High impact information on SCP2

• Chinese hamster ovary cells deficient in peroxisomes lack the nonspecific lipid transfer protein (sterol carrier protein 2) [1].
• Taurine- and glycine-conjugated bile salts (anionic steroid detergent-like molecules), at concentrations well below their critical micellar concentrations, stimulated PC transfer activity of SCP2 80- to 140-fold [2].
• Submicellar bile salts stimulate phosphatidylcholine transfer activity of sterol carrier protein 2 [2].
• To explore a potential role for sterol carrier protein 2 (SCP2, also known as non-specific lipid transfer protein) in hepatocellular phospholipid trafficking, we examined the influence of submicellar bile salt concentrations on phosphatidylcholine (PC) transfer activity of SCP2 [2].
• Rat liver nsL-TP was found to be identical to sterol carrier protein 2, stimulating the microsomal conversion of intermediates between lanosterol and cholesterol [3].

Biological context of SCP2

• 3. The chicken 12 kDa SCP2-like protein purifies similarly to rat SCP2 but the homogeneous chicken SCP2-like protein is dissimilar in amino acid composition and N-terminal amino acid sequence [4].

Anatomical context of SCP2

• Transfer of the resulting unesterified cholesterol to mitochondria can be accomplished in a model system by sterol carrier protein2 (SCP2) [5].

Associations of SCP2 with chemical compounds

• The stimulatory effect of adrenal cytosolic preparations on mitochondrial pregnenolone production can be completely abolished by pretreatment with anti SCP2 IgG [5].

References