| Abstrakt: |
Caveolin-1 was first identified as an approximately 22-kDa tyrosine-phosphorylated protein in Rous sarcoma virus-transformed cells (Glenney, 1989; Glenney and Soppet, 1992). Caveolin-1 has subsequently attracted much attention because it serves as a major coat protein of caveolae (Rothberg, et al., 1992; Smart, et al., 1999). The caveolar membrane system, comprising plasma membrane invaginations and juxtamembrane uncoated vesicles, mediates certain protein transport processes, including transcytosis, potocytosis, and clathrin-independent endocytosis (Anderson, 1998). Caveolin-1 and caveolae are also involved in mediating cellular cholesterol efflux (Smart et al., 1999; Fielding and Fielding, 2001), and a large body of evidence implicates caveolin-1 in regulating intracellular signaling pathways. [ABSTRACT FROM AUTHOR] |
