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Define Physiology. Describe the relationship between Physiology and Anatomy.
- Physiology is the study of the normal functioning of a living organism and its component parts, including chemical and physical processes.
- Anatomy and Physiology cannot truely be separated. The function of a tissue or organ is closely tied to its structure.
Name the 10 systems of the body and their major function:
- 1. Circulatory - transport materials between all cells of the body.
- 2. Digestive - conversion of food into particles that can be transported into the body; elimination of wastes.
- 3. Endocrine - coordination of body function through synthesis and release of regulatory molecules.
- 4. Immune - defense agains foreign invaders.
- 5. Integumentary - protection from external enviornment.
- 6. Musculoskeletal - support and movement
- 7. Nervous - coordination of body function through electrical signals and release of regulatory molecules.
- 8. Reproductive - perpetuation of the species
- 9. Respiratory - exchange of oxygen and carbon dioxide between the internal and external environments.
- 10. Urinary - maintenence of water and solutes in the internal environment; waste removal.
Define Homeostasis. Name some physiological parameters that are maintained homeostatically.
Homeostasis is organisms keeping their internal environment relatively stable. Ex. blood pressure, blood glucose, body temperature, and water balance
Four major themes in physiology:
1. homeostasis and control system - balance, integration of body system functions, dynamic equilibrium (temp, pH, blood pressure)
2. biological energy use - constant E input needed
3. structure-function relationships - molecular interactions, compartmentation
4. communication - cells communicate with other cells, tissues & organs. Membrane transport, signal transduction (electrical and chemical)
dependendent on the independent variable
the function, "why does the system exist and why does the event happen?"
the process, "how"
subjects do not know whether they are receiving the placebo or the treatment
double blind study
there is a 3rd party not involved in the expirement who is the only one who knows whether the subject is receiving the treatment or the placebo
the control group in the first half of the expirement becomes the experimental group in the second half, vice versa
Which organ systems are responsible for coordinating body function?
Nervous and Endocrine system
Which organ system is responsible for protecting the body from outside invaders?
Which organ systems exchange materials with the external environment? What do they exchange?
- Respiratory system - exchanges gases
- Digestive system - absorbs nutrients and water, eliminates wastes
- Urinary system - removes excess water and waste material
- Reproductive system - produces egg and sperm
genome -> genes -> DNA -> information
proteins -> functional -> enzymes
Regulation of plasma calcium concentrations
- calcium: 1. muscle contractions
- 2. bone density
- 3. signal
Endocrine -> antagonists, Skeletal, Digestive system
Ex. parathyroid hormone, calcitonin, Vitamin D
substance that opposes the action of another
hormones or neurons with opposing effects on some homeostatic functions
allows a cell, a tissue, or an organ to specialize and isolate functions.
tiny compartments within the cell : organelles
if you warn people that a drug they are taking may have specific adverse side effects, those people will report a higher incidence of the side effects than a similar group of people who were not warned
if you give someone a pill and tell the person that it will help aliviate some problem, there is a strong possibility that the pill will have exactly that effect, even if it contains only sugar
used when the independent varibables are distinct entities.
commonly used when the independent variable is on a continuous phenomenon
shows relationship between two variables
List 4 kinds of Biomolecules
- carbohydrates - glucose
- lipids - cholesterol
- proteins - creatine, collagen, hemoglobin, enzymes
- nucleotides - ATP, DNA, RNA
The storage form of glucose in plants:
Structural polysaccharide of intevertebrates:
Most abundant carbohydrate on earth:
*humans cannot digest
Storage form of glucose in animals:
When proteins are combined with fatty components they are called:
When proteins are combined with carbohydrates they are called:
The building blocks:
Must be included in our diet:
Essential Amino Acids
Proteins that speed the rate of chemical reactions:
Sequence of Amino Acids in a protein:
Protein chains folded into a ball shaped structure:
Tertiary structure / Globular Proteins
Components of a nucleotide:
- 1. one or more phosphate groups
- 2. five carbon sugar (deoxyribose)
- 3. nitrogenous base (C-N ring) A,C,T,G,U
double ring structure : Adenine & Guanine
single ring: Cytosine, Thymine (DNA only), Uracil (RNA only)
A molecule that binds to another molecule:
The ability of a protein to bind to one molecule but not to another
The part of a protein molecule that bind the ligand:
The ability of a protein to alter its shape to fit more closely with that ligand:
An ion, such as Ca2+ or Mg2+ , that must be present in order for an enzyme to work:
protein whose structure is altered to the point that its activity is destroyed
Protein structure (1O - 4O)
- 1. long sequence chain of amino acids
- 2. amino acid chain in spirals, turns, and pleated sheets (stabalized by H-bonding)
- 3. chain twisted into a ball-shaped structure (fibrous proteins, keratin, globular cells)
- 4. multiple protein ball-shaped structures formed together (hemoglobin)
DNA vs. RNA
- DNA: double helix, deoxyribose, AGCT
- RNA: single band, ribose, AGCU
closely related proteins whos structure and function are similar but their affinities for ligands are different.
Must bind to an enzyme and enhance its activity
allosteric activator & covalent modulator
Should mimic the activity of a normal nervous system signal molecule
Should block the activity of a membrane receptor protein
competitive inhibitor & antagonist
gains or loses one or more electrons
- Anion: gains electron (negative charge)
- Cation: loses electron (positive charge)
no double bonds
List four general functions of the cell membrane:
- physical isolation - seperates intracellular fluid inside the cell from the surrounding extracellular fluid
- regulation of exchanges - controls entry of ions and nutrients, eliminates waste, and releases products from cell
- communication between the cell and its environment - contains proteins that enable the cell to recognize and respond to molecules
- structural support - proteins hold cytoskeleton, maintain cell shape, cell-cell & cell-matrix junctions stabalize the structure of tissues.
Two primary types of bimolecules found in cell membrane:
- particles of insoluble materials
- stored nutrients
- responisble for specific cell functions
- "nonmembranous organelles"
- do not have boundary membranes
- in direct contact with cytosol
Ex. ribosomes, proteasomes, vaults, protein fibers
- membrane bounded compartments
- play specific roles in overall function of cell
Ex. mitochondria, lysosomes
a flexible, changeable three-demisonal scaffolding of actin microfilaments, intermediate filaments, and microtubules that extends throughout the cytoplasm
Functions of Cytoskeleton.
- cell shape - provides mechanical strength to the cell and plays a role in determining shape
- internal organization - stabilize the positions of organelles
- intracellular transport - help transport materials into the cell and within the cytoplasm
- assembly of cells into tissues - linking cells (allow transfer of info) to one another and support materials outside of the cell, provide mechanical strength to tissue
- movement - helps cells move. Cilia and flagella and special motor proteins facilitate movement
short hairlike structures that beat to produce currents in fluid
a bundle of microtubules that aids in mitosis
digestive system of the cell; degrading or recycling components
powerhouse of the cell where most ATP reticulum is produced
degrades long chain fatty acids and toxic foreign molecules
What process activates the enzyme inside lysosomes?
increasing concentrations of H+ decreasing the pH (very acidic environment) and activates enzyme.
Glands that release hormones, which enter the blood and regulate the activities of organs or systems.
- allow material to pass directly from cytoplasm of one cell to another
- create cytoplasmic communication bridges between adjoining cells
- found in muscles, nerve cells, tissues
- prevent movement of materials between cells
- cell membranes of adjacent cells partly fuse together with the help of proteins
- prevent substances from movng freely between internal and external environments
- create blood-brain barrier
- found in epithelia
- allow twisting and stretching of the tissue
- attach cells to each other or to extracellular matrix
- found in skin
- Membrane bound sphere
- Secretory: contain proteins that will be released from the cell
- Storage: never leave the cytoplasm (lysosomes)
Explain how inserting cholesterol into phospholipid bilayer of the cell membrane decreases membrane permeability
Cholesterol molecules which are mostly hydrophobic insert themselves between the hydrophilic heads of phospholipids. Cholesterol helps make membranes impermeable to small water-soluble molecules and keeps membranes flexible over a wide range of temperatures.
a normal event in the life of an organism. During fetal development, apoptosis removes unneeded cells
What property of epithelial tissues might and does make them more prone to developing cancer?
many epithelia are vulnerable to damage and need to be replaced frequently. Cells undergoing frequent mitosis are more likely to develop abnormal cell division.
study of cell structure
Functions of Cell membrane:
- physical isolation
- regulation of exchange with environment
- communication between cell and environment (electrically or chemically)
- structural support
role in digestion and absorbtion of fats in GI tract
larger, bilayer, hollow center with aqueous core
Cytoplasmic protein fibers
- function in structural support and movement
- actin (microfilaments)
- intermediate - mysosin, keratin
- microtubules - centrioles, cilia, flagella
protein synthesis /transfer of proteins
- fixed to ER -> go to golgi aparatus
- free in cytoplasm -> proteins stay in cell
- "post office"
- modification (labeling) of proteins
- packaging into secretory or storage vesicles
The organelle that combines proteins with cotts and packages them within vesicles for secretion is
the Golgi apparatus
- smaller than lysosomes
- degradating of long chain fatty acids
- generate hydrogen peroxide -> contain catalase
- control center
- nuclear envelope
- one or more nucleoli
Three basic forms of work:
- chemical work - the making and breaking of chemical bonds, enables cells and organisms to grow, maintain suitable environment, and stores info for repro. Ex. forming chemical bonds
- Transport work - enables cells to move ions, molecules, and larger particles through the cell membrane and membranes of organelles. Useful for creating concentration gradients. Ex. ER use E to import calcium ions from cytosol back into the cytosol creating "calcium signals" causes action, such as muscle contraction
- Mechanical work - in animals is used for movement Ex. organelles moving around in cell, cells changing shape, and cilia and flagella beating, muscle contractions. Mediated by motor proteins that make intracellular fibers and filaments.
the energy of motion
the sum of all chemical processes through which cells obtain and store energy
speed up rxn rate by decreasing the activation energy of the reaction
reaction that runs in either direction
reaction that releases energy
ability of an enzyme to catalyze one reaction but not the other
boost of energy needed to get a reaction started
The precursors of coenzymes come from
VITAMINS in our diet
gains an electron
loses an electron
The removal of H2O from reacting molecules
Using H2O to break down polymers
The removal of an amino group from a molecule
Transfer of an amino group from one molecule to the carbon skeleton of another molecule (to form a different amino acid)
What happens to the amino group removed from the amino acid?
converted into urea and uric acid
Reactions release energy and result in the breakdown of large biomolecules
Reactions require a net input of energy and result in the synthesis of large biomolecules
In what units do we measure the energy of metabolism?
Metabolic regulation in which the last product of a metabolic pathway (the end product) accumulates and slows or stops reactions earlier in the pathway
Explain how H+ movement across the inner mitochondiral membrane result in ATP synthesis:
- H+ -> inner compartment -> stored E in concentration gradient.
- When ions <- across membrane, released E is trapped in high-E bond of ATP (peptide bond)
Carrier molecules that deliver high-E electrons to the electron transport system
NADH & FADH2
Organelle involved in lipid synthesis?
Biological E use
- The electron transport system traps E in a hydrogen ion concentration gradient
- Metabolic reactions are often coupled to the reaction ATP -> ADP + Pi
- Enzymes catalyze biological reactions
- glycolysis takes place in the cytosol; oxidative phosphorylation takes place in the mitochondria
- proteins are modified in the ER
- Some proteins have S-S bonds between non-adjacent amino acids
- Enzymes catalyze biological reactions
Why is it advantageous for a cell to store or secrete an enzyme in an inactive form
when inactive they cannot harm the cell if accidentally released
Anaerobic vs. Aerobic breakdown of glucose
- Aerobic breakdown - 30-32 ATP
- Anaerobic breakdown - 2 ATP
- Anaerobic breakdown is faster and doesn't require E, but energy yeild is less
Anticodons are apart of tRNA and Amino Acids attach to tRNA.
- membrane transporters
- signal molecules
- binding proteins
- regulatory proteins
- immunoglobulins (antibodies)
- Function = structure/ movement
- inorganic molecules - Ca2+ Mg2+
- conformational change of an active site
- organic molecules - vitamin derivatives, FADH2
- act as receptors and carriers for atoms or functional groups that are removed from substrate
- transport H atoms and small molecules from one enzyme to another
- covalent bonds
- cyanide - binds to cytochrome c-oxidase interrupts e- transport chain
- interact with enzyme
- bind to protein away from active site changing the shape of binding site for better or for worse
- protein without modulator is inactive
- modulator binds to protein away from biding site makes it active
- proteins without modulator is active
- modulator binds to protein away from binding site and inactivates the binding site making protein inactive
How do enzymes lower activation E?
the provide a substrate
- Tyrosine -> melanin
- temperature senstive of enzyme
- different models of same enzyme
- same functions
- catalyze same reaction under different conditions and in different locations
Cells regulate metabolic pathways via
- control of enzyme concentration
- modulator production
- different enzymes for reversible rxns
- compartmentation of enzymes
- ATP/ADP ratio
Complete oxidation of CHO such as glucose requires:
- oxidative phosphorylation
Oxidation of Glucose Equation
C6H12O6 + 6O2 -> 6CO2 + H2O + E
- Glycogen -> animals
- Amylose -> plants
- Starch -> short term E storage for cells
End products of Glycolysis (in cytoplasm)
- from 1 glucose = 2 pyruvate molecules
- Net gain 2 ATP
Fates of Pyruvate
- Anaerobic Catabolism: (muscles) no O2 pyruvate -> lactate
- Aerobic Catabolism: O2 pyruvate -> CAC
from each pyruvate = 3 CO2 molecules
End products of Citric Acid Cycle (in mitochondria matrix)
- 1 ATP
- 3 NADH
- 1 FADH2
- waste: 2 CO2
per pyruvate per cycle
End products of Electron Transport System (mitochondria membrane)
- 2.5 ATP per NADH
- 1.5 ATP per FADH2
DNA -> (transcription) mRNA -> (translation) protein
- Anabolic reaction
- DNA is transcribed into complementary mRNA by RNA polymerase + nucleotides + Cofactors (Mg2+) + ATP (energy)
- mRNA -> string of Amino Acids
- mRNA + ribosomes (rough ER (go outside of cell -> vesicles -> golgi apparatus, vesicles -> cell membrane) / free in cytoplasm (synthesize proteins)) + tRNA (amino acid + anticodon) meet in cytoplasm
- Amino acids are linked via PEPTIDE BOND
MAJOR STEPS TO CONVERT DNA INTO FUNCTIONAL PROTEIN:
(In Nucleus) DNA (gene activation via regulatory proteins) -> mRNA via transcription -> processed mRNA via alternative splicing/ RNA silencing -> polypeptide chain via translation (In Cytoplasm) -> protein via post translational modification (folding, additon of functional group, cleavage, assembly of proteins)
1 glucose molecule -> glycolysis -> 2 ATP, 2 pyruvate, 2 CO2 -> 2 Acetyl CoA -> CAC -> 6 NADH, 2 FADH2, 2 ATP, 4 CO2 -> Electron Transport System -> 2.5 ATP per NADH, 1.5 ATP per FADH2 + 6 H2O
- 6 H20
- 30-32 ATP
- 6 CO2 waste per glucose