High impact information on Erabp

• The epididymal retinoic acid-binding protein has been crystallized from 39 to 43% saturated ammonium sulfate, 10 mm Tris, pH 8 [1].
• Epididymal retinoic acid binding protein expression was significantly induced with dihydrotestosterone, although this effect was not blocked by flutamide, suggesting that RCE cells are not androgen responsive [2].
• Epididymal retinoic acid-binding protein and beta-lactoglobulin, two other lipocalin proteins that bind retinoids such as prostaglandin D synthase, did not show any significant interaction with bile pigments or thyroid hormones [3].
• These observations provide experimental support for the proposition that the charged residues near the open end of the binding pocket are responsible for restricting the specificity of ERABP for retinoic acid [4].
• Epididymal retinoic acid-binding protein (ERABP) is the major androgen-dependent protein present in the lumen of the epididymis and is thought to be involved in sperm maturation [4].

Biological context of Erabp

• One of these is a retinoic acid binding protein, E-RABP, which binds both all-trans and 9-cis retinoic acid [5].
• Rat epididymal retinoic acid-binding protein: development of a radioimmunoassay, its tissue distribution, and its changes in selected androgen-dependent organs after orchiectomy [6].

Anatomical context of Erabp

• Rat epididymal retinoic acid-binding protein (EP-RABP) has been purified to apparent homogeneity from extracts of the epididymis by HPLC [6].
• Rat EP-RABP is a male-specific protein, since it was detected in male organ extracts, including epididymis, testis, prostate, seminal vesicles, liver, spleen, and brain, with a negligible concentration in the female liver and spleen [6].
• Two types of retinoic acid-binding proteins, designated as epididymal retinoic acid-binding protein (ERABP) types A and B, have been purified to homogeneity from rat genital organs [7].

Associations of Erabp with chemical compounds

• CONCLUSION: E-RABP achieves high-affinity binding of both all-trans and 9-cis isomers of retinoic acid by forcing the all-trans form to bind in a folded conformation [5].
• Whereas the wild-type ERABP binds only retinoic acid, the double mutant is capable of binding retinol, retinoic acid and retinaldehyde with similar affinities [4].
• The structure of ERABP with a mixture of all-trans and 9-cis retinoic acid has previously been reported [8].
• ERABP binds both the all-trans and 9-cis isomers of retinoic acid, as well as the synthetic retinoid (E)-4-[2-(5,6,7,8)-tetrahydro-5,5,8,8-tetramethyl-2 napthalenyl-1 propenyl]-benzoic acid (TTNPB), a structural analog of all-trans retinoic acid [8].

Other interactions of Erabp

• The absorption spectrum of ERABP complex with retinoic acid had two peaks at 277 and 354 nm, and showed similar uncorrected fluorescence spectra to that of cellular retinoic acid-binding protein (CRABP) [7].

References