Current understanding of conventional and novel co-expression patterns of mammalian sarcomeric myosin heavy chains and light chains.

A central tenet of muscle physiology that has accrued from several decades of intense investigations is that myosin, and the vast set of isoforms that constitute its six subunits, is a major regulator of contractile properties of smooth, cardiac and skeletal muscle. Two frequent questions are (1) how many myosin heavy chain (MyHC) isoforms and myosin light chain (MLC) isoforms are expressed in mammalian striated muscles and (2) which isoforms of MyHC and MLC are expressed, at the protein level, with each other - that is, what patterns of co-expression exist in single striated muscle fibers? The answer to the former question is straightforward: eleven MyHC isoforms and nine MLC isoforms, are expressed in a developmentally-regulated and muscle-specific manner. The answer to the latter question, on the other hand, is not clear-cut. The observed number of MyHC and MLC isoform combinations among single fibers is far less than the total number of potential permutations, indicating strict regulation of expression in individual muscle cells. This article provides a review of the current and still evolving understanding of the complexity of muscle fiber types defined on the basis of expression patterns of MyHC and MLC isoforms that constitute an intact functioning molecule.