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1 Department of Physiology and Biophysics, Case Western Reserve University School of Medicine, Cleveland, Ohio 44106-4970; and 2 Department of Veterinary and Comparative Anatomy, Pharmacology, and Physiology, Washington State University, Pullman, Washington 99164-6520
Developmentally
regulated alternative RNA splicing generates distinct classes of acidic
and basic troponin T (TnT) isoforms. In fast-twitch skeletal muscles,
an acidic-to-basic TnT isoform switch ensures basic isoform expression
in the adult. As an exception, an acidic segment in the
NH2-terminal variable region of
adult chicken breast muscle TnT isoforms is responsible for the unique exclusive expression of acidic TnTs in this muscle (O. Ogut and J.-P.
Jin. J. Biol. Chem. 273:
27858-27866, 1998). To understand the relationship between acidic
vs. basic TnT isoform expression and muscle contraction, the
contractile properties of fibers from adult chicken breast muscle were
compared with those of the levator coccygeus muscle, which expresses
solely basic TnT isoforms. With use of Triton X-100-skinned muscle
fibers, the force and stiffness responses to
Ca2+ were measured. Relative to
the levator coccygeus muscle, the breast muscle fibers showed
significantly increased sensitivity to
Ca2+ of force and stiffness with a
shift of ~0.15 in the pCa at which force or stiffness was 50% of
maximal. The expression of tropomyosin, troponin I, and troponin C
isoforms was also determined to delineate their contribution to
thin-filament regulation. The data indicate that TnT isoforms differing
in their NH2-terminal charge are
able to alter the sensitivity of the myofibrillar contractile apparatus to Ca2+. These results provide
evidence linking the regulated expression of distinct acidic and basic
TnT isoform classes to the contractility of striated muscle.
alternative ribonucleic acid splicing; developmental regulation; calcium; activation of force and stiffness; tropomyosin
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