Integrin clipping: A novel adhesion switch?
Integrin clipping: A novel adhesion switch?
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DOI：
10.1002/jcb.10675
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发表时间：
2004-01-01
影响因子：
4
通讯作者：
Cress, AE
中科院分区：
文献类型：
--
作者：
Demetriou, MC;Cress, AE
在人类前列腺癌进展过程中，除 α6、α3 和 β1 整合素外，大多数正常表达的整合素均受到抑制。我们已经证明，在前列腺癌中，α6 整合素与 β1 整合素配对，并且存在一种缺乏大部分细胞外结构域 (α6p) 的新型 α6 整合素。 α6pβ1 整合素存在于人类前列腺癌组织样本以及组织培养细胞系中，并在细胞表面形成。这篇综述讨论了 alpha6pbeta1 的产生机制以及该整合素变体的潜在功能。我们当前的工作模型预测 α6pβ1 整合素维持与异二聚体相关的细胞内细胞骨架连接，同时允许细胞粘附的改变。该机制为癌细胞转移提供了选择性优势。 (C) 2003 Wiley-Liss, Inc.
During human prostate cancer progression, the majority of normally expressed integrins are suppressed with the exception of the alpha6, alpha3, and beta1 integrins. We have shown that in prostate cancer, the alpha6 integrin is found paired with the beta1 integrin and that a novel form of the alpha6 integrin that lacks a large portion of the extracellular domain (alpha6p) exists. The alpha6pbeta1 integrin is found in human prostate cancer tissue specimens as well as tissue culture cell lines and is formed on the cell surface. This review discusses the mechanism of alpha6pbeta1 production and the potential functions of this integrin variant. Our current working model predicts that the alpha6pbeta1 integrin maintains the intracellular cytoskeletal connections associated with the heterodimer while allowing for an alteration in cell adhesion. The mechanism provides a selective advantage for cancer cell metastasis. (C) 2003 Wiley-Liss, Inc.