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Tumor Necrosis Factor- Stimulates Lactate Dehydrogenase A Expression in Porcine Cultured Sertoli Cells: Mechanisms of Action

INSERM, U-407, Faculté de Médecine Lyon-Sud, F-69921 Oullins Cedex, France

Address all correspondence and requests for reprints to: Dr. Mohamed Benahmed, INSERM U-407, Faculté de Médecine Lyon-Sud, BP 12, F-69921 Oullins Cedex, France. E-mail: benahmed{at}lsgrisn1.univlyon1.fr

In the present study, we investigated the regulatory action of tumor necrosis factor- (TNF) on lactate dehydrogenase A (LDH A), a key enzyme involved in lactate production. To this end, use was made of a primary culture system of porcine testicular Sertoli cells. TNF stimulated LDH A messenger RNA (mRNA) expression in a dose (ED₅₀ = 2.5 ng/ml; 0.1 nM TNF)-dependent manner. This stimulatory effect was time dependent, with an effect detected after 6 h of TNF treatment and maximal after 48 h of exposition (5-fold; P < 0.001). The direct effect of TNF on LDH A mRNA could not be accounted for by an increase in mRNA stability (half-life = 9 h), but was probably due to an increase in LDH A gene transcription. Inhibitors of protein synthesis (cycloheximide), gene transcription (actinomycin D and dichlorobenzimidazole riboside), tyrosine kinase (genistein), and protein kinase C (bisindolylmaleimide) abrogated completely (actinomycin D, dichlorobenzimidazole riboside, cycloheximide, and genistein) or partially (bisindolylmaleimide) TNF-induced LDH A mRNA expression. These observations suggest that the stimulatory effect of TNF on LDH A mRNA expression requires protein synthesis and may involve a protein tyrosine kinase and protein kinase C. In addition, we report that LDH A mRNA levels were increased in Sertoli cells treated with FSH. However, although the cytokine enhances LDH A mRNA levels through increased gene transcription, the hormone exerts its stimulatory action through an increase in LDH A mRNA stability. The regulatory actions of the cytokine and the hormone on LDH A mRNA levels and therefore on lactate production may operate in the context of the metabolic cooperation between Sertoli and postmeiotic germ cells in the seminiferous tubules.

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