PUBLICATION
Complete primary structure of the I-band region of connectin at which mechanical property is modulated in zebrafish heart and skeletal muscle
- Authors
- Hanashima, A., Hashimoto, K., Ujihara, Y., Honda, T., Yobimoto, T., Kodama, A., Mohri, S.
- ID
- ZDB-PUB-161013-11
- Date
- 2017
- Source
- Gene 596: 19-26 (Journal)
- Registered Authors
- Keywords
- Connectin, Heart, Molecular evolution, Muscle, Titin, Zebrafish
- MeSH Terms
-
- Alternative Splicing
- Amino Acid Sequence
- Animals
- Connectin/chemistry*
- Connectin/genetics
- Connectin/metabolism
- Evolution, Molecular
- Humans
- Mice
- Muscle, Skeletal/metabolism*
- Myocardium/metabolism*
- Phylogeny
- Protein Domains
- Protein Isoforms/chemistry
- Protein Isoforms/genetics
- Protein Splicing
- Sarcomeres/metabolism
- Zebrafish
- Zebrafish Proteins/chemistry*
- Zebrafish Proteins/genetics
- PubMed
- 27725266 Full text @ Gene
Citation
Hanashima, A., Hashimoto, K., Ujihara, Y., Honda, T., Yobimoto, T., Kodama, A., Mohri, S. (2017) Complete primary structure of the I-band region of connectin at which mechanical property is modulated in zebrafish heart and skeletal muscle. Gene. 596:19-26.
Abstract
Connectin, also called titin, is the largest protein with a critical function as a molecular spring during contraction and relaxation of striated muscle; its mutation leads to severe myopathy and cardiomyopathy. To uncover the cause of this pathogenesis, zebrafish have recently been used as disease models because they are easier to genetically modify than mice. Although the gene structures and putative primary structures of zebrafish connectin have been determined, the actual primary structures of zebrafish connectin in heart and skeletal muscles remain unclear because of its large size and the PCR amplification-associated difficulties. In this research, using RT-PCR amplification from zebrafish heart and skeletal muscles, we determined the complete primary structures of zebrafish connectin in the I-band region at which mechanical property is modulated by alternative splicing. Our results showed that the domain structures of zebrafish connectins were largely similar to those of human connectins; however, the splicing pathways in the middle-Ig segment and the PEVK segment were highly diverse in every isoform. We also found that a set of 10 Ig domains in the middle-Ig segment of zebrafish connectin had been triplicated in human connectin. Because these triplicate regions are expressed in human leg and diaphragm, our findings may provide insight into the establishment of walking with limbs and lung respiration during tetrapod evolution.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping