Williams A J, Atkins R C, Fries J W, Gimbrone M A, Cybulsky M I, Collins T
Department of Pathology, Brigham and Women's Hospital, Harvard Medical School, Boston, MA 02115.
Biochim Biophys Acta. 1992 Jun 15;1131(2):214-6. doi: 10.1016/0167-4781(92)90081-a.
Vascular cell adhesion molecule 1 (VCAM-1) is an inducible transmembrane protein which is expressed by vascular endothelium following cytokine activation. VCAM-1 mediated the adhesion of certain blood leukocytes and tumor cells via the interaction with its counter-receptor, the integrin VLA4. When initially cloned from interleukin-1 (IL-1) stimulated human umbilical vein endothelial cells, VCAM-1 was reported to contain six immunoglobulin-like domains. However, subsequent cDNA clones and structural analysis of the human gene evealed an alternatively spliced seventh immunoglobulin domain. This seven domain form appears to be the predominant transcript in IL-1 activated endothelium. In this report, the cloning and nucleotide sequence of rat VCAM-1 is described.
血管细胞黏附分子1(VCAM-1)是一种可诱导的跨膜蛋白,在细胞因子激活后由血管内皮细胞表达。VCAM-1通过与其反受体整合素VLA4相互作用介导某些血液白细胞和肿瘤细胞的黏附。最初从白细胞介素-1(IL-1)刺激的人脐静脉内皮细胞中克隆时,据报道VCAM-1含有六个免疫球蛋白样结构域。然而,随后的cDNA克隆和人类基因的结构分析揭示了一个选择性剪接的第七个免疫球蛋白结构域。这种七结构域形式似乎是IL-1激活的内皮细胞中的主要转录本。在本报告中,描述了大鼠VCAM-1的克隆和核苷酸序列。