Anfosso F, Bardin N, Francès V, Vivier E, Camoin-Jau L, Sampol J, Dignat-George F
Laboratoire d'Hématologie-Immunologie, Unité de Formation et de Recherche Pharmacie, 13385 Marseille, France.
J Biol Chem. 1998 Oct 9;273(41):26852-6. doi: 10.1074/jbc.273.41.26852.
S-Endo-1 antigen (CD146), a transmembrane receptor also known as MUC18/MCAM, is a member of the immunoglobulin superfamily and belongs to a group of cell adhesion molecules. CD146 is highly expressed on the whole vascular tree. We demonstrate here that engagement of CD146 on human endothelial cells isolated from cord blood results in tyrosine phosphorylation of a large panel of cellular proteins, although no tyrosine phosphorylation of CD146 was detected. In particular, CD146 cross-linking induces the tyrosine phosphorylation of the protein tyrosine kinase p125(FAK) as well as p125(FAK) association with paxillin, both events being inhibited by cytochalasin D. No direct association of CD146 with p125(FAK) was observed. Consistent with these data, CD146 associates with p59(fyn), a Src family kinase known to phosphorylate p125(FAK). The identification of a signaling pathway initiated by CD146 engagement and which includes p59(fyn), p125(FAK), and paxillin indicates that CD146 participates in outside-in signaling in endothelial cells.
S-内皮素-1抗原（CD146），一种也被称为MUC18/MCAM的跨膜受体，是免疫球蛋白超家族的成员，属于细胞粘附分子组。CD146在整个血管系统中高度表达。我们在此证明，从脐带血中分离的人内皮细胞上的CD146被激活会导致大量细胞蛋白发生酪氨酸磷酸化，尽管未检测到CD146的酪氨酸磷酸化。特别是，CD146交联诱导蛋白酪氨酸激酶p125（FAK）的酪氨酸磷酸化以及p125（FAK）与桩蛋白的结合，这两个事件均被细胞松弛素D抑制。未观察到CD146与p125（FAK）有直接关联。与这些数据一致，CD146与p59（fyn）相关联，p59（fyn）是一种已知可磷酸化p125（FAK）的Src家族激酶。由CD146激活引发的包括p59（fyn）、p125（FAK）和桩蛋白的信号通路的确定表明，CD146参与内皮细胞的外向内信号传导。
