Identification of a new biological function for the integrin alpha(v)beta(3): Initiation of fibronectin matrix assembly

Identification of a new biological function for the integrin alpha(v)beta(3): Initiation of fibronectin matrix assembly
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DOI:
10.3109/15419069609014219
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发表时间:
1996-01-01
期刊:
CELL ADHESION AND COMMUNICATION
影响因子:
--
通讯作者:
McDonald, JA
McDonald, JA
中科院分区:
其他
文献类型:
--
作者:
Wu, CY;Hughes, PE;McDonald, JA

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纤连蛋白基质组装是由特异性纤连蛋白结合细胞表面受体启动的复杂细胞过程。尽管整合素α(5)β(1)与纤连蛋白基质的组装有关,但源自α(5)整合素无效突变体胚胎的成纤维细胞组装纤连蛋白基质。因此,替代受体必须支持这一过程。虽然血小板整合素α(IIb)β(3)支持纤连蛋白基质组装,但其表达仅限于血小板。我们报道了α(v)β(3)整合素,一种在许多细胞类型上表达的纤连蛋白受体,为可溶性纤连蛋白组装成细胞外基质提供了另一种途径。该过程独立于α(5)β(1)发生,也通过活化进行调节,并且所得基质在生物化学上与在α(5)β(1)控制下组装的基质无法区分。基质组装需要结合到纤连蛋白的第10个III型重复序列中的RGD位点,以及氨基末端基质组装结构域的参与。两种不同的整合素参与纤连蛋白基质组装表明了整合素参与细胞外基质组装和细胞内激活细胞外受体控制的识别双重系统的模型。
Fibronectin matrix assembly is a complex cellular process initiated by specific fibronectin-binding cell surface receptors. Although the integrin alpha(5) beta(1) has been implicated in the assembly of fibronectin matrices, fibroblastic cells derived from alpha(5) integrin null mutant embryos assemble a fibronectin matrix. Thus, alternative receptors must support this process. Although the platelet integrin alpha(IIb)beta(3) supports fibronectin matrix assembly, its expression is restricted to platelets. We report that alpha(v) beta(3) integrin, a fibronectin receptor expressed on many cell types provides an alternative pathway for the assembly of soluble fibronectin into the extracellular matrix. This process occurs independent of alpha(5) beta(1), is also modulated by activation, and the resulting matrix is biochemically indistinguishable from that assembled under the control of alpha(5) beta(1). Matrix assembly requires binding to the RGD site in the 10th type III repeat of fibronectin, as well as the participation of the amino-terminal matrix assembly domain. The participation of two distinct integrins in fibronectin matrix assembly suggests a model for the involvement of integrins in a dual system of extracellular matrix assembly and recognition controlled by intracellular activation of extracellular receptors.