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1 Department of Physiology and Centre for Nephrology, Royal Free & University College Medical School, London, United Kingdom
2 Centre de Recherche en Rhumatologie et Immunologie, Universite Laval, Quebec, Canada
* To whom correspondence should be addressed. E-mail: r.vekaria{at}medsch.ucl.ac.uk.
Evidence is accumulating that extracellular nucleotides act as autocrine/paracrine agents in most tissues, including the kidneys. Several families of surface-located enzymes exist, collectively known as ectonucleotidases, which can degrade nucleotides. Using immunohistochemistry, we have examined the segmental distribution of five ectonucleotidases along the rat nephron. Perfusion-fixed kidneys were taken from anesthetized male Sprague-Dawley rats. Cryostat sections of cortical and medullary regions were incubated with antibodies specific to the following enzymes: ectonucleoside triphosphate diphosphohydrolases 1, 2 and 3 (NTPDases1-3), ectonucleotide pyrophosphatase phosphodiesterase3 (NPP3) and ecto-5'-nucleotidase. Sections were then co-stained with phaseolus vulgaris erythroagglutinin (for identifying proximal tubules) and with antibodies against Tamm-Horsfall protein (for thick ascending limb), Calbindin D28k (for distal tubule) and AQP2 (for collecting duct). The tyramide signal amplification method was used in conditions where the ectonucleotidase and marker antibody were raised in the same species. The glomerulus expressed NTPDase1 and NPP3. The proximal tubule showed prominent expression of NPP3 and ecto-5'-nucleotidase in most, but not all, segments. In contrast, NTPDases 2 and 3, but not NPP3 or ecto-5-nucleotidase, were expressed in the thick ascending limb and distal tubule. NTPDase3, with some low-level expression of ecto-5'-nucleotidase, was also found in the cortical and outer medullary collecting ducts. The inner medullary collecting ducts displayed low-level staining for NTPDases1-3 and ecto-5'-nucleotidase. We conclude that these ectonucleotidases are differentially expressed along the nephron and may play a key role in the activation of purinoceptor receptors by nucleotides and nucleosides.
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