Source:http://linkedlifedata.com/resource/pubmed/id/12871329
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
2003-7-21
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pubmed:abstractText |
Recently, we showed that localization of Glu-plasminogen on cell surfaces enhances its conversion to Lys-plasminogen by exogenous plasmin. This leads to stimulation of plasminogen activation because Lys-plasminogen is the preferred substrate on cell surfaces. Here, we show that Glu-plasminogen was converted to Lys-plasminogen on monocytoid cells in the absence of exogenous plasmin. Culture of cells under serum-free conditions did not affect this conversion, suggesting that the enzymatic activity was cell-derived. Therefore, we tested whether endogenous monocytoid plasminogen could provide a source of plasmin to convert cell-associated Glu-plasminogen to Lys-plasminogen because plasmin is the only enzyme known to effect this reaction. We used a recombinant human plasminogen mutant, [D(646)E]Pg, which can be cleaved by plasminogen activators, but cannot catalyze the generation of Lys-plasminogen. Upon incubation with either THP-1 or U937 monocytoid cells, 35 and 38%, respectively, of the cell-bound ligand was converted to Lys-[D(646)E]Pg. Trasylol, alpha2-antiplasmin, and an anticatalytic antiplasminogen monoclonal antibody decreased Lys-[D(646)E]Pg formation to < 5% on monocytoid cells, consistent with a plasmin-dependent mechanism. Plasminogen was detected in these cells by Northern blotting and RT-PCR. Our results suggest that plasmin converts cell-bound Glu-plasminogen to Lys-plasminogen and that this enzyme is produced by activation of monocytoid plasminogen by endogenous monocytoid plasminogen activators to enhance plasminogen activation on the monocytoid cell surface.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Fibrinolysin,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Plasminogen,
http://linkedlifedata.com/resource/pubmed/chemical/Plasminogen Activators,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/lysyl-plasminogen
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1538-7933
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
1
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1264-70
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:12871329-Cell Line,
pubmed-meshheading:12871329-Enzyme Activation,
pubmed-meshheading:12871329-Fibrinolysin,
pubmed-meshheading:12871329-Humans,
pubmed-meshheading:12871329-Monocytes,
pubmed-meshheading:12871329-Mutation,
pubmed-meshheading:12871329-Peptide Fragments,
pubmed-meshheading:12871329-Plasminogen,
pubmed-meshheading:12871329-Plasminogen Activators,
pubmed-meshheading:12871329-RNA, Messenger,
pubmed-meshheading:12871329-Recombinant Proteins
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pubmed:year |
2003
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pubmed:articleTitle |
Endogenous plasmin converts Glu-plasminogen to Lys-plasminogen on the monocytoid cell surface.
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pubmed:affiliation |
The Scripps Research Institute, CVN-26, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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