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K325CELLBIOLOGYLABORATORY
MuscleContraction
Musclecell
-50 urn
1
Z A I
disk band band

, '---y----' "
Sarcomere ...
A I A I A "

Z ) l'\\_'_
Thinfilament

.:
Thinfilaments Thickfilaments Thinandthick
filamentsin
hexagonalarray
*
Appearanceofcrosssections
Figure132 Org,lftlzatlon0'Slee/eral Musde Cells The
cytoplasm of each muscle cell (muscle fiber) contains
numerous myofibrils whose cross striations are in register.
The ligbt bands (lbands) within the myofibrils contain thin
filaments, whereas tbe dark bands (A bands) contain both
thick and thin filaments. TheZdisks, which run tbrough the
middle ofeach I band, divide tbe myofibril into repeating
units called sarcomeres. Eacb A band contains a central
region, called the H zone, whicb lacks tbtn filaments.
Figures from:
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,. L.J. and V.M. (1995)Principles of Cell and Molecular Biology
(2ndedition). HarperCollmsCollegePublishers,NewYork.
# Wolfe, S.L. (1993)Molecular and Cellular Biology. Wadsworth, Belmont.
1
Figure 1219 Mlcrofllamentsliding in
sarcomerecontraction. (8) Asingle
striated musclesarcomere from frog
semitendinosus muscle. x44,000. Cour-
tesy of J. G. Tidball. (b) Sarcomere
structure in the relaxed state. (c) Sar-
comere under contraction; the thin fila-
ments have slid Inward along the thick
filaments, reducing the width ofthe I
and H bands by an equal distance and
thin zoneofoverlap zoneofoverlap thin
shortening the entire sarcomere.
,1M;;;;'&1 IC$mUU4
,
L (d) Opposite polarity (arrows) of thin fila-

..
ments and myosin crossbrldges. Be-
I.
,, thickfibers /
, /
/
cause of their opposite polarity, the
, /
attach-pull-releasecycle of myosin
a
, /
};-.------- sarcomere-------1'.r
head units pulls the Zlinestogether
and actively shortens the sarcomeres.
---- Aband
I H I
r- band-\ band-----I r- band-\
Z line Mband Z line
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Zline
Zline C-iA of- -h \Ct
06 \.
- -
d
2
S(1M- riCL{;( v e. 0+- -fv\ VVtNl4--cft
(X/y\. \ (\ v IVO
,-
- ------------------_._-
Plasmamembrane
(sarcolemma)
Myofibrils-==------
Openingof
Ttubule
Triad
Terminal
cisterna
-- Sarcoplasmic
Glycogen -----
reticulum
granules
...
\IIZ.. \
t(VYl'Ve.. S c:L+-
$o.Arc.o l .
Aci1CAI\
to
aiJ--
T 1-W?W-4.

'Set yC,O plet

C6c2---T-
l1(/Lc.Jlvd--o -sP-..
<Y:-9+e-v s-nVtA-M.-\a.:hG1A
Vl 0 \,)'e4'
Figure 1316 ThreeDimension,,1 Model Showing the Org"niz"tion of TTubules "lid
S"rtopl",mit Retitu/um in Vertebr"te Ske/et,,'MUlde Note that the T tubules pass from
the cell surface into the cell interior by running down the middle of the I bands, where they
pass betweenflattened channels ofsarcoplasmic reticulum known as terminal cisternae.
' ......
c;o..cM.
Co-Yl"'5lSt-S 0-6 '.

t ..uLc,{A k-Qt\.. )

figure 13-5 Struftur. of Twa 'arms of Myasllt (fop)
*
Electron micrographs and accompanying diagrams /llus-
trating the structural difference between myosin I, which is
Involved in movements In nonmuscle cells, and myosin II,
which Is the main constituent of the thick filaments of mus-
cle cells.Myosin I has a single globular head and a short
tall; myosin II has two globular heads and a long tail.
(Bottom) Diagram showing how protease cleavage Is em-
ployed to cleave myosin II Into fragments. Micrographs
courtesy ofR. E. Cheney andJ. E. Heuser.
4
'Jl., 138' rh. Adln rhln filam.nt (Left) Electron micrograph of a negatively stained
actin filament (Middle)MOdel ofan actin filament sbousng tbe beltcal arrangement of
actin monomers. (Right) Location of tropomyosin and troponin on tbe actin filaments of
muscle cells. Micrograpb courtesy ofH. E. Huxley..
,-' -. '
POk/lM$V"l'}S 10
-fWWl
tJ..- baA'. IIZ+

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22_.2 _1117.a5:'
'-v--'
Longfilament, . , Barezone
*'Figur. 137, filam.nts, 'roduced IJy th. 0''urilled Myosin (fop) Electron
micrograph of negattvely stained sbort filaments produced during myosin polymerization.
The projections at eltber end are tbe globular myosin beads, wbtcb form crossbrldges with
the thin filaments in intact sarcomeres. (Bottom)Schematic representation of the arrange-
ment ofindiVidUal myosin molecules in the short and long filaments generated dUringpoly-
merization. Thesbort filaments consist oftwo sets of overlapping myosin molecules oriented
in opposite directions. Longerfilaments are constructed by the addition of myosin molecules
to both ends, with each newry added molecule always oriented in the same direction as the
molecules already presentat each end. Micrograpb courtesy ofH. E. Huxley.
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Thinfilament (actin)
- 5 4 "'3.... ;'2 i

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s 4 3 2 1

tift;!;:;
Myosinheadbinds
toactinfilament

POWERSTROKE
Changeinconformation
ofmyosinheadcauses
1
slidingofactinfilament

Miiiilii5
"""'" Myosinheadisreleased
.,. fromactinfilament
t
-
S 4 3 2 1


t
Cyclerepeals

AT?
Flgur.1313 1fl.,,,,,,".fII"m."t Mod.'ofMus,'. COIIIr,,"'O" Prior
to contraction, myosin heads containing bound A1P protrude at right
angles from the thick filament. (1) A contraction cycle begins with the
hydrolysis ofATP, generating ADP and Pi molecules that remain bound
to the myosin head. (2) The dissociation of Prfrom myosin Is accompa-
nied by binding of the myosin head to the adjacent actin filament. (3)
DUring-the ensuing power stroke, the myosin head undergoes a confor-
mational change that drives the sliding of the attached actin filament.
At this stage, the myosin heads form crossbridges that lie at a 45angle.
(4) In the final step, ATP binds to the myosin head as ADP Is released,
triggering detachment of the myosin headfrom actin. The net result Is a
ratcbeting mechanism In which myosin heads Induce filament sliding
by progressively engaging successive sites on the adjacent actinfilament.
Note that the sequence of Interactions between myosin and actin closely
parauets the cyclic binding and dissociation that Is observed when purt-
fied actin and myosin are Incubated with ATP (see Figure I3-6).
/ P Thick filament .
Thin filament
e
e
e
e
Zdisk
0
figure 1310 'olarlty 0' t"e r",,, a"d T11ldc Fllame"t.l" a" I"tad S
-- --.
-- DasVtMV\
verses at the Cl!IUer of tbe sarcomere This arran t U artomere Thepolarity of botb types offilaments re-
to move In opposite directions muscle ows the tbtn filaments located on opposite sides of tbe sarcomere
" \\1-1l!'- {-{heN'-s - lInl/\ .v
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-
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q) fA
It C - -+ttAck

-1J ctJ3
c<-cM
L !mls
1
Myosin
light-chain
phosphatase
Myosin Myosin
light-chainkinase light-chainkinase
(inactive) (active)
Figure 1325 Controlof SmoothMuscle Contradion by Myosin LightChain Kinase When the Cal. concentration in the
cytosol rises, Cal. binds to calmodulin and tbe Cal.-calmodulin complex activates myosin light-chain kinase. Theactivated
kinase catalyzes tbe phosphorylation ofa myosin light chain, thereby permitting the myosin molecule to interact with actin
and Initiate contraction. When the Ca" concentration falls. the phosphate group on the myosin light chain Is removed by
myosin lIght-chaln phosphatase. Thedephosphorylated myosin molecule can no longer bind to actin. so the muscle cell relaxes.

!
1Vl\tU \.:?1-hOM of-


ATP cAMP :
protein I protein l
kinase kinase I
(inactive) L(activel l
MLC : MLC
kinase kinase
(active) I (inactive)
: J
. phosphatase_
l
active inactive
crossbridging crossbridging
Figure 12-16 Inhibition of smooth muscle contraction
by hormones triggering cAMP-based regulatory path-
ways (see p. 245for details of the pathways). Attach-
ment of a hormoneto a surface receptor triggers the
synthesis ofcAMP, which activates akinase that adds
phophate groups to MLC kinase. In the phosphorylated
form MLC kinase is inactive, and myosin lightchains
are not phosphorylated even at elevated Ca
2
' concen-
trations. As a result, the crossbridgingcyle is
inhibited. MLC kinase inhibition is reversed by a phos-
phatase presentin smooth muscle cells. The inhibitory
pathway, triggered by l1-adrenergic hormones in higher
vertebrates, produces long-term relaxation of smooth
musclecells.
v:l-

Myosin
light-chainkinase
(inactive)
Myosin
light-chainkinase
(active)
Figure 1325 Controlof SmoothMusde Contradion by Myosin LightChain Kinase When the Ca'" concentration in the
cytosol rises, Ca
l
+ binds to calmodulin and the Ca
l
+-calrnodulin complex activates myosin light-chain kinase. The activated
kinase catalyzes tbe phosphorylation of a myosin light chain, tbereby permitting the myosin molecule to interact with actin
and initiate contraction. When the Ca
2
+ concentration falls, the phosphate group on the myosin light chain is removed by
myosin ugbt-cbat phosphatase. The depbospborylated myosin molecule can no longer bind to actin, so the muscle cell relaxes.

!
IVl \tU 't/lIt of

I\A v-o-Cv-u- CAM?..
ATP cAMP
I
I
protein I protein i
kinase kinase I
(inactive) (active) I
MLC I : MLC
kinase kinase
(active) I (inactive)
: j
. phosphatase.
t
active inactive
crossbridging crossbridging
Figure 1216 Inhibition of smooth musclecontraction
by hormones triggering cAMP-based regulatory path-
ways (see p. 245for details of the pathways). Attach-
ment of a hormone to a surface receptor triggers the
synthesis of cAMP, which activates akinase that adds
phophate groups to MLC kinase. In the phosphorylated
form MLC kinase is inactive, and myosin lightchains
are not phosphorylated even at elevated Ca
2
+ concen-
trations. As a result, the crossbridging cyle is
inhibited. MLC kinase inhibition is reversed by a phos-
phatase present in smooth muscle cells. The inhibitory
pathway, triggered by p-adrenergic hormones in higher
vertebrates, produces long-term relaxation of smooth
musclecells.