Abstract
Abstract By applying immunocytochemistry using monoclonal antibodies, we found that the myofibrillar M band of both presumptive type-I and -II fibers in the pectoralis major muscle of chickens contains two high-molecular-weight proteins, i.e., myomesin ( M r, 185000) and M protein ( M r, 165000), early in embryonic development (7 days in ovo), even though adult type-I fibers lack M protein. The developmental expression of M protein is unusual in that, from 10 to 14 days in ovo, it is gradually suppressed not only in presumptive type-I fibers but also in presumptive type-II fibers formed from primary-generation myotubes. This latter suppression is transient, as M protein is expressed in all adult type-II fibers derived from both the primary- and second-generation myotubes. Myomesin, on the other hand, is continuously expressed in all myotubes throughout development. This finding shows that myomesin and M protein expression is regulated independently in different myotube populations, and that the suppression of M protein in primary-generation myotubes accounts for the delayed accumulation of M protein during development, as previously revealed by biochemical analysis. Presumptive type-I fibers, which form in the deep portion of the muscle, become concentrated in a narrow band known as the red strip.
Published Version
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