Linked Life Data

15095475

Source:http://linkedlifedata.com/resource/pubmed/id/15095475

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2004-4-19
pubmed:abstractText
Cathepsin (Cath) B, CathK and CathL are cysteine proteases that participate in the lysosomal protein degradation system and are expressed in macrophages, epithelioid cells, and multinucleated histiocytic giant cells (MGCs). Both macrophages and MGCs are commonly found adjacent to immunoglobulin light chain-associated (AL) amyloid deposits, which raised the question of whether cysteine proteases are able to cleave AL amyloid proteins and AL amyloid deposits. The present study has investigated whether recombinant human CathB, CathK, and CathL are able to degrade AL(VlambdaVI) amyloid proteins and AL amyloid deposits. Using immunohistochemistry, CathB, CathK, and CathL were found adjacent to AL amyloid deposits. In vitro degradation experiments using purified AL amyloid proteins showed that CathB, CathK, and CathL degrade AL(VlambdaVI) amyloid proteins. Furthermore, using unfixed tissue sections from an amyloidotic spleen as an in vitro model for extracellular proteolysis of intact amyloid deposits, it was demonstrated that all three cysteine proteases are also capable of degrading AL amyloid in situ. This is the first study to show that cysteine proteases are able to cleave AL amyloid proteins. However, the efficiency with which proteolysis occurs depends on the concentration of active protease recruited at the sites of amyloid deposition, and possibly on the structure of the AL amyloid proteins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0022-3417
pubmed:author
pubmed:copyrightInfo
Copyright 2004 Pathological Society of Great Britain and Ireland. Published by John Wiley & Sons, Ltd.
pubmed:issnType
Print
pubmed:volume
203
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
528-37
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:15095475-Aged, pubmed-meshheading:15095475-Amino Acid Sequence, pubmed-meshheading:15095475-Amyloid, pubmed-meshheading:15095475-Amyloidosis, pubmed-meshheading:15095475-Blotting, Western, pubmed-meshheading:15095475-Cathepsin B, pubmed-meshheading:15095475-Cathepsin K, pubmed-meshheading:15095475-Cathepsin L, pubmed-meshheading:15095475-Cathepsins, pubmed-meshheading:15095475-Cysteine Endopeptidases, pubmed-meshheading:15095475-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:15095475-Enzyme Precursors, pubmed-meshheading:15095475-Female, pubmed-meshheading:15095475-Humans, pubmed-meshheading:15095475-Immunoglobulin Light Chains, pubmed-meshheading:15095475-Immunohistochemistry, pubmed-meshheading:15095475-Liver, pubmed-meshheading:15095475-Lysosomes, pubmed-meshheading:15095475-Male, pubmed-meshheading:15095475-Middle Aged, pubmed-meshheading:15095475-Protein Denaturation, pubmed-meshheading:15095475-Spleen
pubmed:year
2004
pubmed:articleTitle
Cleavage of AL amyloid proteins and AL amyloid deposits by cathepsins B, K, and L.
pubmed:affiliation
Institute of Pathology, Otto-von-Guericke-University of Magdeburg, Leipziger Strasse 44, D-39120 Magdeburg, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't