PUBLICATION
TM4SF5 suppression disturbs integrin α5-related signaling and muscle development in zebrafish
- Authors
- Choi, Y.J., Kim, H.H., Kim, J.G., Kim, H.J., Kang, M., Lee, M.S., Ryu, J., Song, H.E., Nam, S.H., Lee, D., Kim, K.W., Lee, J.W.
- ID
- ZDB-PUB-140605-1
- Date
- 2014
- Source
- The Biochemical journal 462(1): 89-101 (Journal)
- Registered Authors
- Keywords
- none
- MeSH Terms
-
- Animals
- Cell Differentiation
- Cell Movement
- Cells, Cultured
- Epithelial-Mesenchymal Transition
- Integrin alpha5/biosynthesis
- Integrin alpha5/physiology*
- Membrane Proteins/biosynthesis
- Membrane Proteins/genetics*
- Mice
- Muscle Development/physiology*
- Signal Transduction/physiology
- Somites/metabolism
- Zebrafish/embryology
- PubMed
- 24897542 Full text @ Biochem. J.
Citation
Choi, Y.J., Kim, H.H., Kim, J.G., Kim, H.J., Kang, M., Lee, M.S., Ryu, J., Song, H.E., Nam, S.H., Lee, D., Kim, K.W., Lee, J.W. (2014) TM4SF5 suppression disturbs integrin α5-related signaling and muscle development in zebrafish. The Biochemical journal. 462(1):89-101.
Abstract
TM4SF5 is involved in epithelial-mesenchymal transition (EMT) for liver fibrosis and cancer metastasis. However, the function(s) of TM4SF5 during embryogenesis remains unknown. Here the effects of TM4SF5 on embryogenesis of zebrafish were investigated. tm4sf5 mRNA was expressed in posterior somites during somitogenesis and in whole myotome 1 dpf. tm4sf5 suppression impaired development of the trunk with aberrant morphology of muscle fibers and altered expression of integrin a5. The arrangement and adhesion of muscle cells were abnormally disorganized in tm4sf5 morphants with reduced muscle fiber masses, where integrin α5-related signaling molecules including fibronectin, FAK, vinculin, and actin were aberrantly localized, compared with those in control fishes. Aberrant muscle developments in tm4sf5 morphants were recovered by additional tm4sf5 or integrin α5 mRNA injection. Such a role for TM4SF5 was observed in the differentiation of C2C12 mouse myoblast cells to multinuclear muscle cells. Altogether, the results show that TM4SF5 controls muscle differentiation via cooperation with integrin α5-related signaling.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping