Phospholipase and lysophospholipase activities of goat spermatozoa in transit from the caput to the cauda epididymidis

Abstract

Phospholipase and lysophospholipase activities were assayed in goat epididymal spermatozoa. Lysophospholipase was 10 times more active than phospholipase, and both enzymes decreased in activity substantially in the transit of spermatozoa from the caput to the cauda epididymidis. A comparative study revealed that phosphatidyl-ethanolamine, -choline and -inositol and phosphatidic acid were hydrolysed by goat sperm phospholipase. Hydrolysis of phosphatidylethanolamine/phosphatidylcholine revealed the end products to be glycerophosphoethanolamine/choline but neither diglycerides nor lysophosphatidylethanolamine/lysophosphatidylcholine were detected.

Phospholipase A₂ Activity in Prostasomes from Human Seminal Plasma

“…The hydrolysis of ethanolamine phosphoglycerides and phosphatidylinositol by ejaculated spermatozoa of rams and bulls was described about 20 years ago [1], Furthermore, evidence was given that the rat testis con tained two phospholipases A2 (PLA2) and these enzy matic activities were found in the interstitial and germi nal cells and seemed to be activated by testosterone and dihydrotestosterone [2], More recent work concerned the PLA2 activity in goat epididymal spermatozoa and this activity decreased substantially in the transport of sper matozoa from the caput to the cauda epididymidis [3].…”

Purification of Lysophospholipase of Human Spermatozoa and its Implication in the Acrosome Reaction1

“…In spermatozoa, the major pathway to regulate the levels of lysolipid is via their hydrolysis by lysophospholipase [4,5]. The levels of lysophospholipase and the modulation of its activity are undoubtedly important factors in controlling the flux of lysophospholipids.…”