Abstract
Thyroid hormone is presumed to play a role in initiating and/or orchestrating the postembryonic expression of the genes encoding isoforms of the myosin heavy chains (MHCs) that characterize the muscle fibres in an adult organism. The fact that the postembryonic development of a free-living amphibian tadpole takes place during its thyroid hormone-dependent metamorphosis has made the metamorphosing tadpole an ideal system for elucidating the molecular mechanism(s) by which this hormone affects these postembryonic changes. In this review, we summarize the results from recent studies focused on the postembryonic expression of the MHC genes in the skeletal muscles and hearts of metamorphosing anuran (Rana catesbeiana) tadpoles. The demonstration that mRNAs encoding at least five of the MHC isoforms present in the tadpole tail muscles are also present in the adult hind-limb muscles and that an mRNA encoding a cardiac-specific MHC isoform is present in the heart of both the tadpole and adult organism, rules out the possibility that thyroid hormone initiates the expression of these MHC genes. Instead, it seems more likely that this hormone acts by modulating the expression of one or more of the genes encoding these particular MHC isoforms. Whatever the case, the fact that sequence homology suggests that the five distinct skeletal muscle-specific MHCs are all “fast” isoforms raises the question of how these MHCs are distributed among the three different fibre types described for Rana. On the other hand, the possibility exists that the mRNAs for one or more of these fast MHC isoforms encode developmental isoforms that are present but not translated in the muscles of the tadpole and/or adult frog. Finally, an evaluation of the evolutionary relatedness of the R. catesbeiana MHCs to the MHCs in another species of Rana and to the MHCs in other vertebrates discloses, among other things, that the nucleotide sequence in the R. catesbeiana cardiac MHC isoform is more closely related to the chicken ventricular MHC isoform than it is to any of the other MHC isoforms examined. Microsc. Res. Tech. 50:458–472, 2000. © 2000 Wiley-Liss, Inc.
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