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1 Department of Medicine, University of Utah Health Sciences Center, Salt Lake City, UT, USA; Department of Physiology, University of Utah Health Sciences Center, Salt Lake City, UT, USA; Nephrology Research, VA Salt lake City Health Care System, Salt Lake City, UT, USA
2 Department of Pathology, University of Utah Health Sciences Center, Salt Lake City, UT, USA; ARUP Laboratories, Salt Lake City, UT, USA
3 Centre de Recherche en Rheumatologie et Immunologie, Universite Laval, Sainte-Foy, Quebec, Germany
4 Department of Medicine, University of Utah Health Sciences Center, Salt Lake City, UT, USA; Nephrology Research, VA Salt lake City Health Care System, Salt Lake City, UT, USA
5 Department of Medicine, University of Utah Health Sciences Center, Salt Lake City, UT, USA
6 AK Neurochemie, Zoologisches Institut, Biozentrum der J.W. Goethe-Universitat, Frankfurt am Main, Germany
7 Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA, USA
* To whom correspondence should be addressed. E-mail: Bellamkonda.Kishore{at}hsc.utah.edu.
The regulation of renal function by extracellular nucleotides encompasses alterations in glomerular hemodynamics, microvascular function, tubuloglomerular feedback, tubular transport, cell growth or apoptosis, and transport of water and solutes in the medullary collecting duct. Nearly all cells can release ATP or other nucleotides, that are then rapidly hydrolyzed in the extracellular milieu. However, little information is available on the cellular expression of ectoenzymes that hydrolyze extracellular nucleotides within the kidney. Nucleoside triphosphate diphosphohydrolases (NTPDases) are plasma membrane-bound ectonucleotidases. NTPDase1 has identity with CD39, a B lymphocyte activation marker, and hydrolyzes extracellular ATP and ADP to AMP within the vasculature, whereas NTPDase2/CD39L(ike)1 preferentially converts ATP to ADP outside of blood vessels. Using immunohistochemical and in situ hybridization approaches we have localized the protein and mRNA of NTPDase1 and 2 in murine renal tissues. In the renal cortex, NTPDase1 is expressed by vascular smooth muscle cells and endothelium in interlobular arteries, afferent glomerular arterioles, and peritubular capillaries. In the inner medulla, NTPDase1 is expressed in ascending thin limbs of Henle's loop, ducts of Bellini, and in the pelvic wall. In contrast, NTPDase2 is expressed in Bowman's capsule, glomerular arterioles, adventitia of blood vessels, and pelvic wall. Thus, the distribution patterns of NTPDases have parallels to the known distribution of P2 receptors within the kidney. NTPDases may modulate regulatory effects of ATP and degradation products within the vasculature, and other sites and thereby potentially influence physiological as well as multiple pathological events in the kidney.
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