Characterization of caveolin-rich membrane domains isolated from an endothelial-rich source: implications for human disease.

作者：Michael P. Lisanti, Philipp E. Scherer, Jolanta Vidugirienė, Z Tang, Anne Hermanowski‐Vosatka, Youquan Tu, R F Cook, Massimo Sargiacomo · 发表于：The Journal of Cell Biology · 年份：1994 · DOI：10.1083/jcb.126.1.111 · 被引用次数：910 · 研究领域：Caveolin-1 and cellular processes、Metabolism, Diabetes, and Cancer、Erythrocyte Function and Pathophysiology

Caveolae are 50-100-nm membrane microdomains that represent a subcompartment of the plasma membrane. Previous morphological studies have implicated caveolae in (a) the transcytosis of macromolecules (including LDL and modified LDLs) across capillary endothelial cells, (b) the uptake of small molecules via a process termed potocytosis involving GPI-linked receptor molecules and an unknown anion transport protein, (c) interactions with the actin-based cytoskeleton, and (d) the compartmentalization of certain signaling molecules, including G-protein coupled receptors. Caveolin, a 22-kD integral membrane protein, is an important structural component of caveolae that was first identified as a major v-Src substrate in Rous sarcoma virus transformed cells. This finding initially suggested a relationship between caveolin, transmembrane signaling, and cellular transformation. We have recently developed a procedure for isolating caveolin-rich membrane domains from cultured cells. To facilitate biochemical manipulations, we have applied this procedure to lung tissue--an endothelial and caveolin-rich source-allowing large scale preparation of these complexes. These membrane domains retain approximately 85% of caveolin and approximately 55% of a GPI-linked marker protein, while they exclude > or = 98% of integral plasma membrane protein markers and > or = 99.6% of other organelle-specific membrane markers tested. Characterization of these complexes by micro-sequencing and immuno-blotting ...