SPARCL1 Influences Bovine Skeletal Muscle-Derived Satellite Cell Migration and Differentiation through an ITGB1-Mediated Signaling Pathway

As an extracellular matrix protein, secreted protein acidic and rich in cysteine (SPARC)-like 1 (SPARCL1) is involved in various cell functions. It was previously implicated in bovine skeletal muscle-derived satellite cell (MDSC) differentiation; however, the underlying mechanism remains unknown. In...

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Bibliographic Details
Published in:Animals (Basel) 2020-08, Vol.10 (8), p.1361
Main Authors: Wang, Yuxin, Liu, Shuaiyu, Yan, Yunqin, Li, Shufeng, Tong, Huili
Format: Article
Language:English
Subjects:
Antibodies
Biotechnology
bovine
Cattle
Cdc42 protein
Cell adhesion & migration
Cell culture
Cell cycle
Cell differentiation
Cells (biology)
Cellular signal transduction
Desmin
Differentiation
Extracellular matrix
Fusion protein
Gene expression
Immunoprecipitation
ITGB1
Kinases
Mass spectrometry
Mass spectroscopy
Matrix protein
migration
Muscles
Musculoskeletal system
MyoD protein
Myotubes
Osteonectin
Paxillin
Physiological aspects
Proteins
Satellite cells
Signal transduction
Skeletal muscle
skeletal muscle-derived satellite cells
SPARCL1
Vinculin
Western blotting
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Summary:As an extracellular matrix protein, secreted protein acidic and rich in cysteine (SPARC)-like 1 (SPARCL1) is involved in various cell functions. It was previously implicated in bovine skeletal muscle-derived satellite cell (MDSC) differentiation; however, the underlying mechanism remains unknown. In this study, immunoprecipitation and mass spectrometry revealed that integrin β1 (ITGB1) combines with SPARCL1. Further, co-immunoprecipitation demonstrated that SPARCL1 interacts with ITGB1. Cell scratch assays explored the influence of SPARCL1 on MDSC migration through ITGB1. In addition, desmin staining for myotube fusion rate and MyoD protein expression results showed that SPARCL1 promotes MDSC early differentiation through ITGB1. Furthermore, Western blotting results demonstrated that SPARCL1 regulates the expression of p-FAK, p-paxillin, vinculin, Cdc42, and Arp2/3 through ITGB1. These findings indicate that SPARCL1 may influence bovine MDSC migration and differentiation through an ITGB1-mediated cell signaling pathway. Herein, we elucidated the mechanism through which SPARCL1 affects MDSC differentiation. Our results provide insight into the molecular mechanism of muscle development and may in the future facilitate skeletal muscle regeneration and treatment.
ISSN:2076-2615
2076-2615
DOI:10.3390/ani10081361