Lactate Dehydrogenases in Human Testes

Blanco, Antonio; Zinkham, William H.

doi:10.1126/science.139.3555.601

Cited by 312 publications

(89 citation statements)

References 9 publications

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“…Lactate metabolism in mammalian sperm is mediated by a lactate dehydrogenase (LDH) isoform that is sperm-specific (Blanco and Zinkham, 1963;Goldberg, 1963) and was designated at the time as LDH-X. In modern nomenclature, it is designated LDH-C4.…”

Section: Mitochondrial Activities: Oxygen As Friendmentioning

confidence: 99%

Mammalian sperm metabolism: oxygen and sugar, friend and foe

Storey¹

2008

Int. J. Dev. Biol.

290

260

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Mammalian spermatozoa expend energy, generated as intracellular ATP, largely on motility. If the sperm cell cannot swim by use of its flagellar motion, it cannot fertilize the egg. Studies of the means by which this energy is generated span a period of six decades. This review gives an overview of these studies, which demonstrate that both mitochondrial oxidative phosphorylation, for which oxygen is friend, and glycolysis, for which sugar is friend, can provide the energy, independent of one another. In mouse sperm, glycolysis appears to be the dominant pathway; in bull sperm, oxidative phosphorylation is the predominant pathway. In the case of bull sperm, the high activity of the glycolytic pathway would maintain the intracellular pH too low to allow sperm capacitation; here sugar is enemy. The cow's oviduct has very low glucose concentration, thus allowing capacitation to go forward. The choice of the pathway of energy generation in vivo is set by the conditions in the oviduct of the conspecific female. The phospholipids of the sperm plasma membrane have a high content of polyunsaturated fatty acids represented in their acyl moieties, rendering them highly susceptible to lipid peroxidation; in this case oxygen is enemy. But the susceptibility of the sperm membrane to lethal damage by lipid peroxidation allows the female oviduct to dispose of sperm that have overstayed their welcome, and so keep in balance sperm access to the egg and sperm removal once this has occurred.

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Section: Mitochondrial Activities: Oxygen As Friendmentioning

confidence: 99%

Mammalian sperm metabolism: oxygen and sugar, friend and foe

Storey¹

2008

Int. J. Dev. Biol.

290

260

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“…These unique isoenzymes have been named LDH-X (Blanco and Zinkham 1963). In the rat testis LDH-X appear between 20 and 30 days of age , a time when late primary spermatocytes are being formed in the seminiferous tubular epithelium, and these isoenzymes are probably located in specialized mitochondria found in late primary spermatocytes and spermatozoa (De Domenech et al 1970, 1972.…”

Section: Introductionmentioning

confidence: 99%

Studies on Testicular Function III. Effects of FSH, LH, Testosterone and Dihydrotestosterone on Restoration and Maintenance of Testicular-Specific Lactate Dehydrogenase Activity in the Hypophysectomized Rat

Elkington¹,

Blackshaw²

1974

Aust. Jnl. Of Bio. Sci.

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Hypophysectomy of the adult male rat depressed the activity of testicular-specific lactate dehydrogenase (LDH-X). Groups of rats were treated with FSH (F), LH (L) or testosterone (T) alone or in combination after 32 days of post-hypophysectomy regression (restoration experiment) for a further 32 days or with F, T or dihydrotestosterone (D) alone or in combination from 2 days after hypophysectomy (maintenance experiment) for 30 days.LDH-X activity per milligram of protein was restored to normal by the hormonal combinations FT and LT while F, L, or T given alone or the FL and FLT combinations were ineffective. However, the total LDH-X activity per testis was only partially restored by the hormonal combinations FT, LT and FLT.In the maintenance experiment LDH-X activity per milligram of protein was maintained by all hormonal treatments except D, while the total LDH-X activity per testis was completely maintained by the FT hormonal combination. All other hormonal treatments except F alone maintained the activity of this isoenzyme above the level in the hypophysectomized rat.The restoration and maintenance of LDH-X activity in the testis of the hypophysectomized rat was successful with those combinations of hormones that were also able to restore or maintain the numbers of late primary spermatocytes and spermatids. Thus, the level of LDH-X activity in the testis is dependent on the presence of late primary spermatocytes and spermatids and hence this enzyme is a good marker for the production of these cells in the rat testis.

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“…The X band resisted the inhibitory action of 2-mercaptoethanol and n-butanol while the other five bands were completely inhibited (Ressler et al, 1965b). No X band was found in pre-pubertal testis or in two post-pubertal specimens showing a marked decrease in spermatogenesis (Blanco and Zinkham, 1963). The relative migration rate of band X was reported by Ressler et al, (1965b) to be dependent on the pH of the supporting medium, a change in pH from 8-6 to 7 0 displacing band X from between isoenzymes 3 and 4 to between isoenzymes 4 and 5, but to be independent of whether the supporting medium was starch or agar.…”

Section: Discussionmentioning

confidence: 86%

“…A single supernumerary band, designated band X, in extracts of human testis has been demonstrated between isoenzyme 3 and 4, at pH 8-6, on starch gel (Blanco and Zinkham, 1963;Ressler, Olivero and Joseph, 1965b), on agar gel (Clausen and Ovlisen, 1965) and on polyacrylamide gel (Goldberg, 1963). The X band resisted the inhibitory action of 2-mercaptoethanol and n-butanol while the other five bands were completely inhibited (Ressler et al, 1965b).…”

Section: Discussionmentioning

confidence: 99%