| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
Stimulates Lactate Dehydrogenase A Expression and Lactate Production in Cultured Porcine Sertoli Cells1
a Institut National de la Santé et de la Recherche Médicale, INSERM U407, Communications Cellulaires en Biologie de la Reproduction, Centre Hospitalier Lyon-Sud, 69 495 Pierre-Bénite, France
By using cultured porcine Sertoli cells as a model, the action of interleukin 1 (IL-1) on lactate production and the site of this action were studied. IL-1 stimulated Sertoli cell lactate production in a time- and dose-dependent manner (with a half-maximal effect [ED50] of 6 pM). Two major sites involved in IL-1 action were identified. First, IL-1 was shown to increase the uptake of glucose substrate in a time- and dose-dependent manner. The maximal effect, with an ED50 of 10 pM, was observed after 24 h of treatment. Second, IL-1 increased the activity of the lactate dehydrogenase (LDH) A4 isoform, which is involved in the conversion of pyruvate into lactate. This increase in LDH A4 activity was detected at 12 h and was maximal, with an ED50 of 9 pM, after 24-h treatment with IL-1. The increase was related to an increase in LDH A4 expression, since IL-1 stimulated LDH A mRNA (size: 1.5 kilobases, evidenced through Northern blotting analysis) in a dose- and time-dependent manner. Assuming that IL-1 might be produced in the seminiferous tubules by both Sertoli and germ cells, which utilize lactate for their energy metabolism, we suggest that these results together show 1) that the cytokine may represent a signal in the metabolic cooperation existing between Sertoli cells and germ cells, and 2) that a redistribution of LDH isoforms in favor of LDH A4 under IL-1 control is a key mechanism(s) in such cooperation used by germ cells to enhance lactate production in Sertoli cells.
2 Correspondence: M. Benahmed, INSERM U407, Communications Cellulaires en Biologie de la Reproduction, BP12, Faculté de Médecine Lyon-Sud, 69 921 Oullins cedex, France. FAX: 33 4 78 86 59 22; benahmed{at}lsgrisn1.univ-lyon1.fr
This article has been cited by other articles:
|
|
 |
|
  M. N. Galardo, M. F. Riera, E. H. Pellizzari, S. B. Cigorraga, and S. B. Meroni The AMP-activated protein kinase activator, 5-aminoimidazole-4-carboxamide-1-b-D-ribonucleoside, regulates lactate production in rat Sertoli cells J. Mol. Endocrinol., October 1, 2007; 39(4): 279 - 288. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. F. Riera, M. N. Galardo, E. H. Pellizzari, S. B. Meroni, and S. B. Cigorraga Participation of phosphatidyl inositol 3-kinase/protein kinase B and ERK1/2 pathways in interleukin-1{beta} stimulation of lactate production in Sertoli cells Reproduction, April 1, 2007; 133(4): 763 - 773. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 T. Ishikawa, K. Hwang, D. Lazzarino, and P. L. Morris Sertoli Cell Expression of Steroidogenic Acute Regulatory Protein-Related Lipid Transfer 1 and 5 Domain-Containing Proteins and Sterol Regulatory Element Binding Protein-1 Are Interleukin-1{beta} Regulated by Activation of c-Jun N-Terminal Kinase and Cyclooxygenase-2 and Cytokine Induction Endocrinology, December 1, 2005; 146(12): 5100 - 5111. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 Y Okuma, K Saito, A E O'Connor, D J Phillips, D M de Kretser, and M P Hedger Reciprocal regulation of activin A and inhibin B by interleukin-1 (IL-1) and follicle-stimulating hormone (FSH) in rat Sertoli cells in vitro J. Endocrinol., April 1, 2005; 185(1): 99 - 110. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
