Immunohistochemical and molecular analysis of β1 and β3 integrins

Clayton Buck , Steven Albelda , Laszlo Damjanovich , Jon Edelman , Daw-Tsun Shih , Joanna Solowska , Steven Albelda , Jon Edelman , Laszlo Damjanovich
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引用次数: 17

Abstract

The expression and function of integrin subunits was examined by immunohistochemical staining of normal and malignant tissues and by producing specific changes in avian β subunit cDNA that were subsequently expressed in mammalian cells. Most tissues express only a restricted number of integrins. These include primarily those thought to function as collagen/laminin receptors. With the exception of metastatic melanomas, tumors show a general down regulation of integrins. Structure/function studies of the β subunit show that the cytoplasmic domain is required for inclusion in adhesion plaques and for promotion of adhesive functions; that the transmembrane domain is required for subunit association, but not proper α subunit selection; and that the amino terminal one third of the subunit must remain intact for subunit selection and ligand binding to occur.

β1和β3整合素的免疫组织化学和分子分析
整合素亚基的表达和功能通过正常和恶性组织的免疫组织化学染色和禽β亚基cDNA的特异性变化来检测,该亚基随后在哺乳动物细胞中表达。大多数组织只表达有限数量的整合素。这些主要包括那些被认为起胶原蛋白/层粘连蛋白受体作用的细胞。除转移性黑色素瘤外,肿瘤普遍表现为整合素的下调。β亚基的结构/功能研究表明,细胞质结构域是粘附斑块和促进粘附功能所必需的;亚基结合需要跨膜结构域,但不需要适当的α亚基选择;亚基的氨基末端三分之一必须保持完整才能进行亚基选择和配体结合。
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