Myosin heavy chain composition of single cells from avian slow skeletal muscle is strongly correlated with velocity of shortening during development.
We have determined the myosin heavy chain (MHC) composition (using a sensitive sodium dodecyl sulfate-polyacrylamide gel electrophoresis system) and the maximal velocity of shortening (Vmax) of single cells from neonatal and adult chicken anterior latissimus dorsi (ALD) muscles. In addition, the MHC, myosin light chain, and regulatory protein (i.e., troponin and tropomyosin subunits) compositions of bundles of ALD fibers were determined at late embryonic, neonatal, and adult ages. At young ages, there are two MHCs in ALD muscle, SM1 and SM2, with SM1 decreasing in relative amount with increasing age, as shown previously by others. The mean Vmax of single fibers also decreases from neonatal to adult ages. A strong quantitative correlation is demonstrated between the specific MHC composition and Vmax among individual cells of the ALD muscle at several ages. Since virtually no changes occur in the regulatory protein and myosin light chain compositions of the ALD muscle between late embryonic and adult ages, it appears that the MHC composition of an individual cell in this muscle is the primary determinant of the maximal shortening velocity. These results are the first to illustrate the functional significance of the developmental transition in myosin heavy chain composition of an avian slow skeletal muscle, consistent with our previous findings on mammalian muscle.
Department of Physiology, School of Medicine, University of Wisconsin, Madison 53706.
P J
PJ
Reiser
M L
ML
Greaser
R L
RL
Moss
D000818:Animals; D002645:Chickens; D004591:Electrophoresis, Polyacrylamide Gel; D007700:Kinetics; D009132:Muscles / Q000201:enzymology*; D009218:Myosins / Q000032:analysis*
D009218:Myosins