High impact information on Osbp

• Support for the role of a cytosolic oxysterol-binding protein in the regulation of 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase was obtained by correlating the relative binding affinities of a wide range of oxysterols to their potency in suppressing HMG-CoA reductase activity in mouse fibroblast cell cultures [1].
• Different forms of the oxysterol-binding protein. Binding kinetics and stability [2].
• Procedures for determining a 7.5 S oxysterol-binding protein in the cytosol fraction of cultured mouse fibroblasts were developed [3].
• Assay of oxysterol-binding protein in a mouse fibroblast, cell-free system. Dissociation constant and other properties of the system [3].
• These include apolipoprotein D (apoD), the mouse homolog of oxysterol-binding protein-like protein 8 (OSBPL8), a diacylglycerol receptor (n-chimerin), and lysophosphatidic acid (LPA) acyltransferase [4].

Anatomical context of Osbp

• We recently showed that oxysterol-binding protein (OSBP), one of twelve related PH domain containing proteins with lipid and sterol binding activity, interacts with VAMP-associated protein (VAP)-A on the endoplasmic reticulum (ER) [5].
• VAMP-associated protein-A regulates partitioning of oxysterol-binding protein-related protein-9 between the endoplasmic reticulum and Golgi apparatus [5].
• 6-Nitrocholesterol has been shown to cause a 50% reduction in the level of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity in animal cells in culture at 1.9 microM and it has relative binding affinity for the cytosolic oxysterol binding protein of 357 nM in cell-free extracts from the same cell line [6].

References