Literature DB >> 16884681

Multiple isoforms of myosin light chain 1 in pig diaphragm slow fibers: correlation with maximal shortening velocity and force generation.

Peter J Reiser1, Sabahattin Bicer.   

Abstract

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.

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Year:  2006        PMID: 16884681     DOI: 10.1016/j.abb.2006.06.013

Source DB:  PubMed          Journal:  Arch Biochem Biophys        ISSN: 0003-9861            Impact factor:   4.013


  4 in total

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Journal:  FASEB J       Date:  2011-02-24       Impact factor: 5.191

4.  Myosin essential light chain 1sa decelerates actin and thin filament gliding on β-myosin molecules.

Authors:  Jennifer Osten; Maral Mohebbi; Petra Uta; Faramarz Matinmehr; Tianbang Wang; Theresia Kraft; Mamta Amrute-Nayak; Tim Scholz
Journal:  J Gen Physiol       Date:  2022-09-02       Impact factor: 4.000

  4 in total

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