Structure and putative function of a murine epididymal retinoic acid-binding protein (mE-RABP).
Vitamin A is required to maintain the epididymal epithelium. In this report, the characterization and putative functions of a murine epididymal retinoic acid-binding protein (mE-RABP) that is secreted into the lumen from the mid-/distal caput epididymidis are discussed. The amino acid sequence analysis of the mE-RABP preprotein shows that mE-RABP is the mouse orthologue of the rat epididymal secretory protein I (ESPI). These proteins belong to the lipocalin superfamily and bind to active retinoids but not to retinol. Therefore, we propose that mE-RABP may function as an extracellular retinoid carrier-protein involved in the paracrine regulation of epididymal function by retinoids.
Lareyre
J J
JJ
Department of Obstetrics and Gynecology, Vanderbilt University, School of Medicine, Nashville, TN 37232-2633, USA.
Mattéi
M G
MG
Kasper
S
S
Newcomer
M E
ME
Ong
D E
DE
Matusik
R J
RJ
Orgebin-Crist
M C
MC
D000595:Amino Acid Sequence; D000818:Animals; D017124:Conserved Sequence; D004822:Epididymis / Q000378:metabolism*; D008116:Lizards; D008297:Male; D051379:Mice; D008969:Molecular Sequence Data; D051381:Rats; D018168:Receptors, Retinoic Acid / Q000235:genetics* / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D015398:Signal Transduction
D018168:Receptors, Retinoic Acid