Involvement of SPARC in in vitro differentiation of skeletal myoblasts
Involvement of SPARC in in vitro differentiation of skeletal myoblasts
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DOI：
10.1006/bbrc.2000.2682
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发表时间：
2000-05-19
影响因子：
3.1
通讯作者：
Lim, WK
中科院分区：
文献类型：
--
作者：
Cho, WJ;Kim, EJ;Lim, WK
β-半胱氨酸蛋白（分泌的酸性蛋白，富含半胱氨酸）是一种细胞外钙结合糖蛋白，与多种组织的形态发生和重塑有关。在这里，在骨骼肌成肌细胞的肌发生中的参与，在体外进行了研究。首先，通过差异显示逆转录（DDRT）-PCR方法初步鉴定了肌发生过程中的mRNA差异表达。在C2 C12小鼠成肌细胞的分化过程中，C2 C12基因的表达显著上调。第二，用抗-β-淀粉样蛋白抗体处理几乎完全阻止了成肌细胞的分化。第三，用EGTA（一种已知抑制C2 C12成肌细胞融合的Ca 2+螯合剂）处理可逆地抑制了C2 C12基因表达的上调。另一方面，用A23187（一种Ca 2+离子载体）处理，快速且显著地增加了E10转录物的水平。这些结果提示，在成肌细胞的形态学变化中，Ca 2+依赖性通路可能调控着Ca 2+依赖性基因的表达。(C)北京大学出版社.
SPARC (secreted protein acidic and rich in cysteine) is an extracellular Ca2+-binding glycoprotein associated with the morphogenesis and remodeling of various tissues. Here, involvement of SPARC in the myogenesis of skeletal myoblasts was investigated in vitro. First, the differential expression of SPARC mRNA during the myogenesis was initially identified by a differential display reverse transcription (DDRT)-PCR method. The expression of the SPARC gene was significantly up-regulated during the differentiation of C2C12 mouse myoblasts. Second, the treatment with anti-SPARC antibody almost completely prevented the differentiation of myoblasts. Third, the treatment with EGTA, a Ca2+ chelator that is known to inhibit the fusion of C2C12 myoblasts, reversibly inhibited the up-regulation of SPARC gene expression. On the other hand, the treatment with A23187, a Ca2+ ionophore, rapidly and dramatically increased the level of SPARC transcript. Taken together, these results suggest that SPARC may play a critical role(s) in the morphological change of myoblasts, and that the expression of SPARC gene may be controlled by Ca2+-dependent pathway in myogenesis. (C) 2000 Academic Press.