PHYSIO EXAM #1

• 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.

• 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.

Homeostasis is organisms keeping their internal environment relatively stable. Ex. blood pressure, blood glucose, body temperature, and water balance

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)

altered variable

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

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

Nervous and Endocrine system

Immune system

• 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

• 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

• carbohydrates - glucose
• lipids - cholesterol
• proteins - creatine, collagen, hemoglobin, enzymes
• nucleotides - ATP, DNA, RNA

STARCH

CHITIN

GLUCOSE

CELLULOSE

*humans cannot digest

GLYCOGEN

LIPOPROTEINS

GLYCOPROTEINS

Amino Acids

Essential Amino Acids

Enzymes

Primary Structure

Tertiary structure / Globular Proteins

• 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)

LIGAND

SPECIFICITY

BINDING SITE

INDUCED FIT

COFACTOR

protein whose structure is altered to the point that its activity is destroyed

• 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: 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.

Ex. Hemoglobin

allosteric activator & covalent modulator

agonist

competitive inhibitor & antagonist

gains or loses one or more electrons

• Anion: gains electron (negative charge)
• Cation: loses electron (positive charge)

no double bonds

• 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.

• proteins
• phospholipids

• 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

• 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

CILIA

CENTRIOLE

LYSOSOME

MITOCHONDRIA

PEROXISOME

increasing concentrations of H+ decreasing the pH (very acidic environment) and activates enzyme.

ENDOCRINE

• allow material to pass directly from cytoplasm of one cell to another
• simplest
• 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)

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

many epithelia are vulnerable to damage and need to be replaced frequently. Cells undergoing frequent mitosis are more likely to develop abnormal cell division.

CYTOLOGY

• 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

• 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 Golgi apparatus

• smaller than lysosomes
• degradating of long chain fatty acids
• generate hydrogen peroxide -> contain catalase

• control center
• nuclear envelope
• chromatin
• one or more nucleoli
• genes

• 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.

KINETIC

POTENTIAL

METABOLISM

speed up rxn rate by decreasing the activation energy of the reaction

REVERSIBLE

EXERGONIC

SPECIFICITY

ACTIVATION ENERGY

VITAMINS in our diet

REDUCED

OXIDIZED

DEHYDRATION

HYDROLYSIS

DEAMINATION

TRANSAMINATION

converted into urea and uric acid

CATABOLIC

ANABOLIC

Kilocalories

FEEDBACK INHIBITION

• H+ -> inner compartment -> stored E in concentration gradient.
• When ions <- across membrane, released E is trapped in high-E bond of ATP (peptide bond)

NADH & FADH2

Smooth ER

• 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

when inactive they cannot harm the cell if accidentally released

• 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.

• enzymes
• membrane transporters
• signal molecules
• receptors
• binding proteins
• regulatory proteins
• immunoglobulins (antibodies)
• globular

• collagen
• actin
• myosin
• filaments
• 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
• penicillin
• 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

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

• control of enzyme concentration
• modulator production
• different enzymes for reversible rxns
• compartmentation of enzymes
• ATP/ADP ratio

• oxidative phosphorylation
• glycolysis
• CAC
• ETC

C6H12O6 + 6O2 -> 6CO2 + H2O + E

• Glycogen -> animals
• Amylose -> plants
• Starch -> short term E storage for cells

• from 1 glucose = 2 pyruvate molecules
• Net gain 2 ATP
• Anaerobic

• Anaerobic Catabolism: (muscles) no O2 pyruvate -> lactate
• Aerobic Catabolism: O2 pyruvate -> CAC

from each pyruvate = 3 CO2 molecules

• 1 ATP
• 3 NADH
• 1 FADH2
• waste: 2 CO2

per pyruvate per cycle

• 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

(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

• OVERALL:
• 6 H20
• 30-32 ATP
• 6 CO2 waste per glucose