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Studies show the 3 steroidogenic acute regulatory-related lipid transfer (START) domain proteins StarD4 (zeige STARD4 Proteine), StarD5 and StarD6 (zeige STARD6 Proteine) have a similar lipid binding pocket specific for sterols (cholesterol in particular), but differing regulation and localization.
StarD4 (zeige STARD4 Proteine) is regulated by sterols via SREBP-2 (zeige SREBF2 Proteine), and StarD5 is activated by ER stress cholesterol metabolism; they serve different functions
demonstrated StarD5 protein in liver cytosolic fractions only, suggesting StarD5 as a directional cytosolic sterol carrier
The presence of StarD5 different human liver cells that are related to inflammatory processes provides new clues to its role of in free sterol transport in the cells and in lipid-mediated atherogenesis.
Data support STARD5 functioning in kidney, specifically within proximal tubule cells, and suggest a role in ER-associated cholesterol transport.
Cholesterol homeostasis is regulated, at least in part, by sterol regulatory element (SRE)-binding proteins (e.g., SREBP1\; MIM 184756) and by liver X receptors (e.g., LXRA\; MIM 602423). Upon sterol depletion, LXRs are inactive and SREBPs are cleaved, after which they bind promoter SREs and activate genes involved in cholesterol biosynthesis and uptake. Sterol transport is mediated by vesicles or by soluble protein carriers, such as steroidogenic acute regulatory protein (STAR\; MIM 600617). STAR is homologous to a family of proteins containing a 200- to 210-amino acid STAR-related lipid transfer (START) domain, including STARD5 (Soccio et al., 2002
StAR-related lipid transfer (START) domain containing 5
, START domain containing 5
, StAR-related lipid transfer protein 5
, START domain-containing protein 5
, stAR-related lipid transfer protein 5
, StAR-related protein 1-4E
, StAR-related protein p3-15E/p3-16E