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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
1992-9-10
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pubmed:abstractText |
Degradation of cartilage proteoglycans was investigated under neutral conditions (pH 7.5) by using pig kidney calpain II (EC 3.4.22.17; Ca(2+)-dependent cysteine proteinase). Aggregate and monomer degradation reached a maximum in 5 min at 30 degrees C when the substrate/enzyme ratio was less than 1000:1. The mode of degradation was limited proteolysis of the core protein; the size of the products was larger than that of papain-digested products and comparable with that of trypsin-digested products. The hyaluronic acid-binding region was lost from the major glycosaminoglycan-bearing region after incubation with calpain II. Calpains thus may affect the form of proteoglycans in connective tissue. Ca(2+)-dependent proteoglycan degradation was unique in that proteoglycans adsorb large amounts of Ca2+ ions rapidly before activation of calpain II: 1 mg of pig cartilage proteoglycan monomer adsorbed 1.3-1.6 mu equiv. of Ca2+ ions before activation of calpain II, which corresponds to half the sum of anion groups in glycosaminoglycan side chains. This adsorption of Ca2+ was lost after solvolysis of proteoglycan monomer with methanol/50 mM-HCl, which was used to desulphate glycosaminoglycans. Therefore cartilage proteoglycans are not merely the substrates of proteolysis, but they may regulate the activation of Ca(2+)-dependent enzymes including calpains through tight chelation of Ca2+ ions between glycosaminoglycan side chains.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1497624-125282,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1497624-126029,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1497624-13971270,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1497624-1984047,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1497624-2016996,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1497624-2189416,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1497624-2268476,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1497624-2719651,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1497624-2785800,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1497624-2824061,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1497624-2840990,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1497624-2981585,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1497624-3000474,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1497624-3021343,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1497624-3107779,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1497624-3124744,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1497624-3827853,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1497624-4091285,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1497624-5241522,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1497624-603625,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1497624-6088477,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1497624-6089371,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1497624-6092335,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1497624-6174523,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1497624-6277880,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1497624-6306001,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1497624-6337000,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1497624-6348946,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1497624-6643472,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1497624-6754738,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1497624-6771253,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1497624-6781489,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1497624-6897650
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
285 ( Pt 3)
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
857-62
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pubmed:dateRevised |
2010-9-7
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pubmed:meshHeading |
pubmed-meshheading:1497624-Animals,
pubmed-meshheading:1497624-Binding Sites,
pubmed-meshheading:1497624-Calcium,
pubmed-meshheading:1497624-Calpain,
pubmed-meshheading:1497624-Chondroitin Sulfates,
pubmed-meshheading:1497624-Humans,
pubmed-meshheading:1497624-Hyaluronic Acid,
pubmed-meshheading:1497624-Kidney,
pubmed-meshheading:1497624-Kinetics,
pubmed-meshheading:1497624-Macromolecular Substances,
pubmed-meshheading:1497624-Papain,
pubmed-meshheading:1497624-Proteoglycans,
pubmed-meshheading:1497624-Swine,
pubmed-meshheading:1497624-Trypsin
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pubmed:year |
1992
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pubmed:articleTitle |
Characterization of proteoglycan degradation by calpain.
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pubmed:affiliation |
Department of Orthopedic Surgery, Faculty of Medicine, Kyoto University, Japan.
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pubmed:publicationType |
Journal Article,
Comparative Study
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