EBP is encoded by the EBP gene, and is also known as 3-beta-hydroxysteroid-Delta(8), Delta(7)-isomerase, Cholestenol Delta-isomerase, Delta(8)-Delta(7) sterol isomerase, D8-D7 sterol isomerase and Emopamil-binding protein. EBP is a vertebrate sterol ∆8-∆7 isomerase which has demonstrated equal high binding affinity for both enantiomers of emopamil, a Ca2+ channel blocker. EBP characterization was achieved using the anti-ischemic drug (-)-(S)-emopamil. EBP catalyzes the shift of the double bond from C8-C9 to C7-C8 position in one of the last steps of cholesterol de novo biosynthesis.
|Basic Information of EBP|
|Aliases||Cholestenol Delta-isomerase, Delta(8)-Delta(7) sterol isomerase, D8-D7 sterol isomerase, Emopamil-binding protein|
|Organism||Homo sapiens (Human)|
EBP is a high-affinity receptor for the phenylalkylamine calcium-antagonist emopamil and other antiischaemic drugs. EBP was shown to be an enzyme of post-squalene cholesterol biosynthesis catalyzing the shift of a double bond in the B-ring of the sterol nucleus. EBP is a high-affinity binding protein for [3H]emopamil and belongs to the family of so-called sigma receptors. The isoenzyme of EBP from yeast, ERG2, is structurally diverse from EBP but is homologous with the sigma1 receptor, which interacts physically and functionally with InsP3 receptors and K+ channels. The pharmacological commonalities of EBP and ERG2 with sigma1 and sigma2 receptors suggested that EBP also belonged to the family of so-called sigma receptors. Meanwhile, EBP is localized on chromosome Xp11.23-p11.22 and is essential for cholesterol biosynthesis. Mutations in EBP cause X-chromosomal dominant chondrodysplasia punctate.
Fig.1 Transmembrane topology of EBP membrane protein (Sanchez, 2014).
Authors in this article assesse the in vivo blocking effects of selective σ1 receptor and EBP blockers on the brain uptake of [11C]SA4503 by the tissue dissection method at a single time point. The results indicated that the contribution of in vivo EBP binding of [11C]SA4503 was negligible in the mouse brain.
This article indicates that EBP is identified and associated with Conradi-Hünermann-Happle syndrome. Meanwhile, there are about 70 different mutations in the EBP gene have been described related to this disease.
The results of this article strongly suggest that EBP and delta 8-delta 7 sterol isomerase are identical proteins in mammals.
This article reports a novel class of EBP inhibitors, which represents a valuable tool for investigating the last steps of cholesterol biosynthesis and related pathologies, as well as a starting point for developing new anticancer drugs.
The work of this article identifies and characterized EBPL, a novel microsomal protein that has neither detectable 3β-hydroxysteroid sterol 8-7 isomerase nor sigma-ligand-binding activity when expressed in yeast, despite a distant evolutionary relationship with EBP.
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