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KMID : 0578319960060060737
Molecules and Cells
1996 Volume.6 No. 6 p.737 ~ p.745
Localization of ¥á3 Integrin in the Sarcomere during Cardiac Myocyte Development in Vitro
Yoon, Sung Won
Gu, Hyunmin/Kwon, Hyockman/Song, Woo Keun/Kang, Man-Sik
Abstract
Using double immunofluorescence microscopy, the cellular distribution of extracellular matrix (ECM) components and integrin alpha chains during neonatal myocyte development in culture
has been demonstrated. Cultured neonatal myocytes appeared to express a variety of integrin alpha chains, such as ¥á1, ¥á3, and ¥á7. The ¥á1 and ¥á3 integrins were responsible for the interaction with collagen. The ¥á7 integrin staining was restricted to myocytes. Laminin was selectively found in myocytes stained by anti-desmin antibody, whereas the distribution of fibronectin was specific for fibroblasts. The ¥á5 integrin staining was prominent in fibroblasts but not in myocytes. These observations demonstrated that the expression of integrin alpha chains was closely associated with the distribution of ECM components on cell sufaces. In addition, the cellular localization of ¥á3 integrin was dramatically changed from a diffuse pattern into a sarcomeric banding pattern during development while other alpha chains appeared in a diffuse staining pattern. The ¥á3 integrin
appeared to be localized in the sarcolemma region adjacent to the Z-band. ¥á-actinin, a component of the Z-band, was also localized in the same region. Double immunostaining revealed that the integration of ¥á3 integrin into the Z-band was next to that of ¥á-actinin and myosin heavy chain but prior to that of desmin, suggesting that ¥á3 integrin was integrated into a pre-existing myofibrillar structure but did not participate in initiat assembly of myofibrillar proteins. The ¥á3 integrin seems to be associated with ¥â1 integrin and to function as a collagen receptor. Thus, the myofibril-collagen fibril linkages mediated by ¥á3¥â1 integrin receptor may play an essential role in the stabilization of myofibril assembly.
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