Titin: structure, isoforms and functional regulation.
- Author:
Chun-Jie GUO
1
;
Liang YU
1
;
Yan-Jin LI
1
;
Yue ZHOU
2
Author Information
1. Department of Exercise Physiology, Beijing Sport University, Beijing 100084, China.
2. Department of Exercise Physiology, Beijing Sport University, Beijing 100084, China. chowyue@163.com.
- Publication Type:Journal Article
- MeSH:
Connectin/genetics*;
Muscle Proteins/metabolism*;
Protein Isoforms/genetics*;
Sarcomeres/metabolism*;
Muscle Fibers, Skeletal/metabolism*
- From:
Acta Physiologica Sinica
2023;75(4):544-554
- CountryChina
- Language:Chinese
-
Abstract:
Titin, the largest known protein in the body expressed in three isoforms (N2A, N2BA and N2B), is essential for muscle structure, force generation, conduction and regulation. Since the 1950s, muscle contraction mechanisms have been explained by the sliding filament theory involving thin and thick muscle filaments, while the contribution of cytoskeleton in force generation and conduction was ignored. With the discovery of insoluble protein residues and large molecular weight proteins in muscle fibers, the third myofilament, titin, has been identified and attracted a lot of interests. The development of single molecule mechanics and gene sequencing technology further contributed to the extensive studies on the arrangement, structure, elastic properties and components of titin in sarcomere. Therefore, this paper reviews the structure, isforms classification, elastic function and regulatory factors of titin, to provide better understanding of titin.
