%0 Journal Article
%T Expression of Cathepsin L and Its Intrinsic Inhibitors in Glomeruli of Rats With Puromycin Aminonucleoside Nephrosis
%A Ayano Kubo
%A Isao Shirato
%A Katsuhiko Asanuma
%A Kazumi Ishidoh
%A Miyuki Takagi
%A Teruo Hidaka
%A Yu Sasaki
%A Yusuke Suzuki
%J Journal of Histochemistry & Cytochemistry
%@ 1551-5044
%D 2018
%R 10.1369/0022155418791822
%X Cathepsin L, a lysosomal cysteine proteinase, may have a key role in various biological and disease processes by intracellular and extracellular degradation of proteins. We examined the levels of cathepsin L and its intrinsic inhibitors in glomeruli of rats with puromycin aminonucleoside (PAN) nephrosis. In contrast to the weak levels of cathepsin L in normal glomeruli, on days 4 and 8, strong immunostaining was detected in almost all podocytes when proteinuria and pathological changes of the podocytes developed. Cathepsin L was reduced after day 28, but remained in a focal and segmental manner. Cystatin ¦Â, an intracellular inhibitor, was not detected in podocytes. However, cystatin C, an extracellular inhibitor, was detected in podocytes after day 4, coincident with cathepsin L. Cystatin C levels were gradually reduced but sustained in many podocytes on day 28, while cystatin C was not detected in podocytes sustained cathepsin L. These results demonstrated that cathepsin L levels are not always accompanied by the levels of its inhibitors in podocytes of PAN nephrosis, suggesting a potential role of cathepsin L in podocyte injury, which is a critical process for the development and progression of tuft adhesion and sclerosis
%K GBM
%K glomerulonephritis
%K proteolytic activity
%U https://journals.sagepub.com/doi/full/10.1369/0022155418791822