REGULATION OF INTEGRIN ALPHA-5-BETA-1 AFFINITY DURING MYOGENIC DIFFERENTIATION
REGULATION OF INTEGRIN ALPHA-5-BETA-1 AFFINITY DURING MYOGENIC DIFFERENTIATION
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DOI：
10.1006/dbio.1995.1142
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发表时间：
1995-05-01
影响因子：
2.7
通讯作者：
CHIQUETEHRISMANN, R
中科院分区：
文献类型：
--
作者：
BOETTIGER, D;ENOMOTOIWAMOTO, M;CHIQUETEHRISMANN, R
鸡整合素纤维连接蛋白受体α链单克隆抗体U1 α识别的抗原鉴定为α 5。它能识别与抗血清相同的多肽，从α 5细胞质结构域提升到一个序列。U1 α抗体具有不同寻常的α链抗体的功能特性，增强α 5 β 1与其配体纤维连接蛋白的结合。用U1 α检测α 5 β 1在肌原性分化过程中的功能。当肌源性细胞从复制型成肌细胞分化为双极性肌细胞时，α 5 β 1的失活导致它们与底物的粘附减少，这可以通过U1 α处理细胞来逆转。U1 α诱导纤维连接蛋白的粘附增加，但不抑制分化过程，通过肌管的形成来测量。然而，U1 α确实干扰细胞迁移和肌管的形态发生。产生的肌管更小，分支更多，细胞核排列不太规则。结果表明，细胞调节α 5 β 1亲和力的能力对肌原性形态发生至关重要。(C) 1995学术出版社，Inc。
The antigen recognized by U1 alpha, a monoclonal antibody to the alpha chain of a chicken integrin fibronectin receptor, was identified as alpha 5. It identifies the same polypeptide as antisera raised to a sequence from the alpha 5 cytoplasmic domain. The U1 alpha antibody has the unusual functional property for alpha chain antibodies of enhancing the binding of alpha 5 beta 1 for its ligand fibronectin. U1 alpha was used to examine the function of alpha 5 beta 1 during myogenic differentiation. As myogenic cells differentiated from replicating myoblasts to bipolar myocytes there was a decrease in their adhesion to the substrate caused by inactivation of alpha 5 beta 1, which could be reversed by treatment of the cells with U1 alpha. The U1 alpha induced increased adhesion to fibronectin but did not inhibit the differentiation process as measured by formation of myotubes. However, U1 alpha did interfere with both cell migration and morphogenesis of myotubes. The resulting myotubes were smaller, more branched, and showed less regular alignment of nuclei. The results suggest that the ability of the cell to regulate alpha 5 beta 1 affinity is critical to myogenic morphogenesis. (C) 1995 Academic Press, Inc.