Document Detail


The role of proteolytic enzymes in the deposition of amyloid proteins.
MedLine Citation:
PMID:  8869753     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Serum albumin from normal individuals and short-term hemodialysis patients was separated by isoelectric focusing into two bands with pIs of 4.7 (Alb-I) and 4.2 (Alb-II). However, serum albumin from long-term hemodialysis patients with CTS migrated as a single band with a pI of 4.2 (Alb-II). The major constituent of the 100,000 x g supernatant proteins from amyloid tissues that were collected from hemodialysis patients with CTS was Alb-II. Incubation of serum albumin by lysosomal enzymes in vitro caused the modification of Alb-I to Alb-II. The ratio of Alb-I/Alb-II was changed in vivo during the hemodialysis and in in-vitro experiments designed to circulate the sera. Lysosomal enzyme levels such as acid phosphatase, glucosidase, glucuronidase and dipeptidyl aminopeptidase in the serum of hemodialysis patients were higher than those of normal individuals. Plasma levels of acid phosphatase and cathepsin L were elevated during hemodialysis. These results suggest that the conformational change of serum albumin by proteolytic modification during hemodialysis may be involved in the hemodialysis-associated amyloidosis.
Authors:
A Sato; M Kawamura; M Nishioka; S Nakamura; J Minaguchi
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Advances in enzyme regulation     Volume:  36     ISSN:  0065-2571     ISO Abbreviation:  Adv. Enzyme Regul.     Publication Date:  1996  
Date Detail:
Created Date:  1996-12-30     Completed Date:  1996-12-30     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  0044263     Medline TA:  Adv Enzyme Regul     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  307-24     Citation Subset:  IM    
Affiliation:
Department of Biochemistry, Kochi State Women's University, Japan.
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MeSH Terms
Descriptor/Qualifier:
Acid Phosphatase / blood,  metabolism
Amyloid / metabolism*
Animals
Blood Proteins / analysis
Carpal Tunnel Syndrome / complications
Cathepsin L
Cathepsins / blood,  metabolism
Cysteine Endopeptidases
Dipeptidases / blood,  metabolism
Electrophoresis, Polyacrylamide Gel
Endopeptidases / metabolism*
Glucosidases / blood,  metabolism
Glucuronidase / blood,  metabolism
Glycosylation End Products, Advanced / metabolism
Humans
Isoelectric Focusing
Lysosomes / enzymology
Rats
Renal Dialysis / adverse effects
Serum Albumin / chemistry,  metabolism
Chemical
Reg. No./Substance:
0/Amyloid; 0/Blood Proteins; 0/Glycosylation End Products, Advanced; 0/Serum Albumin; EC 3.1.3.2/Acid Phosphatase; EC 3.2.1.-/Glucosidases; EC 3.2.1.31/Glucuronidase; EC 3.4.-/Cathepsins; EC 3.4.-/Endopeptidases; EC 3.4.13.-/Dipeptidases; EC 3.4.22.-/Cysteine Endopeptidases; EC 3.4.22.15/CTSL1 protein, human; EC 3.4.22.15/Cathepsin L; EC 3.4.22.15/Ctsl protein, rat

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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