cis Interaction of the cell adhesion molecule CEACAM1 with integrin beta(3).
cis Interaction of the cell adhesion molecule CEACAM1 with integrin beta(3).
复制标题
cis 细胞粘附分子 CEACAM1 与整合素 beta(3) 的相互作用。
DOI：
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发表时间：
2001
影响因子：
6
通讯作者：
C. Wagener
中科院分区：
文献类型：
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作者：
J. Brümmer;A. Ebrahimnejad;R. Flayeh;U. Schumacher;T. Löning;A. Bamberger;C. Wagener
CEACAM 1是一种细胞粘附分子，参与了许多生理过程（例如，上皮组织中的肿瘤抑制因子、微血管形成中的有效血管生成因子、人粒细胞和上皮细胞中的微生物受体）。CEACAM 1的作用机制在很大程度上仍然没有得到解决，但最近的研究结果表明，细胞质CEACAM 1结构域间接连接到肌动蛋白为基础的细胞骨架。我们使用CEACAM 1尾部亲和纯化分离了整合素β（3）作为相关蛋白。这种关联依赖于CEACAM 1胞质结构域中Tyr-488的磷酸化。共聚焦激光扫描显微镜证实了这两种分子在人粒细胞和上皮细胞中的体内共定位。此外，在侵袭性黑色素瘤肿块的肿瘤-间质界面处的集中共定位表明CEACAM 1-整合素β（3）相互作用在黑色素瘤侵袭中的功能作用。此外，这两种粘附分子还共存于妊娠子宫内膜腺细胞的顶端表面。CEACAM 1和整合素β（3）在母胎界面从增殖到侵袭的绒毛外滋养层的过渡区的共定位支持CEACAM 1/整合素β（3）复合物在细胞侵袭中的作用。
CEACAM1 is a cell adhesion molecule that has been implicated in a number of physiological processes (eg, tumor suppressor in epithelial tissues, potent angiogenic factor in microvessel formation, microbial receptor in human granulocytes and epithelial cells). The mechanism of CEACAM1 action is still largely unresolved but recent findings demonstrated that the cytoplasmic CEACAM1 domain is linked indirectly to the actin-based cytoskeleton. We have isolated integrin beta(3) as an associated protein using CEACAM1 tail affinity purification. This association depends on phosphorylation of Tyr-488 in the CEACAM1 cytoplasmic domain. Confocal laser scanning microscopy confirmed in vivo colocalization of both molecules in human granulocytes and epithelial cells. Furthermore, the concentrated colocalization at the tumor-stroma interface of invading melanoma masses suggests a functional role of CEACAM1-integrin beta(3) interaction in melanoma invasion. Moreover, colocalization of the two adhesion molecules is also found at the apical surface of glandular cells of pregnancy endometrium. Colocalization of CEACAM1 and integrin beta(3) at the transitional zone from proliferative to invasive extravillous trophoblast of the maternal-fetal interface supports a role for CEACAM1/integrin beta(3) complexes in cell invasion.