Immunocytochemical localization of cathepsin H in rat kidney. Light and electron microscopic study.
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.
D000818:Animals; D056655:Cathepsin H; D002403:Cathepsins / Q000032:analysis*; D003546:Cysteine Endopeptidases; D006651:Histocytochemistry; D005779:Immunodiffusion; D007124:Immunoenzyme Techniques; D007668:Kidney / Q000166:cytology / Q000201:enzymology* / Q000648:ultrastructure; D007687:Kidney Tubules, Proximal / Q000201:enzymology / Q000648:ultrastructure; D008247:Lysosomes / Q000201:enzymology / Q000648:ultrastructure; D008854:Microscopy, Electron; D051381:Rats
D002403:Cathepsins; D003546:Cysteine Endopeptidases; D056655:Cathepsin H; C534128:Ctsh protein, rat