Identification of caveolin-1 in lipoprotein particles secreted by exocrine cells
Identification of caveolin-1 in lipoprotein particles secreted by exocrine cells
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DOI：
10.1038/14067
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发表时间：
1999-10-01
影响因子：
21.3
通讯作者：
Anderson, RGW
中科院分区：
文献类型：
--
作者：
Liu, PS;Li, WP;Anderson, RGW
小窝蛋白-1是一种蛋白质成分（相对分子质量22，000）的条纹外套，装饰细胞质表面的小窝膜。先前的生物化学和分子生物学测试表明，小窝蛋白-1是一种整合的膜蛋白，其顺时针插入成纤维细胞和上皮细胞的内质网膜中，使得其羧基和氨基末端位于细胞质中。在这里，我们确定小窝蛋白-1的外分泌细胞的分泌途径。胰腺腺泡细胞和转染的外分泌细胞系分泌小窝蛋白-1，但中国仓鼠卵巢细胞不分泌小窝蛋白-1，其分泌受促分泌素分泌素、胆囊收缩素和地塞米松的刺激。分泌的小窝蛋白-1共分馏与载脂蛋白，表明它可能是分泌在一个复杂的脂质。
Caveolin-1 is a protein component (of relative molecular mass 22,000) of the striated coat that decorates the cytoplasmic surface of caveolae membranes. Previous biochemical and molecular tests have indicated that caveolin-1 is an integral membrane protein that is cc-translationally inserted into endoplasmic-reticulum membranes of fibroblast and epithelial cells such that its carboxy- and amino-terminal ends are in the cytoplasm. Here we identify caveolin-1 in the secretory pathway of exocrine cells. Secretion of caveolin-1 from pancreatic acinar cells and a transfected exocrine cell line, but not from Chinese hamster ovary cells, is stimulated by the secretagogues secretin, cholecystokinin and dexamethasone. The secreted caveolin-1 co-fractionates with apolipoproteins, indicating that it may be secreted in a complex with lipids.