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The role of oxidative phosphorylation in the generation of ATP in human spermatozoa

Summary. Washed human spermatozoa had an endogenous oxygen uptake of 2·14 ± 0·17 nmol O₂/10⁸ spermatozoa/min (mean ± s.e.m., n = 35) which was stimulated by succinate (V_max = 9·64 ± 0·44 nmol O₂/10⁸ spermatozoa/min) but not by other substrates. The ATP concentration in freshly washed spermatozoa was 12·18 ± 0·54 (s.e.m.) nmol/10⁸ spermatozoa (n = 26) and was maintained for 2 h in the presence of 2 mM-D-glucose but fell to 9·56 ± 0·73 (s.e.m.) nmol/10⁸ spermatozoa (n = 13) in its absence. The presence of 2 µM-antimycin A, 2 µM-rotenone, 0·4 µM-carbonyl cyanide m-chlorophenyl hydrazone or 8 µM-oligomycin caused the ATP concentration to fall to <2 nmol/10⁸ spermatozoa but their effect was partly alleviated by 2 mM-glucose. Sodium malonate (5 mM) prevented the stimulation of respiration by succinate but had no effect on the ATP concentration of the spermatozoa or their ability to produce ¹⁴CO₂ from [U-¹⁴C]glucose.

The least active of the tricarboxylic acid cycle enzymes was 2-oxoglutarate dehydrogenase (EC 1.2.4.2 [EC] ) (3·1 ± 0·6 (s.e.m.) nmol substrate transformed/10⁸ spermatozoa/h (n = 4). Cytochrome c oxidase (EC 1.9.3.1 [EC] ) was much less active than in rat spermatozoa (22·3 ± 6·0 (s.e.m., n = 4) and 615 ± 87 (n = 4) nmol transformed/10⁸ spermatozoa/min).

It is concluded that human spermatozoa can obtain ATP by the respiration of endogenous substrate but the substrates and metabolic pathways involved remain obscure.

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