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Correlation between the protein and mRNA levels for myosin light chains and tropomyosin subunits during chick fast muscle development in vivo
Author(s) -
Roy Raman K.,
Sarkar Satyapriya
Publication year - 1982
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(82)81063-6
Subject(s) - tropomyosin , myosin , myofibril , gene isoform , myosin light chain kinase , skeletal muscle , immunoglobulin light chain , messenger rna , in vivo , myh7 , chemistry , biology , actin , microbiology and biotechnology , biochemistry , gene , anatomy , genetics , antibody
Using myosin light chains and tropomyosin subunits as representative myofibrillar proteins, we have characterized their isoprotein forms and also correlated them with the accumulation of the corresponding mRNAs during development of a fast muscle in chicken, viz, pectoralis. Both slow and fast myosin light chain isoforms, except fast myosin light chain LC 3 , and the two subunits of tropomyosin are present in early embryonic muscle. During development, the slow myosin light chains and β‐tropomyosin appear in reduced amounts in pectoralis muscle and finally they disappear in adult muscle. Translation studies with total cellular RNA from developing muscle indicates that while the protein levels of the above isoforms, in general, correlate with the accumulation of corresponding mRNAs, for LC 3 , additional post‐transcriptional control appears to modulate the expression of this isoprotein skeletal muscle development in vivo.