecule
Seven different functional categories of proteins-
1. enzymes- biological catalysts
2. membrane transporters- move substances between intra and extra cellular compartments
3. signal molecules- hormoes and other signal molecules
4. receptors- proteins that bind signal molecules and initiate cellular responses
5. binding proteins- found mostly in extracellular fluid bind/transport molecules throughout the body
6. immunoglobulins- (antibodies) help protect the body from foreign invaders and substances.
7. regulatory proteins- turn cell processes on or off, up and down.
Protien modulation- altered by factors such as pH, temp., and molecules that interact w/ protein.
1. cofactors- required for ligand binding at binding site.
2. proteolytic activation- converts inactive to active form by removing part of molecules.
3. competitive inhibitor- competes directly with ligand by binding reversibly to active site.
4. irreversible inhibitor- binds to binding site and cannot be displaced
5. allosteric modulator- binds to protein away from binding site and changes activity; may be inhibitors or activators
6. covalent modulator- binds covalently to protein and changes its activity.
7. pH/temperature- alter 3Dimensional shape of protein by disrupting hydrogen or S-S bonds; may be irreversible if protein becomes denatured.
44
Anion
an atom that gains an electron
45
What system produces 2 ATP molecules for each glucose molecule processed?
glycolysis
46
Covalent bond
a bond where electrons are shared between atoms
47
What are the byproducts of the citric acid cycle(krebs cycle)?
36 ATP molecules, water, and carbon dioxide
48
ionic bond
in this type of bond, one atom loses an electron and the other gains one, and they are held together by their +/- attraction.
49
hydrophobic(covalent)
molecules that do not dissolve readily in water
50
hydrophilic(ionic)
molecules that dissolve readily in water
51
pH scale acids
when considering pH, the lower the number the more acidic
52
atomic mass
the number of protons plus the number of neutrons i
53
atomic number
the number of protons in an element
54
pH
this variable measures the concentration of hydrogen ions in a solution
55
Concentration
the measurement of the amount of solute per unit volume
56
organic molecules
any molecule that contains carbon (such as propane, carbon dioxide, cholestrol, etc)
57
biomolecule
molecules that contain carbon AND are associated with living organisms, such as carbohydrates, lipids, etc.
58
Understand the difference between a concept map, process map, feedback loop, and a graph. Can you draw each if given a scenario?
concept maps-used to understand patterns in structure/ function or group related vocabulary terms.
process map(flow chart)- shows a sequence of events, indicates passage of time, steps must be in order
feedback loops- show how homeostasis is maintained, basic process map: stimulus, sensor, afferent pathway, integrating center, efferent pathway, effector, effector's action, response, and back to stimulus
59
carbohydrates
a category of biomolecule that is the most abundant energy source used in the body
60
lipids
these biomolecules are hydrophobic and serve many roles in the body, including energy storage, signaling molecules, and form an integral component of cell membranes.
61
Proteins
these biomolecules serve many functions throughout the body including signaling molecules, receiving signals, transporting other molecules or ions across the cell membrane, catalyzing reactions, regulating gene expression, and defending the body against pathogens.. "workers of the cell"
62
nucleic acids
this type of polymer plays an important role in information transfer from one generation to the next and in the creation of new proteins from single amino acids monomers.
63
monosaccharides
the monomers of carbohydrates
64
glycogen
is a polymer of glucose molecules that stores energy in animals. Humans can also digest this polymer.
65
Starch
is a polysaccharide that stores energy in plants. Humans can also digest this polymer.
66
Amino Acids
these molecules are the monomer form of proteins
67
Fatty Acids
these molecules are the building blocks of lipids, and can be saturated, monounsaturated, or polyunsaturated
68
nucleotide
these building block molecules are composed of a nitrogenous base, a 5 carbon sugar, and a phosphate molecule.
69
conjugated
when one kind of biomolecule is attached to a different kind of biomolecule.
70
lipoprotein
when a lipid s attached to a protein
71
glycoprotein
when a sugar molecule is attached to a protein
72
triglycerides
the primary storage form of lipids
73
purines
a sub group of nucleotides formed by adenine and guanine
74
quaternary(level of organization)
when multiple protein subunits combine to form a functional protein
75
secondary(level of organization)
when an amino acid chain folds into alpha-helices or beta pleated sheets
76
tertiary(level of organization)
when globular proteins attain a complex, three-dimensional shape, consisting of pockets, channels, or protruding knobs
77
primary(level of organization)
the linear sequence of amino acids constitutes this level of protein organization
78
immunoglobulins
these extracellular immune proteins, also called antibodies, help protect the body from pathogens
79
receptors
proteins that bind signal molecules and initiate cellular responses
80
regulatory proteins
this category of proteins modulates cell processes, like when transcription factors bind to DNA and up-regulate or down regulate gene expression.
81
binding proteins
Some important biomolecules and gases are not very soluble in water. Therefore proteins of this class bind to these biomolecules or gases and make them water soluble so that they can be transported through the body.
82
Water
(the primary organic solvent)
83
Membrane transporters
these proteins help to move substances back and forth between the intracellular and extracellular compartments.
84
signal molecules
This category of peptides is used to transmit information from one cell to another.
85
binding proteins(examples)
some examples of these proteins are hemoglobin, low density lipoproteins(LDL), and high density lipoprotein(HDL)
86
Enzymes
these proteins catalyze chemical reactions.
87
reversible
when a reaction can proceed in both directions
88
ligands
are molecules that bind to proteins at specialized binding sites.
89
affinity
the amount of attraction between a substrate and its binding site.
90
equilibrium(reaction example)
reversible reactions proceed to a point of EQUILIBRIUM where the forward reaction happens at the same rate as the reverse reaction
91
agonists
two or more ligands that compete with each other for a binding site or mimic each other's actions
92
isoforms
closely related proteins whose function is similar, but whose affinity for ligands differs
93
proteolytic activation
this occurs when a fragment of an inactive protein is removed to create an active protein.
94
cofactor
an ion or small organic functional group that some proteins require for activation
95
antagonists
also called inhibitors, are chemical modulators that bind to a protein and decrease its activity.
96
allosteric activation
occurs when a modulator molecule binds to a proteins away from the binding site and activates that binding site.
97
denatured
when a protein loses its conformation, either by exposure to a temperature or pH outside it optimum
98
up-regulation
when the amount of a protein(eg. receptors, enzymes, and membrane transporters) is increased.
99
saturation
a point achieved when all binding sites are occupied and the rate of work can no longer increase
100
plasma
this extracellular fluid is the fluid portion of the blood
101
interstitial fluid
this extracellular fluid is the fluid environment that surrounds most cells in body tissues and organs.
102
cell membrane
this outer surface of the cell is composed mostly of lipids and embedded proteins
103
fluid mosaic model
the concept of the many components of the outer surface of a cell are not static, but rather can move and rearrange their distribution.
104
integral proteins
these proteins are tightly bound to the membrane, and the only way they can be removed is by disrupting the membrane structure with detergents or other harsh methods.
105
inclusions
these are particles of insoluble material inside a cell that are sometimes called non-membranous organelles.
106
cytoplasm
includes all material inside the cell membrane, except the nucleus.
107
ribosomes
these are small, dense granules of RNA and protein that manufacture proteins under the direction of the cell's DNA.
108
cytoskeleton
the cells internal support system formed with insoluble protein fibers
109
motor proteins
these are proteins that can convert stored energy into directed movement.
110
mitochondria
these organelles have their own genetic material, and are the primary site of aerobic energy production in the cell.
111
endoplasmic reticulum
this organelle is a network of interconnected membrane tubes with three major functions: synthesis, storage, and transport of biomolecules.
112
golgi apparatus
this organelle receives proteins made in the rough endoplasmic reticulum and packages them into vesicles.
113
nucleus
this organelle in the cell contains all the genetic material used to make proteins and control cell processes.
114
lysosomes
these are small storage vesicles that contain powerful enzymes and act as the digestive system of the cell.
115
desmosomes
these cell-cell anchoring junctions attach to intermediate filaments of the cytoskeleton.
116
In the reaction I+J → P+Q, the letters "I" and "J" represent what? P+Q represent what?
reactants(substrates), products
117
enzyme(in relation to equation)
catalyst, often above arrow in reaction equation
118
energy
defined as the capacity to do work
119
chemical work
enables cells and organisms to grow, reproduce, and carry out normal activities.
120
Transport work
enables cells to move molecules to create concentration gradients.
121
Kinetic energy
the general term used to describe energy of motion.
122
potential energy
is the general term used to describe stored energy
123
free energy
the energy stored in the chemical bonds of a molecule and available to perform work
124
activation energy
the energy invested to start the reaction, (in most biological reactions)
125
exergonic reaction
reaction that breaks chemical bonds, makes simpler molecules from complex ones, and release free energy for use elsewhere
126
endergonic reactions
a reaction that forms new chemical bonds, makes more complex molecules from simpler ones, and stores free energy in those bonds.
127
ATP
a molecule that is the primary energy source for biological reactions.
128
Irreversible reaction
is a reaction that can only proceed in one direction
129
exergonic reaction
130
endergonic reaction
131
Enzymes lower the _________ of reactions, making them more likely to start.
activation energy
132
isozymes
a variety of related forms of enzymes, which catalyze the same reaction, but in different tissues, under different conditions, or at different rates.
133
Reduction
When a molecule gains a high energy electron (and an H+ ion) during a chemical reaction
134
Oxidation
when a molecule loses a high energy electron (and an H+ ion) during a chemical reaction
135
Phosphorylation
when a molecule gains a phosphate group during a chemical reaction
136
kinase
an enzyme that transfers( or exchanges) a phosphate group from one molecule to another
137
dehydration reaction
a water molecule is removed to make one large molecule from several smaller ones.
138
dehydrogenase reaction
an enzyme that removes high energy electrons and H+ ions from a reactant
139
phosphorylase
this kind of enzyme adds phosphate groups from an inorganic source(like HPO subset 4) to other molecules
140
phosphotase
this kind of enzyme removes phosphate groups from molecules
141
transaminase
this kind of enzyme transfers an amino group from one molecule to another.
142
synthetase
this kind of enzyme will join two substrates using the energy from ATP
143
peptidase
an enzyme that splits proteins into smaller fragments or single amino acids through the addition of water
144
metabolism
refers to all chemical reactions that take place in an organism.
145
anabolism
term for energy utilizing reactions that result in the synthesis of large biomolecules from smaller monomers.
146
catabolism
the term for reactions that release energy through the breakdown of large biomolecules into smaller monomers.
147
in this general chemical reaction, A arrow B arrow C arrow D, the molecules B and C would be considered what?
intermediates
148
aerobic reaction
metabolic reaction that requires oxygen
149
anaerobic reaction
metabolic reaction that does not require oxygen and takes place in the cytoplasm
150
electron transport system
this aerobic metabolic pathway produces the most ATP molecules per molecule of glucose
151
glycolysis
this set of anaerobic reactions transforms a 6 carbon sugar molecule into two 3 carbon molecules, and produces a net of 2 ATP molecules.
152
citric acid cycle
this aerobic pathway produces 2 ATP molecules and a total of 8 nucleotide-based molecules that store high energy electrons.
153
NADH
this molecule stores high energy electrons and ultimately contains enough potential energy to produce 2.5 ATP molecules on average.
154
FADH subset 2
this molecule also stores high energy electrons, but only contains enough potential energy to produce 1.5 ATP molecules on average.
155
Glucose
this molecule is the primary(starting) substrate for glycolysis
156
pyruvate
this molecule is the primary(end) product of glycolysis.
157
Water
byproduct of the electron transport system besides ATP
158
Mitochondria
the site of aerobic respiration in the cell
159
how many high energy phosphate bonds does ATP contain?
2 high energy phosphate bonds
160
hydrolysis
enzymatic process releases energy from ATP by breaking a high energy phosphate bond through the addition of a water molecule.
161
dehydration synthesis
enzymatic process uses energy to rebuild ATP from ADP and inorganic phosphate.
162
creatine phosphate
the immediate source of energy fro rebuilding ATP
163
What are the two ways ATP production enters the cell?
glucose for ATP production either enters the cell from the blood, or is produced by the hydrolysis of glycogen stored in muscle cells and the liver.
164
What happens to pyruvate(or pyruvic acid) in the absence of oxygen? and what does that do?
lactic acid, brings about muscle fatigue
