| The role of proteolytic enzymes in the deposition of amyloid proteins. | |
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MedLine Citation:
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PMID: 8869753 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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A Sato; M Kawamura; M Nishioka; S Nakamura; J Minaguchi |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Advances in enzyme regulation Volume: 36 ISSN: 0065-2571 ISO Abbreviation: Adv. Enzyme Regul. Publication Date: 1996 |
Date Detail:
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Created Date: 1996-12-30 Completed Date: 1996-12-30 Revised Date: 2009-11-19 |
Medline Journal Info:
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Nlm Unique ID: 0044263 Medline TA: Adv Enzyme Regul Country: ENGLAND |
Other Details:
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Languages: eng Pagination: 307-24 Citation Subset: IM |
Affiliation:
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Department of Biochemistry, Kochi State Women's University, Japan. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Acid Phosphatase
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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:
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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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