Abstract
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.
Highlights
SPARC, as a member of the secreted protein acidic and rich in cysteine (SPARC) family of acidic secretory glycoprotein, is known in a variety of cell functions, including cell proliferation, cell turnover, cell differentiation and tissue repair [1,2,3]
We hypothesized that SPARCL1 may interact with ITGB1 and play a role in muscle-derived satellite cell (MDSC) differentiation
The anti-SPARCL1 antibody was used for immunoprecipitation followed by Western blotting with the anti-ITGB1 antibody (Figure 1A) or vice versa (Figure 1B)
Summary
SPARC (osteonectin or BM-40), as a member of the secreted protein acidic and rich in cysteine (SPARC) family of acidic secretory glycoprotein, is known in a variety of cell functions, including cell proliferation, cell turnover, cell differentiation and tissue repair [1,2,3]. SPARC has been reported to play important roles in skeletal muscle myoblast differentiation [4,5]. 1, known as ECM2, Hevin, MAST 9, or SC1), belongs to SPARC family of matricellular proteins, it shares a follistatin-like module and an extracellular Ca2+ binding domain in that of SPARC in mouse [6]. Animals 2020, 10, 1361 played important roles in C2C12 cell differentiation and bovine skeletal muscle-derived satellite cells (MDSCs) differentiation [7,8].
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