ArticleHistochemistry1986
Immunocytochemical localization of cathepsin H in rat kidney. Light and electron microscopic study.
Article in Histochemistry, 1986. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 32 citations in OpenAlex.
- Protein handling in kidney tubules.Nature reviews. Nephrology · 2025Review
- Spatiotemporal organisation of protein processing in the kidney.Nature communications · 2022Article
- Combined Structural and Functional Imaging of the Kidney Reveals Major Axial Differences in Proximal Tubule Endocytosis.Journal of the American Society of Nephrology : JASN · 2018Article
- Expression of cathepsin H in differentiating rat spermatids: immunoelectron microscopic study.Histochemistry and cell biology · 2003Article
- Article
- Immunoenzyme localization of cathepsins in the Golgi region of rat hepatocytes and renal tubule cells.Histochemistry · 1990Article
- A new method of the immunohistochemical detection of cellular antigens for light and electron microscopy.Histochemistry · 1989Article
- Localization of cathepsin L in rat kidney revealed by immunoenzyme and immunogold techniques.Histochemistry · 1988Article
- The heterogeneity of rat kidney lysosomes revealed by immunoelectron microscopic staining for cathepsins B and H.Histochemistry · 1988Article
- Immunocytochemical localization of cathepsins B and H in rat liver.Histochemistry · 1987Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Light and electron microscopic localization of cathepsin H in rat kidney was studied using post-embedding immunocytochemical techniques. For light microscopy, Epon sections of the kidney were stained by immunoenzyme method after removal of Epon and for electron microscopy, ultrathin sections of the Lowicryl K4M-embedded material were labeled by protein A-gold (pAg) technique. By light microscopy, fine granular staining was found in throughout the nephron, but the staining intensity considerably varied. The strongest staining was noted in the S1 segment of the proximal tubules followed by the S2 and S3 segments and the medullary collecting tubules. The glomeruli, the distal tubules, and the cortical collecting tubules were weakly stained. By electron microscopy, a gold label was found exclusively in lysosomes, which showed various sizes and labeling intensity. The results were quite consistent with the light microscopic results. The labeling intensity tended to increase as the matrix of lysosomes was condensed. Quantitative analysis of the labeling density of lysosomes demonstrated that the highest labeling density is found in the S1 segment of the proximal tubules and the labeling density of other renal segments is significantly low levels. The results indicate that a main site for cathepsin H in rat kidney is the S1 segment of the proximal tubules.
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