Multiple pathways for cationic amino acid transport in rat seminiferous tubule cells.
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Cerec V, Piquet-Pellorce C, Aly HA, Touzalin AM, Jegou B, Bauche F
Multiple pathways for cationic amino acid transport in rat seminiferous tubule cells.
Biol Reprod. 2007 Feb;76(2):241-9. Epub 2006 Oct 25.
- PubMed ID
- 17065601 [ View in PubMed]
- Abstract
Arginine and ornithine are known to be important for various biological processes in the testis, but the delivery of extracellular cationic amino acids to the seminiferous tubule cells remains poorly understood. We investigated the activity and expression of cationic amino acid transporters in isolated rat Sertoli cells, peritubular cells, pachytene spermatocytes, and early spermatids. We assessed the l-arginine uptake kinetics, Na(+) dependence of transport, profiles of cis inhibition of uptake by cationic and neutral amino acids, and sensitivity to trans stimulation of cationic amino acid transporters, and studied the expression of the genes encoding them by RT-PCR. Our data suggest that l-arginine is taken up by Sertoli cells and peritubular cells, principally via system y(+)L (SLC3A2/SLC7A6) and system y(+) (SLC7A1 and SLC7A2), with system B(0+) making a minor contribution. By contrast, system B(0+), associated with system y(+)L (SLC3A2/SLC7A7 and SLC7A6), made a major contribution to the transport of cationic amino acids in pachytene spermatocytes and early spermatids. Sertoli cells had higher rates of l-arginine transport than the other seminiferous tubule cells. This high efficiency of arginine transport in Sertoli cells and the properties of the y(+)L system predominating in these cells strongly suggest that Sertoli cells play a key role in supplying germ cells with l-arginine and other cationic amino acids. Furthermore, whereas cytokines induce nitric oxide (NO) production in peritubular and Sertoli cells, little or no upregulation of arginine transport by cytokines was observed in these cells. Thus, NO synthesis does not depend on the stimulation of arginine transport in these somatic tubular cells.
DrugBank Data that Cites this Article
- Drug Targets
Drug Target Kind Organism Pharmacological Action Actions Arginine High affinity cationic amino acid transporter 1 Protein Humans UnknownNot Available Details Ornithine High affinity cationic amino acid transporter 1 Protein Humans UnknownNot Available Details Ornithine Low affinity cationic amino acid transporter 2 Protein Humans UnknownNot Available Details