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First published online November 4, 2005
Journal of Experimental Biology 208, 4243-4253 (2005)
Published by The Company of Biologists 2005
doi: 10.1242/jeb.01904

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Expression of eight distinct MHC isoforms in bovine striated muscles: evidence for MHC-2B presence only in extraocular muscles

L. Toniolo¹, L. Maccatrozzo², M. Patruno², F. Caliaro², F. Mascarello^2,* and C. Reggiani¹

¹ Dipartimento di Anatomia e Fisiologia Umana, Università di Padova, Italy
² Dipartimento di Scienze Sperimentali Veterinarie, Università di Padova, Italy

^* Author for correspondence (e-mail: masca{at}unipd.it)

Accepted 28 September 2005

This study aimed to analyse the expression of myosin heavy chain (MHC) isoforms in bovine muscles, with particular attention to the MHC-2B gene. Diaphragm, longissimus dorsi, masseter, several laryngeal muscles and two extraocular muscles (rectus lateralis and retractor bulbi) were sampled in adult male Bos taurus (age 18-24 months, mass 400-500 kg) and analysed by RT-PCR, gel electrophoresis and immunohistochemistry. Transcripts and proteins corresponding to eight MHC isoforms were identified: MHC- and MHC-ß/slow (or MHC-1), two developmental isoforms (MHC-embryonic and MHC-neonatal), three adult fast isoforms (MHC-2A, MHC-2X and MHC-2B) and the extraocular isoform MHC-Eo. All eight MHC isoforms were found to be co-expressed in extrinsic eye muscles, retractor bulbi and rectus lateralis, four (ß/slow, 2A, 2X, neonatal) in laryngeal muscles, three (ß/slow, 2A and 2X) in trunk and limb muscles and two (ß/slow and ) in masseter. The expression of MHC-2B and MHC-Eo was restricted to extraocular muscles. Developmental MHC isoforms (neonatal and embryonic) were only found in specialized muscles in the larynx and in the eye. MHC- was only found in extraocular and masseter muscle. Single fibres dissected from masseter, diaphragm and longissimus were classified into five groups (expressing, respectively, ß/slow, , slow and 2A, 2A and 2X) on the basis of MHC isoform electrophoretical separation, and their contractile properties [maximum shortening velocity (v₀) and isometric tension (P₀)] were determined. v₀ increased progressively from slow to fast 2A and fast 2X, whereas hybrid 1-2A fibres and fibres containing MHC- were intermediate between slow and fast 2A.

Key words: myosin, MHC isoforms, cattle, skeletal muscles, extraocular muscles, laryngeal muscles, RT-PCR, electrophoresis, immunohistochemistry

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