ClAcetyl CoA (2 +2 carbon chain Ca2+ 16 carbon fatty acidcarbon chain) Na+ 6 carbon chain 14 carbon fatty acid

+2 carbon chain Na+ Glucose (6 carbons) 0.5 Na ATPCO2 Low Osm Low Na+ + Na+ 2 NAD+ 0.1 NAD+ isotonic NADH, 2 HighOsm CO Low solute Na+ FADHsolute 2 hypotonic High Na+ + HighNADH + 2 ATPOsm hypertonic X A M C h apters 0.3 Na Nacarbon chain E 1 5 Acetyl CoA solute coA 1: 5 2 NADH High Acetyl Low solute cell swells cell shrinks K + carbon chainP T E R CH Krebs 4 ATPPyruvate 1 4 IntracellularA fluid Intracellular 2 0.3 Osmfluid 0.3 K + Extracellular fluidATP) H2O (net Extracellular fluid physiology ho things ork w and funct ion ATP4 carbon chain (32 w Osm H2O H+ 2 Pyruvate carbons) 0.3 C ounto dy rganization: C otFigure port rans O ert port rans several levels Acetyl CoA B 1 ATP Osm H+ Figure inf funct ion cell of ; class focus proteins is 18 carbonacids& 2 FADH2 3 NADH acid M olecular can luence fatty Am ino Glucose Cellular m olecules m lular for cel units different ; cells special ize into: .. Figure 3 HCO31) m uscle ATP 2) nerve ATP 3) epithel ial ATP 4) connective issue ls t cel ADP Tissue different iated cells with similar propert ies me co together for m issue four to t in ADP classes: ADP Fi gure 4 1) m uscle aids m o ve ment m aterial m in of fro one part the of body another to 2) nerve coordinate and control physiological function 3) epithel m ining ial for l and coverings 4) connective issue holds t things together Organs consists several of kinds t of issues; consists subunits led of cal funct ional units Organ syste ms interact ion organs an of for overal l function ho m eostasis hu man body aintains relat m a ive constant internal environ ment (ex: body te mperature; H p balance; ionic concentrat ion) ho m eostatic control includes range a and point set H o m eostatic e c hanis ms: M negative feedback requires change the a in environ ment happen; to end product a of process inhibi an ts earl step the ier in process regulat ing the mount product a of produced; important m aintaining meostasis seen reflex in ho ; in arcs o reflex arc begins with (1) imulus, hich a a st w is change the in internal external or environ ment; a (2) receptor detects the imulus st producing signal a that ravels t the (3) afferent path way towards the integrat (4) ing center; the signal ravels t the efferent (5) path way way m a fro the integrat ing center the effector here change to (6) w a in act ty ivi produces the response the (7) of syste m posi ive t feedback requires change the a in environ ment happen; to end product a of process that accelerates keeps process or a going (ex: contract ions during th; bir blood clot ing) t feedforward regulat ion anticipates change; a happens before change a (ex: going m fro a hot building cold to outside, body begins shivering before body mperature te drops; s mell ing food anticipat or ing eating, o uth ivates m sal and mach sto begins digest ive secret ions) adaptation change gene in frequency over ime t due select to ion accl matization change physiology i in due longter m to environ mental issues (ex: low sea level to high sea level has less oxygen) crit ical period t ime during develop ment and aturat m ion here w acclimatizat ion per manent is no atter here m w you (ex: go children iving high l in sea level area have puffed out chest and stays even hen o ved low w m to sea level ; adults acquire puffed out chest hen iving high w l in sea level but goes way hen o ved low a w m to sea level)
C H APTER 2

C he mical o n ds: m B fro strongest w eakest to covalent shared electrons; che mical react ions ake m and break bonds o polar unequal distr ibut ion charge; of hydrophil (water ic soluble); ipophobic; l l cel

m e m brane restr icts o ve ment m nonpolar equal distr ibut ion charge; ipophil ( ipid of l ic l soluble); hydrophobic;

m o ves through cell m e m brane easi ly ionic attract ion between cations and anions (ex: C O 3; N a + ; Cl; Ca 2+ ) H hydrogen at tract ion between part charges part ial of icles; important deter mining in biological structure V an der a als important hen ms W w ato are very close together a m p hipathic olecule has polar m a region one at end and larger nonpolar region the at other end; ms for droplets bilayer or Classes O rganic olecules: of M Carbohydrates m ade carbon, of hydrogen, and oxygen the m n(H 2O) n; provides in for C cel l with energy; ater w soluble; o nosaccharide m glucose 6H 12O 6) (C stored the in body as polysaccharide glycogen; glucose fructose + sucrose table ( sugar; disaccharide) Lipids co m posed carbons of and hydrogen; insoluble w ater; in provides source of energy o fatty acids consists a of chain carbon of and hydrogen with carboxyl group the at end; has even m ber carbons nu of saturated ty fat acid no double bonds between carbons the in chain unsaturated ty fat acid one m ore or double bonds between carbons the in chain; one double bond o nounsaturated; ore = m m than one double bond = polyunsaturated t iglyceride r (fat) consists glycerol of and three ty fat acids; provides energy cel for l funct ions; adds padding and insulat ion; important endocrine in syste m function phospholipids consists glycerol of , two ty fat acids and phosphate a group; a mphipathic olecule; m ipid m for l bilayers plas ma in and intercel lular e m brane m steroids consists four of carbon ings r connected together that a is part every of

o o o

steroid Proteins consists carbon, of hydrogen, oxygen, and nitrogen; mposed 20 co of different a mino acids (subunits proteins) of bonded a by peptide bond o peptide bond for med hen w carboxyl group one mino of a acid bonds with mino a

group another; of covalent polypeptide sequence a mino of acids inked peptide l by bonds

all proteins are polypeptides, but l al polypeptides are O T N proteins Protein Structure: 1) primary deter mined nu m ber by and type a mino of acid polypeptide in chain 2) secondary two types: alpha helix and beta sheet; Rgroup a mino of acid luences inf w hich type folding of will take place; four factors deter mine polypeptide folding: hydrogen bonds ionic bonds attraction between nonpolar (hydrophobic) regions covalent bonds 3) ter iary interact t ion between mino a acid Rgroups ms for 3D shape protein of

4) quaternary not l al proteins have this level ; proteins mposed m ore co of than one polypeptide chain (ex: moglobin) he C H APTER 3 Protein Synthesis: regulated process cytoplas m; N A in D contains code a mino for acids m ake to proteins 1) D N A copies R N A ming to for primary N A ranscript R t 2) Splicing occurs moving re introns and keeping exons ming R N A for m o exons part gene of that carries proteincoding infor mation

o o o

introns do not effect protein synthesis coding

3) m R N A o ves m out cel and of l infor mation t is ranslated polypeptide to chain o posttranslational o dification occurs m after polypeptide chain asse mbled is spl t ing it m ethylat ion glycosalat ion covalent o dulat m ion alloster m o dulat ic ion protein degradation control led process mpletely co breaking wn do proteins; used to regulate m ber proteins; r nu of i reversible; caused inappropriate H te mperature by p or denaturing process breaking wn do proteins t ter iary structure but leaving primary

structure intact ; can occur three by different ethods: m changing ionic concentrat ion increasing mperature te changing H p Protein Binding Sites: binding te a a si is locat ion a on protein here l w a igand taches at to inf luence protein functions; there ay several m be binding tes a si on protein; there are four character t of protein is ics a binding te: si 1) Specif ty: ici the select ty a ivi of binding te bind si to specif l ic igands based shape; on there m ay a imited m ber l be l nu of igands a for part icular binding te si (ex: drug that used is to control blood pressure will bind protein to control ing l blood pressure, but ay m also bind to other proteins unrelated pressure) to 2) Affini ease l ty: of igandprotein binding and w ikely l ho l a igand will stay bound a to protein binding te; si charge distr ibut ion luences ini shape inf aff ty; can also influence aff ty ike ini l specif ty; igand ici l concentrat ion aff ty ini 3) Saturat ion: the mount binding tes a of si occupied any at given ime; t the lower the igand l concentrat ion needed bind to half the binding tes si , the higher the affini two ty; factors affect percent saturat ion binding tes: of si o concentration unbound igand the of l in concentrat ion

aff ty binding te the igand ini of si for l

4) C o m peti ion: hen ore t w m than one type l of igand can bind the me to sa binding te; si increased concentrat ion one igand, of l increases chance i of t being bound and reduces the a mount bound the for other igand l R egulation Binding of Site h aracterist C ics: two echanis ms m Alloster M o dulat ic ion: contains two tes here si w noncovalent binding one te of si effects the shape the of second binding te si o functional te carries physiological si out function protein of

regulatory te the igand si l (modulator olecule) m binding this te ters to si al the shape,

thus the activi of ty, the funct ional te; si considered the olecular m switch that controls the functional te al ing ts si by ter i shape and/or affini ty C ovalent o dulat M ion: ter al ing shape and ivi of protein covalent act ty a by bonding of charged che mical groups o phosphorylation che mical react ion covalently taching phosphate at a group (net negative charge) ediated a m by protein kinase protein kinase an enzy me that accelerates the rate react of ion for phosphorylat ion phosphatase enzy me used dephosphorylat in ion re move to phosphate group and return protein original to shape deact by ivat ing t i E nzy mes:proteins with binding tes si called ive tes act si and igands l called substrates; can increase both forward and reverse react ion rates; lowers ivat act ion energy react of ion; two m o dels enzy mesubstrate of interact ion: 1. lockandkey configurat ion 2. induced i o del f tm nonspecif binding w hen l ic a igand binds other to receptors besides the one interest of R egulation E nzy meM e diated eactions: of R substrate concentrat ion al tered cel by lular react ions factors or outside the l cel ; substrate concentrat ion rate enzy mem ediated of react ion

enzy me concentrat ion enzy me concentrat ion rate enzy mem ediated of react ion at any substrate concentrat ion; enzy me concentrat ion al is tered the by rate enzy me of forward synthesis degradation or enzy me ivi act ty can al be tered hen w alloster or ic covalent o dulat m ion alters the propert ies the of enzy mes ive te act si C ell Structure: two ain m parts plas ma e m brane boundary m between extracel lular and intracel lular luid f o phospholipid bilayer co mposed phospholipids of with polar regions the on outside and

nonpolar region the in middle proteins two classes m e m brane of proteins:

o o

integral e m brane m proteins e mbedded within the e m brane; mphipathic; ost m a m are t rans me m brane proteins because they span the entire e m brane m peripheral e m brane m proteins located the e m brane at m surface here w they are bound polar to regions t of rans me m brane proteins the on inside the l of cel ; help with cel l shape and otil ty m i cholesterol polar lat ing ,f r shape; ts nonpolar si in region plas ma e m brane; of m helps m aintain cell f luidi ty glycocalyx consists short of chains sugar of attached the to outside plas ma of m e m brane; enable cells identify to and interact with each other cytoplas m the region inside the l cel (outside the nucleus) containing cell organelles and cytosol o cytosol fluid ion port containing ater w and other atersoluble w proteins

organel les fro m strands proteins co mplex of to structures

m e m branous

nucleus double e m brane; ain m m funct ion storage is and rans mission t of genetic infor mation; contain nuclear pores that lo w al passage large of m olecules mitochondria double e m brane; T P m A production endoplas mic iculu m R) ret (E o rough R riboso mes bound the E are to surface and has lat f tenedsac

appearance; processing proteins m olgi fro G apparatus s mooth R branched, E tubular structure; ipid l synthesis and shortter m calciu m storage

G olgi apparatus f tened lat sacs ming cupshaped for a structure with vesicles that ransport t products out cel (exocytosis) provide of l or storage; o difies m proteins m fro rough R E lysoso mes contains acidic luid f inside and are kno wn recycling as centers; breaks wn do cell debris and dead ls cel ; involved with apoptosis (progra m m ed kil ing cel l of l)

peroxiso mes undergoes react ions moving re hydrogen m ipids, fro l alcohol , and potential toxic ly substances nonm e m branous r iboso mes protein factories the l of cel ; proteins are synthesized here then released into the cytosol i tached rough R, ransferred the olgi or f at to E t to G apparatus then secreted m fro the l to cel or organelles cytoskeleton m ade a i mentous of f la network that aintains m and changes the shape the of cell and produces l o ve ment; cel m three cytoskeletal i ments: f la o microfila ments co m posed contractile of protein in act and y osin m

o o

inter mediate i ments provide f la structural support microtubules co m posed the of protein tubulin; ost igid m r and present in nerve ls cel , centr ioles and mitot spindle important mitosis) ia ic ( in , cil , and f lagel la

M etabolic Path ways Cellular Respirat ion C 6H 12O 6 O 2 A D P P i C O 2 H 2O A T P ; + 6 + 38 + 38 6 + 6 + 38 aerobic; uses oxygen and glucose produce T P to A and carbon; yields A T P m 38 fro three processes o Glycolysis takes place cytosol; in can produce T P A anaerobical fro m ly lactate (replaces

pyruvate) Fig. 1 Krebs ycle takes C place inner mpart ment mitochondria; in co of can only occur in aerobic condit ions; occurs twice per olecule glucose; m of acetyl coenzy me A (acetyl C o A) begins Krebs cycle process with l a inking step (Fig. then 2) continues into the process (Fig. 3) O xidative Phosphorylat ion takes place inner in mitochondrial e m brane; m requires oxygen and cytochro mes funct to ion; yields A T P; 34 produces ater w and A D + N

<amino acids < oxidation

Fat and Protein etabolis m M Fat etabolis m M o Beta xidation 18 O carbon chain can yield 146 T P A

--> we are going to cut off half in doing so we get some NADH, NAD and such. Fat makes you lighter,

o o

Protein and mino cid etabolis m A A M D ea mination an mino a group for med is into keto a acid; produces urea; necessary for an mino a acid be to used cellular in respirat ion t or ransfor med into carbohydrate fat a or Transa minat ion a mino group t is ransferred m a mino fro an acid a to keto acid; cannot produce essential mino a acids

C h a pter 4 M o ve ment M olecules of across ell e m branes C M Passive ransport m o ves t along the gradient (fro m greater concentrat ion lesser to concentrat ion); energy m o ve ment m for fro surroundings with direct no cost cel to l o Diffusion rando m o ve ment m olecules m location another; m of fro one to path of m olecule unpredictable; is will fro m go higher concentrat ion lower to concentrat ion unti l equil ibriu m reached is R ate Diffusion of te mperature rate particle size rate surface area rate gradient rate m olecular interact ion m ediu m of (viscosi ty) ra te semi-permeability per meability rate

Per meabil ty i can through be one l ike cel l the plas ma e m brane a m or layer cel of ls l ike epithel m e m brane; ial o Per meability through layer cells a of can t be ranscel lular through ( the l) cel ;

paracel lular (between the cell) Transcellular ransport controlled m e m brane t is by proteins Paracellular meability regulated t per is by ight junct ions T y pes Diffusion of Si mple diffusion through l a ipid bilayer

passive Transport

N onpolar olecules m diffuse rapidly unlike polar olecules m (ex: oxygen, carbon dioxide, ty fat acids, steroid hor mones) Si mple diffusion through channels

C hannels usual m ade integral e m brane ly of m proteins that m for channels lo wing al ions such N a + ,Cl,K + ,Ca 2+ ,N a + /K pass as to through

small ions, and water can be moved through the channels there is no channel just for waterb

passive Transport

Active

o ( o

C hannels exist open closed in or state process by kno wn channel as gating; three factors deter mine channel gating, effect ing w ho long ho w or often channel a opens: 1. Ligandgated channels binding specif m olecules channel of ic to proteins direct or ly indirect produce ly alloster or ic covalent change shape in 2. V oltagegated channels changes the e m brane in m potential cause o ve ment m of the charged regions, ter al ing ts i shape 3. M echanical lygated channels physical defor ming tretching) ly (s the e m brane m m ay affect confor mation Facil ta i ted diffusion m o ves olecules m m fro higher concentrat ion lower to concentrat ion without T P; A uses ransporter t protein with binding te part si for icular solute m o ve to across e m brane; m has axi mal lux m f A ctive ransport referred as t to ion m ps A T Pase; pu or goes against the gradient (fro m lesser concentrat ion greater to concentrat ion); two types: ,it changes the shape the ATP Pri mary active ransport requires lular t cel use energy m T P Changes the shape of fro A Secondary ive ransport uses act t electroche mical gradient across e m brane; m has m axi mal lux; f has two binding tes: si one the for solute o ving m against the gradient and -sodium ion,theres more sodium outside the cell then inside one driving for the solute 3 sodium out and two potassium in , thus there will be more sodium outside M e diated ransport requires t special ized protein t ( ransporter protein); can passive be or act ive With a mediated transport it will use the same usage of the binding site

is what

the cell

what is a lipid solute?

Fig. 4 cotransport m o ve ment act of ively ransported t solute into the l cel countertransport m o ve ment act of ively ransported t solute out the of cell

E n docytosis and xocytosis doesnt E require olecules pass m to through the e m brane; o ves m m m olecules changing by shape m e m brane of Endocytosis regions plas ma e m brane of m fold into the cell for ming mall s pockets that produce intracel lular e m branebound ,m vesicles that enclose s mall a volu me of extracel lular luid f o phagocytosis bacteria large icles or part engulfed entirely cell by Exocytosis m e m branebound vesicles the in cytoplas m fuse with the plas ma e m brane m and release contents outside the l cel O s m osis diffusion w ater m of fro high concentrat ion low to concentrat ion diffusion m or fro low concentrat ion solute high of to concentrat ion solute of penetrating solute solute that goes through the e m brane; ipid m l soluble; doesnt luence inf w ater o ve ment m nonpenetrating solute solute that does not readi cross e m brane; ly m causes ater o ve ment w m but not solute o ve ment; m do i have a net movement of water ? or do i have a movement of water? os m ol one mol equal 1 ol solute os is to m of part icles O s m olarity total solute concentrat ion; does not offer infor mation about ater o ve ment; w m includes both penetrat ing and nonpenetrat ing solutes the water is going to move in hypoos m otic a solut ion containing less than 0.3 mol/L os solutes and the cell will swell -Hypo isoos m otic a solut ion containing 0.3 mol/L os solutes water is going move out and the cell hyperos m otic a solut ion containing ore m than 0.3 mol/L os solutes which is hyper For nonpenetrating solutes N L Y O
for the three Hyp,iso, and hyperosmotic it has to have a total solute concentration

total solute concentration

will shrink

T o nicity hypotonic concentrat ion nonpenetrat of ing solutes less is than 0.3 mol/L cells os in causing w ater m o ve to into l lo wing t to cel al i swell isotonic nonpenetrat ing solutes not do leave enter or cell because equal of intra and extracel lular luids 0.3 mol/L; net o ve ment f of os no m hypertonic concentrat ion nonpenetrat of ing solutes m ore is than 0.3 mol/L cel causing os in ls w ater m o ve to out cell and t shrinks of i E xa m ples 1. 0.3 M glucose (nonpenetrat ing) 0.3 mol isotonic, os = isoos motic + 2. 0.3 a Cl N 0.3 a 0.3 os mol M N and M Cl 0.6 = hypertonic, hyperos motic 3. 0.3 M urea (penetrat ing) 0.3 mol hypotonic, os = isoos motic

4. 0.3 M urea and 0.3 M glucose 0.3 mol os urea and 0.3 mol glucose isotonic, os of = hyperos motic C h a pter 5 Signal Transduction binding a essenger a of m to receptor protein t ing sequence ini iat a of events leading the to cells response that essenger; to m advantages: 1. signal mplif a icat ion 2. integrat ion and coordinat ion the of response l ipidsoluble essenger receptor m located inside nucleus; used regulate ranscript to t ion and the mount proteins cell a of in w atersoluble essenger receptors m are rans me m brane t proteins; binding tes si on extracel lular side protein; of four types receptors: of 1. l igandgated ion channel receptors increases per meabil ty i 2. receptors that funct ion enzy mes tyrosine as ( kinase) phosphorylates protein inside all 4 of these cel l and changes ts i behavior 3. JA K kinases direct associated ly with e m brane m protein; resul in w ts ne proteins 4. Gproteincoupled receptors Gprotein bound receptor couple t with ion to to i an channel enzy me or f irst essengers che mical essengers m m that bind specif plas ma e m brane to ic m receptors second essengers substances m that enter are or generated cytoplas m a in as resul of t receptor act ivat ion Signal Transduction Path ways C yclic M P 1st essenger binds receptor ivates A m to act G protein act ivates effector protein (adenylyl cyclase) converting T P c A M P nd A to (2 ip3 removes calcium m essenger) ivates A M Pdependent act c protein kinase phosphorylates other enzy mes leading cel response; to ls can terminated enzy me be by phosphodiesterase (A phosphodiesterase (PDE) is any enzyme that breaks a phosphodiester bond.) Protein Kinase 1st essenger binds receptor ivates C m to act G protein act ivates effector protein (phospholipase C) breaking wn do PIP2 D A G to and IP3(2nd essengers) m 1. D A G ivates act protein kinase C phophorylates proteins leading cel response to ls 2. 3 IP binds receptors endoplas mic iculu m to in ret opens 2+ Ca channels releasing t into i cytosol produces ore m events leading the ls cel response C alciu m/cal modulin as nd essenger, 2+ 2 m Ca binds the to protein modulin cal 2+ cal modulin changes shape Ca cal modulin activate inhibi modulin or t cal dependent protein kinases modulindependent cal protein kinases ivate act or inhibi other t proteins Eicosanoid Synthesis 1st essenger binds receptor act m to ivates phospholipase 2 i arachidonic A spl ts acid m e m brane fro m phospholipids m etabolizedby two path ways 1. cyclooxygenase path way O X) (C leads for mation cyclic to of endoperoxides, prostaglandins (vascular actions) and thro mboxanes (blood clot ing t and vascular ions) act 2. l ipoxygenase path way leads for mation leukotrienes to of (mediate lergic al or inf m m atory la react ions)
Calmodulin - is a calcium-binding messenger protein expressed in all eukaryotic cells. CaM is a multifunctional intermediate messenger protein that transduces calcium signals by binding calcium ions and then modifying its interactions with various target proteins

new idea if i have a nerve cell and we move a signal along this. there are two ways / to use. there is a membrane that is used and a synapse on the way what we use is a neuotransmitter <===============* there neuons are long really long so we are going to look at what are these membrane that interest us. there are A) resting, B) Graded , C) Action the resting is preparing to sent the message, or is ready to sent a message if we apply a stimulus it will change from resting to graded so depending on the stimulus the grading period will put it in order either it will have a big change or a small change . if i reach a special number it will reach the ACTION potential that is on the exon it is always the same value and excited to work its an all or none response. so if we start with this resting potential there making a graninet so the Na+/K+ ATPase elctrogemtive makes gradient of Na+/K+ more open K+ channel then Na+ channel which means that there is more posstiaum channels then Na+

we first have to have some Ions that Are trapped inside the cell in a resting potential there is 70mV so we apply the stimulates and get a graded potential so we are going to change the membrane permeability so by opening the Na+ channels we get a depolarization this is called exicitatory then we open K channels k out----> more negative