The presence of platelet-activating factor (PAF) has been demonstrated recently in mammalian spermatozoa, together with evidence for a role of this phospholipid in enhancing sperm motility and fertilizing ability. To investigate whether PAF synthesis and release occurs in human spermatozoa following incubation with stimuli that induce acrosome reaction, spermatozoa were incubated with progesterone and A23187, two known inducers of the exocytotic event. PAF synthesis (remodelling pathway) was assessed by [3H]acetate incorporation into PAF. Treatment of spermatozoa with progesterone and A23187 resulted in an increase of [3H]acetate incorporation into PAF. Most of the newly synthesized [3H]PAF formed in response to acrosome reaction was found in the supernatant, suggesting a release of the phospholipid from spermatozoa. PAF-like material extracted from human spermatozoa was able to induce aggregation of rabbit platelets and showed identical retention time and the same ion m/e values as authentic PAF when analysed with g.c.-m.s. Lyso-PAF:acetyl-CoA acetyltransferase (EC 2.3.1.67) activity in human spermatozoa was also studied and showed similar kinetic parameters to those described for other cell systems. Stimulation of spermatozoa with progesterone and A23187 induced an increase of [3H]arachidonic acid release, suggesting an activation of phospholipase A. In conclusion, our results demonstrated increased production and release of PAF in human sperm following stimulation with progesterone and A23187 and suggest a role for this phospholipid in the activation of spermatozoa.

Total lactate dehydrogenase (LDH) activity was measured in washed sperm from 74 oligozoospermic patients and 148 normospermic men. In the same samples, an additional iso-enzyme specific for germ cells, LDH-X was also measured. Both enzymatic activities were significantly higher in sperm from oligozoospermic patients than in those from normospermic men (P less than 0.001). In oligozoospermic patients, sperm LDH and LDH-X activities were related inversely to sperm concentration (r = -0.61 and r = -0.53, respectively). In normospermic men, this inverse relationship was less evident (r = -0.28 and r = -0.25, respectively). After separation of sperm on a discontinuous gradient of Percoll, LDH and LDH-X activities were increased in the non-migrated-sperm fractions and reduced in the migrated-sperm fractions in both groups of subjects when compared to the initial semen specimens. In addition, migrated sperm from oligozoospermic and normospermic men did not differ in their LDH and LDH-X activities. Although the possible contribution of immature germ-cells to these findings remains to be defined, the data suggest clearly that high levels of intracellular LDH and LDH-X are a biochemical feature of sperm from oligozoospermic subjects.

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Total lactate dehydrogenase (LDH), LDH-X, creatine phosphokinase (CPK) activities and ATP content were measured in washed spermatozoa from 188 normospermic and 94 oligozoospermic men. These four biochemical parameters were significantly higher (p < 0.001) in spermatozoa from oligozoospermic men than in those from normospermic men and were related inversely to sperm concentration. In oligozoospermic men the activity of sperm LDH and LDH-X was related significantly to sperm CPK activity (r = 0.5486 and r = 0.4442, respectively), whereas this relationship was less evident in normospermic men (r = 0.4124 and r = 0.3844, respectively). Sperm ATP content was related weakly to sperm LDH, LDH-X and CPK activities both in oligozoospermic and normospermic men. After separation on a discontinuous (40% and 80%) Percoll gradient LDH, LDH-X, CPK activities and ATP content in 80% separated sperm fractions from 48 normospermic and 30 oligozoospermic men were found to be significantly lower than in the initial semen sample in both groups of subjects. The 80% separated sperm fractions from oligozoospermic and normospermic men did not differ in their LDH or LDH-X activities or ATP content, whereas sperm CPK activity was still significantly higher in oligozoospermic men. These data suggest that, of the four parameters studied, high levels of intracellular CPK activity are the most relevant biochemical feature of spermatozoa from oligozoospermic men.

An immunologically reactive albumin-like protein (albumin) was localized, by an immunostaining technique, in the testis of infertile men (normal spermatogenesis, obstructive azoospermia) at the level of the Sertoli cells and in some cells of the germinal epithelium (secondary spermatocytes and early spermatids). No positive reaction was detectable in prepubertal testis. In vasectomized men, mean seminal albumin values were drastically reduced (by about 80%) in comparison to fertile controls, indicating a probable testicular origin. Mean seminal albumin values were also decreased in patients affected by azoospermia due to a seminiferous tubular lesion (about 40%) and in oligozoospermic patients (about 30%). In the same seminal samples transferrin, an index of Sertoli cell function, was also measured. Albumin and transferrin results were well correlated in the seminal plasma of each group (with the exception of vasectomized subjects), including a group of men with abnormally high concentrations of seminal transferrin. A weak correlation was found between seminal albumin and sperm count. We suggest that the presence of albumin in the human adult testis and in seminal plasma could be related to its ability to transport androgens.