Muscle type specific expression of tropomyosin isoforms in bovine skeletal muscles
M Oe1, M Ohnishi-Kameyama, I Nakajima
1National Institute of Livestock and Grassland Science, Tsukuba, Ibaraki 305-0901, Japan.
Abstract:
Nucleotide sequences encoding an entire coding region for bovine tropomyosin (TPM) isoforms were determined. Three TPM isoforms, TPM1, TPM2 and TPM3, were expressed in bovine skeletal muscles, and exhibited a 93.3%, 99.6% and 100% amino acid homology to the human sequence, respectively. Based on the sequences, the composition of TPM isoforms was analyzed on cDNA and protein levels from five physiologically different muscles (masseter, diaphragm, psoas major, longissimus thoracis and semitendinosus) using RT-PCR and proteome analyses. Although the content of TPM2 was constantly about 50% of the total TPM in all muscles, the contents of TPM1 and TPM3 were different in muscles according to their function in muscle contraction. In masseter, the content of TPM3 cDNA was about 50% and higher than that of other muscles. In longissimus thoracis and semitendinosus, the contents of TPM1 cDNA were 29.6% and 31.7%, respectively, which were comparatively higher than that of other muscles. The result suggests that the TPM dimer consists of the TPM2 subunit regularly and TPM1 or TPM3 depending on whether the muscle is fast or slow type, respectively.
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