Immunocytochemical localization of cathepsin D in lysosomes of cortical collecting tubule cells of the rat kidneyS Yokota, H Tsuji and K Kato
Immunocytochemical localization of cathepsin D in rat renal tubules was investigated by means of indirect immunoenzyme and protein A--gold techniques. By light microscopy, fine granular staining was seen in the mesangial cells of glomeruli. Heavy reaction deposits were present in the cortical tubular segments and some of the medullary collecting tubules. The proximal tubules contained a few positive granules. Other segments were negative for cathepsin D. By electron microscopy, gold particles representing the antigenic sites for cathepsin D were present in cytoplasmic granules and multivesicular bodies of the segment of the cortical collecting tubule. These cytoplasmic granules were presumed to be digestive vacuoles (secondary lysosomes) from their morphological profile. The proximal tubule cells contained the very weakly labeled secondary lysosomes. No specific labeling was noted in other segments of the nephron. Control experiments confirmed the specificity of the immunostaining. Quantitative analysis of the labeling density in each subcellular compartment also confirmed that the main subcellular sites for cathepsin D are the secondary lysosomes and multivesicular bodies. The labeling density in these granules of the lysosomal system varied widely with the individual granules, suggesting that there is a considerable heterogeneity of enzyme content among the granules of the lysosomal system. The prominent presence of cathepsin D in the cortical collecting tubule suggests a certain segment-specific function of this proteinase.
Volume 33,
Issue 3,
pp. 191-200,
03/01/1985
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R. Nielsen, P. J. Courtoy, C. Jacobsen, G. Dom, W. R. Lima, M. Jadot, T. E. Willnow, O. Devuyst, and E. I. Christensen Endocytosis provides a major alternative pathway for lysosomal biogenesis in kidney proximal tubular cells PNAS, March 27, 2007; 104(13): 5407 - 5412. [Abstract] [Full Text] [PDF] |
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C. M. Haraguchi, T. Mabuchi, S. Hirata, T. Shoda, K. Hoshi, K. Akasaki, and S. Yokota Chromatoid Bodies: Aggresome-like Characteristics and Degradation Sites for Organelles of Spermiogenic Cells J. Histochem. Cytochem., April 1, 2005; 53(4): 455 - 465. [Abstract] [Full Text] [PDF] |
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K. Shirahama-Noda, A. Yamamoto, K. Sugihara, N. Hashimoto, M. Asano, M. Nishimura, and I. Hara-Nishimura Biosynthetic Processing of Cathepsins and Lysosomal Degradation Are Abolished in Asparaginyl Endopeptidase-deficient Mice J. Biol. Chem., August 29, 2003; 278(35): 33194 - 33199. [Abstract] [Full Text] [PDF] |
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E. I. Christensen, O. Devuyst, G. Dom, R. Nielsen, P. Van Der Smissen, P. Verroust, M. Leruth, W. B. Guggino, and P. J. Courtoy Loss of chloride channel ClC-5 impairs endocytosis by defective trafficking of megalin and cubilin in kidney proximal tubules PNAS, July 8, 2003; 100(14): 8472 - 8477. [Abstract] [Full Text] [PDF] |
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N. Ayasaka, T. Goto, T. Tsukuba, M.A. Kido, E. Nagata, T. Kondo, K. Yamamoto, and T. Tanaka Immunocytochemical Localization of Cathepsin D in Rat Junctional Epithelium Journal of Dental Research, February 1, 1993; 72(2): 502 - 507. [PDF] |
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