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Human Physiology 402

by: Karely Mendez

Human Physiology 402 Human Biology 402

Karely Mendez


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Week 1 notes and Monday/Wednesday of Week 2
Human Physiology
Dr. Hanke
Class Notes
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This 35 page Class Notes was uploaded by Karely Mendez on Friday February 5, 2016. The Class Notes belongs to Human Biology 402 at 1 MDSS-SGSLM-Langley AFB Advanced Education in General Dentistry 12 Months taught by Dr. Hanke in Winter 2016. Since its upload, it has received 88 views. For similar materials see Human Physiology in Biology at 1 MDSS-SGSLM-Langley AFB Advanced Education in General Dentistry 12 Months.


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Date Created: 02/05/16
HP EXAM 1 CHAPTER 3 Cellular structure, proteins and metabolism VIEWS • MechanistsvsV italist views • Mechanist • Conventional USA medicine • Body is separated into compartments and healed as compartments • Vitalist • More Chinese style • Body is a whole self healing organisms • Hippocrates • Four humors • Blood, yellow bile, black bile, phlegm • All aresupposedto be balanced • Four temperaments • Sanguine, melancholy, choleric, phlegmatic PRINCIPLESOF FUNCTION • Structure= function • Structure determines function • Structures are changed evolution • Evolution does not mean perfection though • Cell differentiation allows specialization of function and increases efficiency. FOURTYPESOF TISSUES Four primary cell types (ECNM) • 1. Epithelial cells • Arebarriers • Form boundaries for protection • Selective secretion, absorption • Skin cells, endothelial cells • 2. Connective tissuecells • Connect, anchorandsupportotherstructuresofthebody • Bone, blood cells • Carry things to other parts,connects them • 3. Nerve cells • Communication • Initiates, integrates and conducts electrical signals to other cells • Neuron isthe fundamental cell • 4. Muscle cells • Generate force • Skeletal muscle, cardiac muscle BODY FLUID COMPARTMENTS • Body fluidsfoundin two places • 1. Intracellular space • Everything inside the cells • Also called cytoplasm • Majority of water in the body is inside the cell membrane • About 2/3 of whole water • 2. Extracellular space • Is about 1/3 of the body water • Outside the cells • 2 subcategories • A. Interstitial fluid • 75-80% ofthe 1/3 • B. Blood plasma • 20-25% ofthe 1/3 • So extracellular fluid= plasma + interstitial fluid • nutrientsgo plasma to intracellular PROPERTIES OFWATER • Has covalent bond • Non polar in contrast is • does not havetobe nonpolarthough • Hydrophobic (shared =) • Lipophilic • Has high degree of Hbonding • Non charged • HasH bonds • Which hold itself together with other H • Water very important to dissolve charged particles • Waterimportant bc everything follows water • Water is a polar molecule • hasone + end and one – end • Hydrophilic • likeswater • Lipophobic • Do notdissolvein oil • Is charged PROPERTIES OFWATER • Dissociate into H+ and OH- • Example: Molarity of H+ is 0.1M find (hydroxide) the pH? • OH- • pH= -log[M] • Gives you pH= -log[H+] • pH= -log[0.1] • Low pH have high H ions • pH= -log[1x10 ] • pH= 2 • Example: H+ pH 10 find M? • pH= 10 • M= 0.00000000001 HENDERSONHASSELBALCH EQUATION • Molecules with lipid like • Example: Will Asprin pass the characteristics are what get membrane if pka= 3 and stomach through cell membranes pH=2 • Cell membranes are composedof • pH= pka + log (A-/HA) lipids and are charged • 2= 3 + log (A-/HA) • so only other lipids can pass • -1= log (A-/HA) • pH= pKa + Log (A-)/(HA) • Antilog -1= log (A-/HA) • A- • 0.1= A-/HA • Ionized, water soluble • 1/10= A-/HA • impermeable • So for every 1 impermeaAle - • charged • There is10 permeable HA • HA • So Asprin will pass • Permeable • Uncharged MOLECULARSTRUCTUREOF ATP SYNTHASE • Very mechanical like • It spins around PROTEINSTRUCTURES • Composed of amino acids • R group • Thebuilding blocks • Side chain • With 20 different amino acids • Arranged in one long continuous chain • So 20 different R groups • DNA is the codethat determinesthe • Areall uniqueinshape arrangement • Determinefunction ofprotein • Transcription and translation • Centralalpha carbon • Transcription=DNA toRNA • ConnectsRgroup, carboxyl , amino • Translation=RNAto Protein group • Need carboxyl and amino group on the • All linked other end • Link amino acids by forming peptide bonds • Dehydrationsynthesisreaction • Temperature denaturesproteinsthat’s why T is so important • Adultcan go up to 105 • Childrenalittlemore106ish Connects AA andCA groups 20 different amino acids Determine protein function PROTEINSTRUCTURES • Structural levels • Primary • Linear chain; order of amino acids • Secondary • Alpha helix • Screw type • Beta sheet • Crazy ribbon type • All connected byloop conformation • Tertiary • Fully folded 3D • Takesonitsfunctiononce3D • Quaternary • oneamino acidchainngofmorethan • Things likehemoglobinmolecules • assembled togetheraryproteins PROTEINSTRUCTURES • Factors determining protein shape • H bonds • on side chains • Ionic bonds • to side chains • Vander Waals forces • Hydrophobic regions • Covalent linking of side chains • disulfide bondsh AA with • Denaturing agent • Acetic acid, ethanol, formaldehyde • They disrupt protein structure RECEPTORS AND ENZYMES • Proteins havebinding pockets • Receptors bind to ligands • Trigger cell response • Typically this action is to take an existing protein and modify it in some way to either activate or deactivate it. • Enzymes bind to substrates • Generate newproducts RECEPTORS AND ENZYMES • Ligand receptor binding • Ligand= any molecule or ion that is bound to protein • Binding is determinedby both shape and charge • Which is determined by amino acid sequence • Selectivity (specificity) • Is the ability to distinguish btw two ligands with the same shaplarpesims • Allowsprotein to bind to one specific ligand outof hundreds • Zeno estrogens • Is a protein selectivity problem • Because ligands loolikeestrogen so much that they bindour estrogen receptors • Found in the environment now, like plastic in microwave • Outcome is too much estrogen in our bodies • Couldbe the cause of estrogen driven cancers RECEPTORS AND ENZYMES • Proteinbindingaffinity • Tightness of the boding process • Requiredto activate a cell o • High affinity a u • Strongly stuck together a • Intermediate affinity S • Not so strong % • Low affinity • No binding • Less effective at triggering a cellular response Ligand Concentration • As the concentration of ligandgoes up (x) • Percent saturation goes up (y) RECEPTORS AND ENZYMES • Kd • Receptor binding affinity • Kd • concentrationofligandat which halfof the available receptors are bound • Kd decreases as affinity increases • Inversely related • = Affinity up, Kd down Kd Ligand Concentration RECEPTORS AND ENZYMES • Agonist • Antagonist • Molecule or ligandthat binds a • A ligand that binds the receptor but receptor andactivates a cellular doesdoesnot activate the cellular response response • Cannot turn the key • Medically usedto prevent agonists from working CHEMICAL REACTIONRATES • Number of product molecules being produced per unit of time • Influencedby (5) • 1. Reactant concentration t a • 2. Energy of activation n • 3. pH i • Affectsrate c • 4. Temperature e • Affectsspeed R Saturation • 5. Presence of catalyst (enzyme) • Homeostasis allows reactions to be predictable • Enzyme reactions are saturable SubstrateConcentration • If you increase thenumberof enzymesin acell • the enzyme reaction rate goes up • Like addingLucy’shusbandtothe line, it increases upe number of enzymes there to wrap chocolates MODULATION • Allosteric Modulation • Needtwo binding sites in a protein • 1. Functionalsite • where ligand binds • 2. Regulatory site • on off switch • binding of the modulating molecules • changes shape of functional site • Modulation molecules can be inhibitory or stimulatory • Covalent Modulation • 2 sites • 1. Binding site (Functional site) • 2. Phosphorylation site • Strongly negatively charged • Helps change the shape of the protein • Requires 2 enzymes • Kinase • Adds a phosphate to the target protein • Phosphatase • Removes phosphate from target protein END PRODUCTINHIBITION (77) • Negative feedback pathway • Final product of an enzymatic cascade will allosterically (shape wise) inhibit one of the earlier enzymatic steps GLYCOLYSISREGULATION Hexokinase + glucose • Hexokinase • Converts glucose into glucose 6 Glucose 6 inhibits phosphate Glucose 6 • Hexokinase is inhibitedby glucose 6 phosphate ATP inhibits • The very thing it creates Phosphofructokinase + fructose 6 phosphate • Phosphofructokinase • Converts fructose 6phosphate into fructose 1,6biphosphate 1,6 Biphosphate • Phosphofructokinase is Inhibitedby ATP ENERGY PRODUCTION TransitionReaction Krebs Cycle: Glycolysis = glucose with 6 C NADH Oxalocacetaltwo O2 out 2 pyruvate with 3release 2 CO2 FADH2 NADH 2 Acetylco A 2C 6 citrate CELLULAR SIGNALING • Transduction pathway • Cellularsignaling • Cells surface receptorstructure • The diverse sequences of events • Outer ligand binding region btw receptor activation andcellular • Recognizes specific ligand responses • Inner signaling region • Signal= • Receptor activation • Activates or inhibits intracellular • Transduction pathway • Agonist • Stimulus transformed into response • Binds receptors and activates transduction pathway • Antagonist • Binds receptor does not activate transduction • 7 transmembrane spanning regions INTRACELLULARRECEPTOR • Also called steroid hormone receptors • go right through skin bc are lipid soluble • go through cell membrane • associated with controlling your DNA • require lipophilic ligand • Hormone + Receptor= • function as transcription factions • Directly influences gene transcription • hormone response element on DNA control DNA transcription SPECIFICITYOF RESPONSE • we can dump epinephrine in our blood stream and expose all body cells to it • but only a small % of cells will respond bc only those can make the receptor for it • so cells response to agonist of whom they produce a receptor for G PROTEIN • Activatedcell surface commonly • Steps in G protein activation activates G proteins • 1. Ligand bind with receptor • G proteins contain 3 subunits • Receptor changes shape • Alpha, beta gamma • 2. Alpha, Beta, Gamma parts of the G • Alpha protein bind tothe receptor • Can bind GDP and GTP • decreases affinity for GDPonthe • Beta and Gamma alpha subunit • Help anchorthe Alphasubunitinto • 3. GDP dissociates and GTP the membrane associates • Calledactivationofthealphasubunit • 4. Alpha subunit releases beta and gamma subunits • gives ita new shape • 5. Alpha subunit bindseffection enzyme • 6. Adenylyl cyclaseactivated G PROTEINS • Steps Review • These has to be a mechanism to turn this systemoff though • 1. Ligand binds to receptor • 2. Receptor changes shape • if not, once scaredand activated, • 3. Three parts of G proteins bindto you’d be scaredthe your whole life receptor • InactivationofG protein • alpha, beta gamma • alpha has GTPase • 4. Docking • activity converts GTP-GDP • 5. GDP comes off andGTP goes in • alpha subunit rebinds to beta • 6. Activation of alpha subunit systemreset • 7. Alpha subunit changes shape • G PROTEINS • Cholera toxins • Locks in GPT bound form • Pertussis toxin locks in GDP bound form • Whooping cough= pertussis • Causes thick mucus so can’t get it out • Screws up osmotic balance in lungs SIGNAL TRANSDUCTION PROCESS • Signal transduction is the transmission of molecular signals from the extracellular to intracellular. • Signals received by cells must be transmitted into the cell to ensure an appropriate • This step is initiated bycell-surface receptors • Is dependent onan amplification step • Highly amplifiessignal • 1 epinephrineto10kmoleculesof glucose • As you go down the chain you multiply in numbers • Enzymatic cascades • enzyme 1 leads to an activation of multiple enzymes 2s • which then leads to activation of enzyme 3 • so 1x—2 10x---3 100x • in this system kinase enzymes are extremely common • bc kinase is the one off switch • can turn on or off by adding removing phosphate SIGNAL TRANSDUCTIONPROCESS • Is dependent on an amplification step • Highly amplifiessignal • 1 epinephrineto10kmoleculesof glucose • As you go down the chain you multiply in numbers • Enzymaticcascades • enzyme 1 leads to an activation of multiple enzymes 2s • In this system kinase enzymes are extremely common • bc kinase is the one off switch • can turn on or off by addingor removing phosphate CLASSIC PATHWAYS Adenylyl Cyclase • 1. Adenylyl Cyclase • first ever discovered ATP Cyclic AMPdegraded by phosphodiesterase • converts ATP molecule to cyclic AMP 2 P lost • 2 phosphates come off • when you take caffeine it is like Activates protein kinase (PKA) taking a bit of epinephrine shot • exacerbates thispathway Protein phospholization Cell Response CLASSIC PATHWAYS PhospholipaseC • 2. Phospholipase C • secondone discovered PIP2 IP3 DAG Protein kinase C (PKC) Targets endoplasmic reticulum Protein Protein where we store a ton of Ca+ Triggers Once released binds toCalmadelin Muscle contractions Hormone release… Calmadelin kinase Protein Protein CLASSIC PATHWAYS Phospholipase A • 3. Phospholipase A • So Asprin gets rid of Phospholipids Arachidonic Acid pain and inflammation • But also the ability to Cychooxigenase Lypoxygenase clot blockedby Asprin • Thisis agoodthing when we have a heart attack Prostaglandis Thromboxenes Leukotrienes • Chew up Asprin painandinflammation Clotting quick to open up response veins and prevent clotting Short lived <1 minute


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