GP-83 and GP-39, two glycoproteins secreted by human epididymis are conjugated to spermatozoa during maturation.

Abstract

Surface glycoconjugates of spermatozoa are modified during epididymal maturation, which is closely related to the development of sperm function. In addition, recognition of surface glycoconjugates is one of very critical events in sperm-oocyte interaction. The binding of carbohydrate-specific lectins to the human sperm surface during epididymal maturation has been investigated. However, the glycoproteins responsible for lectin binding in sperm maturation are not well documented. This study used wheat germ agglutinin (WGA), peanut agglutinin (PNA) and concanavalin A (Con-A) to identify sperm maturation-related glycoproteins in human epididymis. Histochemical localization revealed that the binding sites of WGA, PNA and Con-A were mainly in the principal cells and luminal contents of the human epididymis, but not in the interstitial regions. Each lectin displayed a fairly distinct regional localization. On Western blots probed with WGA and Con-A, glycoproteins of 83 kDa (GP-83) and 39 kDa (GP-39) were identified in the sperm extracts, epididymal fluid and tissue extracts of the corpus and cauda epididymides, but not in the caput. PNA identified GP-83 in the same manner as WGA and Con-A, but did not recognize GP-39. These results suggest that lectin-binding glycoproteins GP-83 and GP-39 found on mature spermatozoa may be secreted by the principal cells of corpus and cauda epididymis, and conjugated to spermatozoa during their transit in human epididymis.