Myosin heavy-chain composition in striated muscle after tenotomy

A. Jakubiec-Puka, T. C. Catani, U. Carraro

Research output: Contribution to journalArticlepeer-review

Abstract

The myosin heavy-chain (MHC) isoform pattern was studied by biochemical methods in the slow-twitch (soleus) and fast-twitch (gastroenemius) muscles of adult rats during atrophy after tenotomy and recovery after tendon regeneration. The tenotomized slow muscle atrophied more than the tenotomized fast muscle. During the 12 days after tenotomy the total MHC content decreased by about 85% in the slow muscle, and only by about 35% in the fast muscle. In the slow muscle the ratio of MHC-I to MHC-2A(2S) remained almost unchanged, showing that similar diminution of both isoforms occurs. In the fast muscle the MHC-2A/MHC-2B ratio decreased, showing the loss of MHC-2A mainly. After tendon regeneration, the slow muscle recovered earlier than the fast muscle. Full recovery of the muscles was not observed until up to 4 months later. The embryonic MHC, which seems to be expressed in denervated adult muscle fibres, was not detected by immunoblotting in the tenotomized muscles during either atrophy or recovery after tendon regeneration. The influence of tenotomy and denervation on expression of the MHC isoforms is compared. The results show that: (a) MHC-1 and MHC-2A(2S) arc very sensitive to tenotomy, whereas MHC-2B is much less sensitive; (b) expression of the embryonic MHC in adult muscle seems to be inhibited by the intact neuromuscular junction.

Original languageEnglish
Pages (from-to)237-242
Number of pages6
JournalBiochemical Journal
Volume282
Issue number1
Publication statusPublished - 1992

ASJC Scopus subject areas

  • Biochemistry

Fingerprint Dive into the research topics of 'Myosin heavy-chain composition in striated muscle after tenotomy'. Together they form a unique fingerprint.

Cite this