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Alternative splicing of smooth muscle myosin heavy chains and its functional consequences

✍ Scribed by Hannelore Haase; Ingo Morano

Publisher: John Wiley and Sons
Year: 1996
Tongue: English
Weight: 680 KB
Volume: 60
Category: Article
ISSN: 0730-2312
DOI: 10.1002/(sici)1097-4644(19960315)60:4<521::aid-jcb8>3.0.co;2-u

No coin nor oath required. For personal study only.

✦ Synopsis

The aim of our study was to determine the relation between alternatively spliced myosin heavy chain (MHC) isoforms and the contractility of smooth muscle. The relative amount of MHC with an alternatively spliced insert in the 5 ' (amino terminal) domain was determined on the protein level using a peptide-directed antibody (a25K/50K) raised against the inserted sequence (QGPSFAY). Smooth muscle MHC isoforms of both bladder and myometrium but not nonmuscle MHC reacted with a25/50K. Using a quantitative Western-blot approach the amount of 5'4nserted MHC in rat bladder was detected to be about eightfold higher than in normal rat myometrium. The amount of heavy chain with insert was found to be decreased by about 50% in the myometrium of pregnant rats. Although bladder contained significantly more 5'-inserted MHC than myometrium, apparent maximal shortening velocities (Vmax) were comparable, being 0.138 +-0.012 and 0.114 2 0.023 muscle length per second of skinned bladder and normal myometrium fibers, respectively. Phosphorylation of myosin light chain 20 induced by maximal Ca2+/calmodulin activation was the same in bladder and myometrial fibers. These results suggest that the amount of 5'-inserted MHC is not necessarily associated with contractile properties of smooth muscle.

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