Characterization of monoclonal antibodies specific for rabbit renal brush-border hydrolases: application to immunohistological localizationM Tauc, F Chatelet, P Verroust, A Vandewalle, P Poujeol and P Ronco INSERM U64, Hopital Tenon, Paris, France. By use of immunodepletion studies, we characterized four monoclonal antibodies reactive with rabbit brush-border (BB) as specific for aminopeptidase N (AP), dipeptidylpeptidase IV (DPPIV), neutral endopeptidase (EP), and angiotensin-converting enzyme (ACE), and we used these antibodies for immunohistochemical detection of these four hydrolases. Expression within the kidney was studied by light and electron microscopy. All four hydrolases are expressed on the various segments of the proximal tubule. In addition, EP and DPPIV are detectable on visceral epithelial cells of the glomerulus and AP on the cells of Bowman's capsule. Outside the kidney, the four hydrolases are expressed within the digestive and genital tracts, where AP, EP, and DPPIV predominate on epithelial structures, whereas ACE is essentially located in vascular structures. The latter localization is also characteristic of ACE in the other organs studied, where clear-cut systematic distribution of the other hydrolases was often difficult to demonstrate. In addition, AP, DPPIV, and EP were detected on lymphoid cells. As compared to reports of data obtained essentially by enzymatic or immunoradiometric assays, these observations suggest considerable interspecies variations of extrarenal expression of the major BB hydrolases. This should be taken into account in attempting to define a general physiological role for a given enzyme.
Volume 36,
Issue 5,
pp. 523-532,
05/01/1988
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H. Tagawa, Y. Kizuka, T. Ikeda, S. Itoh, N. Kawasaki, H. Kurihara, M. L. Onozato, A. Tojo, T. Sakai, T. Kawasaki, et al. A Non-sulfated Form of the HNK-1 Carbohydrate Is Expressed in Mouse Kidney J. Biol. Chem., June 24, 2005; 280(25): 23876 - 23883. [Abstract] [Full Text] [PDF] |
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P. Ronco and H. Debiec Molecular Pathomechanisms of Membranous Nephropathy: From Heymann Nephritis to Alloimmunization J. Am. Soc. Nephrol., May 1, 2005; 16(5): 1205 - 1213. [Abstract] [Full Text] [PDF] |
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F. Ebihara, G. Seno Di Marco, M. Aparecida Juliano, and D. E. Casarini Neutral endopeptidase expression in mesangial cells Journal of Renin-Angiotensin-Aldosterone System, December 1, 2003; 4(4): 228 - 233. [Abstract] [PDF] |
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H. Debiec, V. Guigonis, B. Mougenot, J.-P. Haymann, A. Bensman, G. Deschenes, and P. M. Ronco Antenatal Membranous Glomerulonephritis with Vascular Injury Induced by Anti-Neutral Endopeptidase Antibodies: Toward New Concepts in the Pathogenesis of Glomerular Diseases J. Am. Soc. Nephrol., June 1, 2003; 14(90001): S27 - 32. [Full Text] [PDF] |
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H. Debiec, V. Guigonis, B. Mougenot, F. Decobert, J.-P. Haymann, A. Bensman, G. Deschenes, and P. M. Ronco Antenatal Membranous Glomerulonephritis Due to Anti-Neutral Endopeptidase Antibodies N. Engl. J. Med., June 27, 2002; 346(26): 2053 - 2060. [Full Text] [PDF] |
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S. M. Najjar, J.-P. Broyart, L. T. Hampp, and G. M. Gray Intestinal aminooligopeptidase in diabetic BioBreed rat: altered posttranslational processing and trafficking Am J Physiol Gastrointest Liver Physiol, January 1, 2001; 280(1): G104 - G112. [Abstract] [Full Text] [PDF] |
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S. MARUYAMA, E. CANTU III, C. DEMARTINO, A. VLADUTIU, P. R. B. CALDWELL, C. Y. WANG, V. D'AGATI, G. GODMAN, D. M. STERN, and G. ANDRES Membranous Glomerulonephritis Induced in the Pig by Antibody to Angiotensin-Converting Enzyme: Considerations on Its Relevance to thePathogenesis of Human Idiopathic Membranous Glomerulonephritis J. Am. Soc. Nephrol., October 1, 1999; 10(10): 2102 - 2108. [Abstract] [Full Text] |
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