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Chok Biochem 4th Shift Reviewer Muscle

Chok Biochem 4th Shift Reviewer Muscle

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Published by: api-3742802 on Oct 15, 2008
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03/18/2014

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MUSCLE METABOLISM
Group
Muscle Protein
Notes
Major
Myosin (M)
most important, 65% of weight, thickfilaments, 2 identifcal heavy chains (forms superhelix) with a
globular head at N terminus and 4 light chains (at globular heads), binds other myosin molecules,
binds actin filaments,AT Pase activity
Actin (A)
thin filaments, 20-25% of muscle proteins, 2 strands of polymerized monomers
Tropomyosin (Tm)
2 \u03b1 helical chains wound along actin groove, blocks myosin binding site in relaxed muscle
Troponin (Tn)
three subunits (TnC \u2013 Ca binding,TnI \u2013 binds actin,TnT \u2013 binds tropomyosin), in thin filament,
regulator of muscle contraction
Minor
Associated
with Z disk
\u03b1-actinin
binds to ends of actin filaments, may attach them to Z disk
Desmin & Vimentin
at A disk periphery, keep adjacent myofibrils in lateral register
Titin
largest polypeptide known, extends from thick filament to Z disk, acts as spring to keep thick filament
centered in sarcomere, may control length of thick filaments
Nebulin
repeating 35-residue acting binding motif, predicted to be \u03b1-helical
Associated
with M disk
C & M proteins
participate in thick filament assembly
Dystrophin
inner surface of muscle membrane, anchor specific membrane glycoproteins in RBC
Duchenne Muscular Dystrophy (DMD)
Becker Muscular Dystrophy (BMD)

2-5 years, degeneration exceeds regeneration, death at 20 y/o,
usually no dystrophin
Mutation @ C-terminus or actin binding region

5-10 years, less progression, longer lifespan,
altered or semifunctional dystrophin
Mutation @ \u03b1 helix (shortening)

Organization of Striated Muscle
\ue000Muscle\ue001 bundle of muscle fibers\ue001 muscle fiber\ue001 myofibril\ue001 sarcomere
\ue000
Sarcomere:
Z disk
A Band
H band
I band
M disk
Z\ue001 Z = sarcomere
Electron dense, thick + thin filaments
Thick filaments
2x actin, thin filaments
Middle of sarcomere
\ue000
Sliding Filament Model \u2013 thin slides over thick filaments, A bands remain constant, I bands contract, Z disks approach each other
\ue000
Crossbridge cycle

1. ATP binding \u2013 ATP binds to myosin, A-M bridge rapidly dissociates
2. ATP hydrolysis \u2013 Free myosin moves into position to attach to actin, ATP hydrolyzed but does not release ADP + Pi
3. A-M binding \u2013 Myosin rebinds to actin

4.Powerstroke \u2013 actin displaces Pi then ADP from myosin, myosin heads bend (stroke), ready to ATP binding
o
Each powerstroke of 500 myosin heads = 10 nm contraction
o
During strong contraction, powerstroke repeated 5 times / second
o
Mn2+ as cofactor
\ue000
Sequence: Action potential\ue001 Ach release\ue001 Depolarization\ue001 opening of Ca channels\ue001 \u2191 ICF Ca\ue001 Ca binds to TnC\ue001 Tm reveals binding site
\ue001 Crossbridge cycle \ue001contraction \ue001 Ca returns to SR \ue001TnC releases Ca \ue001Tm covers binding site \ue001relaxation
\ue000
Regulation by calcium
o
Ca + TnC\ue001 Tn drags Tm 10 \u00c5\ue001 binding site revealed\ue001 myosin binds
\ue000
Sarcoplasmic Reticulum \u2013 Ca reuptake via:
o
calsequestrin \u2013 lots of negative AA
o
calcium ATPase pump \u2013 pumps Ca into SER
Muscle Energy Production
\ue000
Principal task \u2013 perform mechanical energy at the expense of ATP
\ue000
ATP synthesis from glucose, fatty acids, ketone bodies
\ue000During light exercise \u2013 glucose\ue001 CO2, H2O
\ue000
Muscle contraction increases O2 consumption, especially cardiac muscle
\ue000
ATP Generation Pathways
Creatine Phosphate
Aerobic respiration
Anaerobic respiration
Pathway
Uses creatine kinase
Glucose + O2\ue001 ATP + H2O
Glycolysis\ue001 pyruvate
ATP
generation
Quickly exhausted, reversible,
replenished during rest
20x more ATP than anaerobic
2.5x faster than aerobic
Usage
1st used, short periods (10-15s)long term source (>40s), resting/slowly-active
muscle, with FA, glucose / glycogen if very active
Used in moderate period (30-40s) of strenuous
activity, long term use = \u2191 lactic acid
\ue000
Energy Metabolism
o
Rapid ATP replenishment \u2013 creatine phosphate + ADP + creatine kinase\ue001 ATP + creatine
o
ADP + adenlyate kinase (myokinase)\ue001 ATPand AMP
o
AMP + AMP deaminase\ue001 IMP; to pull equilibrium of reaction in favorable direction
o
Glycogen \u2013 most important long term reserve
\ue000
Degradation \u2013 activated byepinephrine viac AMP\ue001 activation of phoshorylase kinase\ue001 glycogen phosphorylase

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