Multiple isoforms of myosin light chain 1 in pig diaphragm slow fibers: correlation with maximal shortening velocity and force generation.
Pig diaphragm slow fibers exhibit heterogeneity in myosin light chain 1 (MLC1) isoform expression, with many expressing fast-type MLC1 (MLC1F), as well as two isoforms of slow-type MLC1 (MLC1Sa and MLC1Sb). The goal of this study was to test if there is a relationship between MLC1 isoform expression and contractile properties among these fibers. Maximal shortening velocity (V(max)) and maximal isometric force generation, normalized with fiber cross-sectional area (P(o)/CSA), were measured in single fibers. V(max) was inversely related to the relative level of MLC1Sa. The level of MLC1Sa was reciprocally related to the levels of MLC1Sb and of MLC1F among individual fibers. Fibers expressing MLC1Sa and in which MLC1Sb was not detected generated greater P(o)/CSA, compared to fibers expressing MLC1Sb and not MLC1Sa. The results indicate a complex pattern of MLC1 isoform expression among pig diaphragm slow fibers and suggest that shortening velocity and force generation are modulated, in these fibers, by the MLC1 isoform composition.
Reiser
Peter J
PJ
Oral Biology, Ohio State University, Columbus, OH 43210, USA. reiser.17@osu.edu
Bicer
Sabahattin
S
D000595:Amino Acid Sequence; D000818:Animals; D002478:Cells, Cultured; D003964:Diaphragm / Q000502:physiology* / Q000648:ultrastructure*; D005260:Female; D008969:Molecular Sequence Data; D009119:Muscle Contraction / Q000502:physiology*; D018657:Muscle Fibers, Slow-Twitch / Q000737:chemistry / Q000502:physiology* / Q000648:ultrastructure*; D018994:Myosin Light Chains / Q000737:chemistry / Q000502:physiology* / Q000648:ultrastructure*; D020033:Protein Isoforms / Q000502:physiology / Q000648:ultrastructure; D013223:Statistics as Topic; D013314:Stress, Mechanical; D013329:Structure-Activity Relationship; D013552:Swine
D018994:Myosin Light Chains; D020033:Protein Isoforms; C076659:myosin light chain I