Polyol pathway along the bovine epididymis
- 29 September 2004
- journal article
- research article
- Published by Wiley in Molecular Reproduction and Development
- Vol. 69 (4) , 448-456
- https://doi.org/10.1002/mrd.20170
Abstract
During the epididymal transit, male gametes acquire new surface proteins necessary for their fertilizing ability. We have previously shown that membranous vesicles, called epididymosomes, interact with sperm surface within the epididymal fluid allowing transfer of some proteins to different subcellular compartments of spermatozoa. We previously showed that one of the major proteins associated with epididymosomes was an aldose reductase (gene: AKR1B5) and confirmed that aldose reductase is located in the epithelial cells bordering the intraluminal compartment of the epididymis. The present study shows that cytosolic aldose reductase activity was maximal in the proximal and middle segments of the epididymis and decreased in the distal epididymis. Western and Northern blot analysis confirmed the distribution pattern of aldose reductase and of the encoding mRNA. The optimal pH of epididymal aldose reductase was 6.0–6.5 when glucose was used as a substrate; this corresponds to the pH of the intraluminal epididymal fluid. In order to evaluate the possible involvement of sorbitol in sperm physiology, Western blot of tissue homogenates were probed with an anti-sorbitol dehydrogenase antibody. The amount of enzyme immunodetected was higher in the proximal and distal segments of the epididymis when compared to the amount detectable in the middle segment of the epididymis. Sorbitol dehydrogenase activity as well as the level of the encoding mRNA showed the same pattern of distribution. Furthermore, immunohistological studies using the anti-sorbitol dehydrogenase revealed that this enzyme was synthesized by the epididymal epithelial cells bordering the intraluminal compartment. Knowing the importance of sorbitol and fructose in sperm metabolism, we hypothesized that the polyol pathway is involved in the modulation of sperm motility within the epididymis. Mol. Reprod. Dev. 69: 448–456, 2004.Keywords
This publication has 31 references indexed in Scilit:
- An Aldose Reductase with 20α-Hydroxysteroid Dehydrogenase Activity Is Most Likely the Enzyme Responsible for the Production of Prostaglandin F2α in the Bovine EndometriumPublished by Elsevier ,2003
- Selected Proteins of “Prostasome-Like Particles” from Epididymal Cauda Fluid Are Transferred to Epididymal Caput Spermatozoa in Bull1Biology of Reproduction, 2002
- Prostasome‐like particles are involved in the transfer of P25b from the bovine epididymal fluid to the sperm surfaceMolecular Reproduction and Development, 2001
- P34H Sperm Protein Is Preferentially Expressed by the Human Corpus EpididymidisEndocrinology, 1999
- Light and Electron Microscopic Immunohistochemical Localization of Protein Gene Product 9.5 and Ubiquitin Immunoreactivities in the Human Epididymis and Vas Deferens1Biology of Reproduction, 1996
- Rat Sperm are Mechanically Immobilized in the Caudal Epididymis by “lmmobilin,” a High Molecular Weight GlycoproteinBiology of Reproduction, 1983
- Immunohistochemical localization of aldose reductase. I. Enzyme purification and antibody preparation--localization in peripheral nerve, artery, and testisDiabetes, 1980
- L'aldose-réductaseBiochimica et Biophysica Acta, 1960
- Sorbitol Dehydrogenase in SpermatozoaNature, 1958
- Le mécanisme de la transformation de glucose en fructose par les vésicules séminalesBiochimica et Biophysica Acta, 1956