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Journal of Histochemistry and Cytochemistry, Vol. 51, 471-478, April 2003, Copyright © 2003, The Histochemical Society, Inc.

ARTICLE

Biochemical and Immunohistochemical Evidence for a Non-muscle Myosin at the Neuromuscular Junction in Bovine Skeletal Muscle

Elena Pompilia, Antonio De Lucab, Stefania L. Noric, Bruno Marasd, Gabriella De Renzisc, Fulvia Ortolanie, and Lorenzo Fumagallia
a Department of Cardiovascular Sciences, University La Sapienza, Rome, Italy
b Institute of Topographical Anatomy, Second University of Naples, Naples, Italy
c Institute of Human Anatomy, Catholic University, Rome, Italy
d Department of Biochemical Sciences, University La Sapienza, Rome, Italy
e Department of Medical and Morphological Research, University of Udine, Udine, Italy

Correspondence to: Elena Pompili, University “La Sapienza,” Dept. of Cardiovascular Sciences, Via A. Borelli 50, 00161 Rome, Italy. E-mail: elena.pompili@uniroma1.it

We identified 220-kD protein in bovine skeletal muscle homogenate by affinity chromatography on an agarose column and subsequent SDS-PAGE. Peptide mass fingerprinting (MALDI mass spectrometry) and internal sequence analysis revealed that this protein has homology with several members of the myosin superfamily, particularly with human cardiac ß-myosin heavy chain (ß-MHC). A rabbit polyclonal antibody against the 220-kD protein specifically stained a 220-kD band in Western blots of skeletal muscle homogenate. Immunohistochemical experiments on cryostat sections demonstrated that in skeletal muscle this protein is exclusively localized at the neuromuscular junctions, no immunoreactivity being present at the myofibril level. Because of its relative homology with cardiac ß-MHC, we also investigated the distribution of the 220-kD protein in bovine heart. In cardiac fibers, 220-kD protein-related immunoreactivity was restricted to the intercalated disks, whereas myofibrils were completely devoid of specific immunoreactivity. This distribution pattern was completely different from that of cardiac ß-MHC, which involved myofibrils. Because of the above biochemical and immunohistochemical features, the 220-kD protein we have identified is suggested to be a novel member of the non-muscle (non-sarcomeric) myosin family. (J Histochem Cytochem 51:471–478, 2003)

Key Words: non-muscle myosin heavy, chain, immunohistochemistry, neuromuscular junction


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