OTOT

Drs. ARIF KUSWIRASASONO

JL. SULAWESI UTARA IA/7 (0321)862700
E-mail : arifkuswiro@yahoo.co.id

SISTEM MUSKULARIS
Gerak salah satu ciri hewan
Otot berperan dalam sistem gerak
didukung struktur yang kuat tapi lentur.
Materi intraselualar yang didominasi oleh
filamen-filamen aktin dan myosin
kontraksi dan relaksasi)
Jika semua unit motoris secara bersamaan
berkontraksi sehingga mampu menarik tulang
yang berhubungan dengannya, maka terjadi
suatu gerakan.

Biology
TRAININ
ITS

Copyright 2005 Program Studi Biologi ITS Surabaya

BACK

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a. Sarkolema
b. Sarkoplasma,
c. Miofibril
tersusun atas
Filamen
(myofilamen) Aktin
dan Miosin
d. Mitokondria
e. Retikulum
sarkoplasmik

BACK

Hubungan neuromuskular

Struktur Otot Saat Relaksasi

Mekanisme Kerja Otot

Meski struktur otot berbeda namun mekanisme
dasar kontraksi tetaplah sama, yaitu
melalui pertautan antar myofilamen (f. aktin
dan f. myosin )

Biology
TRAININ
ITS

Copyright 2005 Program Studi Biologi ITS Surabaya

 A pair of tropomyosin molecules is associated with

every 7 pairs of G-actin residues along a thin filament
each tropomyosin molecule covers the myosin binding
sites of 7 G-actin residues, preventing interaction
between actin and myosin and thus maintaining the
relaxed state.
troponin, the second accessory protein of thin filaments.
Troponin is attached to one end of each tropomyosin
molecule and to actin, physically linking tropomyosin to
actin.
One of the troponin subunits, troponin-C (Tn-C), is a
calcium-binding protein

 When Tn-C binds calcium, the whole

troponin molecule undergoes the
conformational change that moves the
attached tropomyosin away from the
myosin binding sites on actin. This event
permits nearby myosin heads to interact
with myosin binding sites

Events on the thin filament can be

summarized as follows:
Prior to the appearance of free calcium in the
sarcoplasm, tropomyosin covers the myosin binding
sites on actin.
The appearance of calcium in the sarcoplasm leads to
calcium binding on Tn-C. The resulting conformational
changes in troponin move the attached tropomyosin
molecule more deeply into the helix groove of F-actin,
uncovering the myosin binding sites on G-actin subunits.
The exposed sites are then available to interact with
myosin headpieces.
Removing calcium from the sarcoplasm restores the
original conformational states of troponin and
tropomyosin, preventing interaction between actin and
myosin and leading to the relaxed state.

Regulation of Sarcoplasmic Calcium

Events that stimulate muscle activity by raising sarcoplasmic

calcium begin with neural excitation at neuromuscular junctions.
Excitation induces local depolarization of the sarcolemma, which
spreads to the associated T tubule system and deep into the interior
of the myofiber.
T tubule depolarization spreads to the sarcoplasmic reticulum (SR),
with the effect of opening voltage-gated calcium channels in the SR
membranes.
This is followed by massive, rapid movement of cisternal calcium
into the sarcoplasm close to nearby myofibrils.
The appearance of calcium very close to the Tn-C subunit of
troponin results in the production of multiple myosin power strokes
RELAXATION --sarcoplasmic calcium is pumped back into the SR
cisternae by an extremely active ATP- driven calcium pump, which
comprises one of the main proteins of the SR membrane.

OTOT
JANTUNG