alexa Does Nebulin Make Tropomyosin Less Dynamic in Mature Myofibrils in Cross- Striated Myocytes?
ISSN: 2157-7099

Journal of Cytology & Histology
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Mini Review

Does Nebulin Make Tropomyosin Less Dynamic in Mature Myofibrils in Cross- Striated Myocytes?

Dube DK*, Wang J, Fan Y, Sanger JM and Sanger JW

Department of Cell and Developmental Biology, SUNY Upstate Medical University, 750 East Adams Street, Syracuse, NY, USA

*Corresponding Author:
Dipak K Dube
Department of Cell and Developmental Biology
SUNY Upstate Medical University, 750 East Adams Street
Syracuse, NY 13210, USA
Tel: 315-464-8563
Fax: 315-464-8255
E-mail: [email protected]

Received date: February 20, 2014; Accepted date: April 23, 2014; Published date: April 25, 2014

Citation: Dube DK, Wang J, Fan Y, Sanger JM, Sanger JW (2014) Does Nebulin Make Tropomyosin Less Dynamic in Mature Myofibrils in Cross-Striated Myocytes?. J Cytol Histol 5:239. doi:10.4172/2157-7099/1000239

Copyright: © 2014 Dube DK, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

 

Abstract

Myofibrils in vertebrate cardiac and skeletal muscles are characterized by groups of proteins arranged in contractile units or sarcomeres, which consist of four major components – thin filaments, thick filaments, titin and Zbands. The thin actin/tropomyosin-containing filaments are embedded in the Z-bands and interdigitate with the myosin-containing thick filaments aligned in A-bands. Titin is attached to the Z-band and extends upto the middle of the A-Band. In this mini review, we have addressed the mechanism of myofibril assembly as well as the dynamics and maintenance of the myofibrils in cardiac and skeletal muscle cells. Evidence from our research as well as from other laboratories favors the premyofibril model of myofibrillogenesis. This three-step model (premyofibril to nascent myofibril to mature myofibril) not only provides a reasonable mechanism for sequential interaction of various proteins during assembly of myofibrils, but also suggests why the dynamics of a thin filament protein like tropomyosin is higher in cardiac muscle than in skeletal muscles. The dynamics of tropomyosin not only varies in different muscle types (cardiac vs. skeletal), but also varies during myofibrillogenesis, for example, premyofibril versus mature myofibrils in skeletal muscle. One of the major differences in protein composition between cardiac and skeletal muscle is nebulin localized along the thin filaments (two nebulins/thin filament) of mature myofibrils in skeletal muscle cells, but which is expressed in a minimal quantity (one nebulin/50 actin filaments) in ventricular cardiomyocytes. Interestingly, nebulin is not associated with premyofibrils in skeletal muscle. Our FRAP(Fluorescence Recovery After Photobleaching) results suggest that tropomyosin is more dynamic in premyofibrils than in mature myofibrils in skeletal muscle, and also, the dynamics of tropomyosin in mature myofibrils is significantly higher in cardiac muscle compared to skeletal muscle. Our working hypothesis is that the association of nebulin in mature myofibrils renders tropomyosin less dynamic in skeletal muscle.

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