SHANDONG SCIENCE ›› 2017, Vol. 30 ›› Issue (2): 25-36.doi: 10.3976/j.issn.1002-4026.2017.02.005

• Pharmacology and Toxicology • Previous Articles     Next Articles

The research progress of sarcomere assembly

HOU Cai-ping1,2, HAN Li-wen1, HOU Hai-rong1, WANG Xi-min1, ZHANG Shan-shan1,ZHANG Xuan-ming1, WANG Xue1, LI Xiao-bin1, TIAN Qing-ping2, HE Qiu-xia1,2*, LIU Ke-chun1,2*   

  1. 1.Shandong Provincial Engineering Laboratory for Biological Testing Technology, Shandong Provincial Key Laboratory of Biosensors, Institute of Biology,Shandong Academy of Sciences, Jinan 250014,China;2. School of Pharmacology, Shanxi Medical University, Taiyuan 030001, China
  • Received:2016-12-12 Published:2017-04-20 Online:2017-04-20

Abstract:

As the basic contractile unit of striated muscles, sarcomere has a highly ordered structure, which was assembled by Actin, Myosin, and a variety of related proteins. During the assembling process, the correcting assembly of Z belt, M belt, and a series of associated proteins is essential for maintaining movement of muscles, so the study on the mechanism of folding and assembling of sarcomere composition protein is very important for understanding the causes of muscle disease and carrying out targeted therapy. In this paper, the research progress of sarcomere primary components and sarcomere assembling process was reviewed. It was considered that the present studies on sarcomere skeleton assembly, the function of the sarcomere contractile complex, and the relationship between the chaperones and muscle diseases were not deep enough. Therefore, in the future, more studies should be developed on the relationship between Myosin binding protein, Titin, molecular chaperones, and diseases, to find new ideas and solutions to the treatment of muscle related diseases.

Key words: sarcomere, assembling, molecular chaperones, assembling, molecular chaperones, muscle protein, sarcomere, muscle protein

CLC Number: 

  • Q445

Open Access This article is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License (CC BY-NC 4.0), which permits third parties to freely share (i.e., copy and redistribute the material in any medium or format) and adapt (i.e., remix, transform, or build upon the material) the articles published in this journal, provided that appropriate credit is given, a link to the license is provided, and any changes made are indicated. The material may not be used for commercial purposes. For details of the CC BY-NC 4.0 license, please visit: https://creativecommons.org/licenses/by-nc/4.0