1. 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.
  2. 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.
  3. 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
  4. 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)
  5. Independant variable
    altered variable
  6. Dependant variable
    dependendent on the independent variable
  7. Teleological
    the function, "why does the system exist and why does the event happen?"
  8. Mechanistic
    the process, "how"
  9. blind study
    subjects do not know whether they are receiving the placebo or the treatment
  10. 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
  11. crossover study
    the control group in the first half of the expirement becomes the experimental group in the second half, vice versa
  12. Which organ systems are responsible for coordinating body function?
    Nervous and Endocrine system
  13. Which organ system is responsible for protecting the body from outside invaders?
    Immune system
  14. 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
  15. Genomics
    genome -> genes -> DNA -> information
  16. Proteomics
    proteins -> functional -> enzymes
  17. Regulation of plasma calcium concentrations
    • calcium: 1. muscle contractions
    • 2. bone density
    • 3. signal

    Endocrine -> antagonists, Skeletal, Digestive system
  18. Antagonist:
    Ex. parathyroid hormone, calcitonin, Vitamin D

    substance that opposes the action of another

    hormones or neurons with opposing effects on some homeostatic functions
  19. Compartmentation
    allows a cell, a tissue, or an organ to specialize and isolate functions.

    tiny compartments within the cell : organelles
  20. nocebo effect
    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
  21. placebo effect
    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
  22. bar graphs
    used when the independent varibables are distinct entities.
  23. line graphs
    commonly used when the independent variable is on a continuous phenomenon
  24. scatter plot
    shows relationship between two variables
  25. List 4 kinds of Biomolecules
    • carbohydrates - glucose
    • lipids - cholesterol
    • proteins - creatine, collagen, hemoglobin, enzymes
    • nucleotides - ATP, DNA, RNA
  26. The storage form of glucose in plants:
  27. Structural polysaccharide of intevertebrates:
  28. Monosaccharide:
  29. Most abundant carbohydrate on earth:

    *humans cannot digest
  30. Storage form of glucose in animals:
  31. When proteins are combined with fatty components they are called:
  32. When proteins are combined with carbohydrates they are called:
  33. The building blocks:
    Amino Acids
  34. Must be included in our diet:
    Essential Amino Acids
  35. Proteins that speed the rate of chemical reactions:
  36. Sequence of Amino Acids in a protein:
    Primary Structure
  37. Protein chains folded into a ball shaped structure:
    Tertiary structure / Globular Proteins
  38. 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
  39. Purines
    double ring structure : Adenine & Guanine
  40. Pyrimidines
    single ring: Cytosine, Thymine (DNA only), Uracil (RNA only)
  41. A molecule that binds to another molecule:
  42. The ability of a protein to bind to one molecule but not to another
  43. The part of a protein molecule that bind the ligand:
  44. The ability of a protein to alter its shape to fit more closely with that ligand:
  45. An ion, such as Ca2+ or Mg2+ , that must be present in order for an enzyme to work:
  46. Denatured:
    protein whose structure is altered to the point that its activity is destroyed
  47. 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)
  48. DNA vs. RNA
    • DNA: double helix, deoxyribose, AGCT
    • RNA: single band, ribose, AGCU
  49. Isoforms:
    closely related proteins whos structure and function are similar but their affinities for ligands are different.

    Ex. Hemoglobin
  50. Must bind to an enzyme and enhance its activity
    allosteric activator & covalent modulator
  51. Should mimic the activity of a normal nervous system signal molecule
  52. Should block the activity of a membrane receptor protein
    competitive inhibitor & antagonist
  53. Ions:
    gains or loses one or more electrons

    • Anion: gains electron (negative charge)
    • Cation: loses electron (positive charge)
  54. Saturated:
    no double bonds
  55. 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.
  56. Two primary types of bimolecules found in cell membrane:
    • proteins
    • phospholipids
  57. Inclusions
    • 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
  58. Organelles
    • membrane bounded compartments
    • play specific roles in overall function of cell

    Ex. mitochondria, lysosomes
  59. Define Cytoskeleton.
    a flexible, changeable three-demisonal scaffolding of actin microfilaments, intermediate filaments, and microtubules that extends throughout the cytoplasm
  60. 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
  61. short hairlike structures that beat to produce currents in fluid
  62. a bundle of microtubules that aids in mitosis
  63. digestive system of the cell; degrading or recycling components
  64. powerhouse of the cell where most ATP reticulum is produced
  65. degrades long chain fatty acids and toxic foreign molecules
  66. What process activates the enzyme inside lysosomes?
    increasing concentrations of H+ decreasing the pH (very acidic environment) and activates enzyme.
  67. Glands that release hormones, which enter the blood and regulate the activities of organs or systems.
  68. Gap Junctions
    • 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
  69. Tight Junctions
    • 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
  70. Adhesive Junctions
    • allow twisting and stretching of the tissue
    • attach cells to each other or to extracellular matrix
    • found in skin
  71. Vesicle
    • Membrane bound sphere
    • Secretory: contain proteins that will be released from the cell
    • Storage: never leave the cytoplasm (lysosomes)
  72. 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.
  73. Apoptosis
    a normal event in the life of an organism. During fetal development, apoptosis removes unneeded cells
  74. 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.
  75. study of cell structure
  76. Functions of Cell membrane:
    • physical isolation
    • regulation of exchange with environment
    • communication between cell and environment (electrically or chemically)
    • structural support
  77. Micelle
    role in digestion and absorbtion of fats in GI tract
  78. Liposome
    larger, bilayer, hollow center with aqueous core
  79. Cytoplasmic protein fibers
    • function in structural support and movement
    • actin (microfilaments)
    • intermediate - mysosin, keratin
    • microtubules - centrioles, cilia, flagella
  80. Ribosomes
    protein synthesis /transfer of proteins

    • fixed to ER -> go to golgi aparatus
    • free in cytoplasm -> proteins stay in cell
  81. Golgi Complex
    • "post office"
    • modification (labeling) of proteins
    • packaging into secretory or storage vesicles
  82. The organelle that combines proteins with cotts and packages them within vesicles for secretion is
    the Golgi apparatus
  83. Peroxisomes
    • smaller than lysosomes
    • degradating of long chain fatty acids
    • generate hydrogen peroxide -> contain catalase
  84. Nucleus
    • control center
    • nuclear envelope
    • chromatin
    • one or more nucleoli
    • genes
  85. 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.
  86. the energy of motion
  87. stored energy
  88. the sum of all chemical processes through which cells obtain and store energy
  89. Enzymes
    speed up rxn rate by decreasing the activation energy of the reaction
  90. reaction that runs in either direction
  91. reaction that releases energy
  92. ability of an enzyme to catalyze one reaction but not the other
  93. boost of energy needed to get a reaction started
  94. The precursors of coenzymes come from
    VITAMINS in our diet
  95. gains an electron
  96. loses an electron
  97. The removal of H2O from reacting molecules
  98. Using H2O to break down polymers
  99. The removal of an amino group from a molecule
  100. Transfer of an amino group from one molecule to the carbon skeleton of another molecule (to form a different amino acid)
  101. What happens to the amino group removed from the amino acid?
    converted into urea and uric acid
  102. Reactions release energy and result in the breakdown of large biomolecules
  103. Reactions require a net input of energy and result in the synthesis of large biomolecules
  104. In what units do we measure the energy of metabolism?
  105. Metabolic regulation in which the last product of a metabolic pathway (the end product) accumulates and slows or stops reactions earlier in the pathway
  106. 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)
  107. Carrier molecules that deliver high-E electrons to the electron transport system
    NADH & FADH2
  108. Organelle involved in lipid synthesis?
    Smooth ER
  109. 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
  110. Compartmentation
    • glycolysis takes place in the cytosol; oxidative phosphorylation takes place in the mitochondria
    • proteins are modified in the ER
  111. Molecular Interactions
    • Some proteins have S-S bonds between non-adjacent amino acids
    • Enzymes catalyze biological reactions
  112. 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
  113. 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
  114. Anticodons
    Anticodons are apart of tRNA and Amino Acids attach to tRNA.
  115. Soluble proteins
    • enzymes
    • membrane transporters
    • signal molecules
    • receptors
    • binding proteins
    • regulatory proteins
    • immunoglobulins (antibodies)
    • globular
  116. Insoluble proteins
    • 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
  119. Irreversible binding
    • covalent bonds
    • penicillin
    • cyanide - binds to cytochrome c-oxidase interrupts e- transport chain
  120. Allosteric Modulators
    • interact with enzyme
    • bind to protein away from active site changing the shape of binding site for better or for worse
  121. Agonist
    • protein without modulator is inactive
    • modulator binds to protein away from biding site makes it active
  122. Antagonist
    • proteins without modulator is active
    • modulator binds to protein away from binding site and inactivates the binding site making protein inactive
  123. How do enzymes lower activation E?
    the provide a substrate
  124. Siamese Cats
    • Tyrosine -> melanin
    • temperature senstive of enzyme
  125. Isoenzymes
    • different models of same enzyme
    • same functions
    • catalyze same reaction under different conditions and in different locations
  126. Cells regulate metabolic pathways via
    • control of enzyme concentration
    • modulator production
    • different enzymes for reversible rxns
    • compartmentation of enzymes
    • ATP/ADP ratio
  127. Complete oxidation of CHO such as glucose requires:
    • oxidative phosphorylation
    • glycolysis
    • CAC
    • ETC
  128. Oxidation of Glucose Equation
    C6H12O6 + 6O2 -> 6CO2 + H2O + E
  129. Energy storage
    • Glycogen -> animals
    • Amylose -> plants
    • Starch -> short term E storage for cells
  130. End products of Glycolysis (in cytoplasm)
    • from 1 glucose = 2 pyruvate molecules
    • Net gain 2 ATP
    • Anaerobic
  131. Fates of Pyruvate
    • Anaerobic Catabolism: (muscles) no O2 pyruvate -> lactate
    • Aerobic Catabolism: O2 pyruvate -> CAC

    from each pyruvate = 3 CO2 molecules
  132. End products of Citric Acid Cycle (in mitochondria matrix)
    • 1 ATP
    • 3 NADH
    • 1 FADH2
    • waste: 2 CO2

    per pyruvate per cycle
  133. End products of Electron Transport System (mitochondria membrane)
    • 2.5 ATP per NADH
    • 1.5 ATP per FADH2
  134. Protein Synthesis
    DNA -> (transcription) mRNA -> (translation) protein
  135. Transcrption
    • Anabolic reaction
    • DNA is transcribed into complementary mRNA by RNA polymerase + nucleotides + Cofactors (Mg2+) + ATP (energy)
  136. Translation
    • 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
Card Set
study for exam 1