Please use this identifier to cite or link to this item: http://scholarbank.nus.edu.sg/handle/10635/133925
Title: Renal tubular antiproteinase (alpha-1-antitrypsin and alpha-1-antichymotrypsin) response in tubulo-interstitial damage
Authors: Khan, T.N. 
Sinniah, R. 
Keywords: α1-antichymotrypsin
α1-antitrypsin
Lysozyme
Proteases
Proteinase inhibitors
Tubulo-interstitial damage
Issue Date: 1993
Source: Khan, T.N., Sinniah, R. (1993). Renal tubular antiproteinase (alpha-1-antitrypsin and alpha-1-antichymotrypsin) response in tubulo-interstitial damage. Nephron 65 (2) : 232-239. ScholarBank@NUS Repository.
Abstract: We studied the role of proteinase inhibitors (Pls) α1-antitrypsin and α-antichymotrypsin in relation to lysozyme (LZM), and membrane attack complex (C5b-9) in renal tubular damage by immunohistochemical techniques. Fifty-five cases, including 45 patients with glomerular diseases, and 10 controls were studied. The patients were divided into two groups; one with tubulo-interstitial lesions (TILs; 30 cases), and the other without (15 cases). Significant antiproteinase response was observed in the proximal tubules in both disease groups, indicating that they were subjected to proteolytc attack. This response correlated with proteinuria and occurred in tubules which showed protein reabsorption as demonstrated by the presence of LZM staining in consecutive serial sections. Increased deposition of membrane attack complex (C5b-9) was observed in the disease group with TILs, indicating direct damage to cell membranes. C5b-9 may also generate oxygen species, potent inhibitors of Pls, which allow the proteases to cause tubular damage.
Source Title: Nephron
URI: http://scholarbank.nus.edu.sg/handle/10635/133925
ISSN: 00282766
Appears in Collections:Staff Publications

Show full item record
Files in This Item:
There are no files associated with this item.

Page view(s)

7
checked on Jan 20, 2018

Google ScholarTM

Check


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.