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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
1995-2-23
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pubmed:abstractText |
Protease nexin-2/amyloid beta-protein precursor (PN-2/A beta PP) is a Kunitz-type protease inhibitor which has been shown to be a tight-binding inhibitor of enzymes, factors XIa and IXa (FIXa), suggesting a role for this protein in hemostasis. Since coagulant reactions are modulated on biologic surfaces, we investigated how 25:75 (mol/mol) phosphatidylserine/phosphatidylcholine vesicles (PSPC), thrombin-activated platelets, or umbilical vein endothelial cells influence inactivation of FIXa by PN-2/A beta PP. The Km of human or porcine FIXa activation of human factor X in the presence of PSPC, activated platelets, or endothelial cells in the absence or presence of thrombin-activated factor VIII (FVIIIa) was similar, (0.05-0.39 microM). The presence of FVIIIa increased the catalytic efficiency (kcat/Km ratio) of human and porcine factor IXa's activation of factor X 4952-406-fold, respectively. In the presence of PSPC, the Ki of human and porcine FIXa inhibition by PN-2/A beta PP was Ki = 1.9 x 10(-9) M and 5.8 x 10(-9) M, respectively. After the addition of FVIIIa to the reaction, the Ki for both human and porcine FIXa inhibition by PN-2/A beta PP on PSPC increased 13- and 4-fold to Ki = 2.5 x 10(-8) M and 2.4 x 10(-8) M, respectively. These Ki for inhibition of human FIXa on phospholipid vesicles by PN-2/A beta PP were similar when factor X activation was measured by chromogenic or activation peptide release assays. FVIIIa reduced the inhibition of FIXa by PN-2/A beta PP only in the presence of PSPC.(ABSTRACT TRUNCATED AT 250 WORDS)
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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/APP protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Amyloid beta-Protein Precursor,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Factor IXa,
http://linkedlifedata.com/resource/pubmed/chemical/Factor VIIIa,
http://linkedlifedata.com/resource/pubmed/chemical/Factor X,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylcholines,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylserines,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipids,
http://linkedlifedata.com/resource/pubmed/chemical/Protease Nexins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
31
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pubmed:volume |
34
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1171-8
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:7827067-Amyloid beta-Protein Precursor,
pubmed-meshheading:7827067-Animals,
pubmed-meshheading:7827067-Blood Platelets,
pubmed-meshheading:7827067-Carrier Proteins,
pubmed-meshheading:7827067-Cell Membrane,
pubmed-meshheading:7827067-Enzyme Activation,
pubmed-meshheading:7827067-Factor IXa,
pubmed-meshheading:7827067-Factor VIIIa,
pubmed-meshheading:7827067-Factor X,
pubmed-meshheading:7827067-Humans,
pubmed-meshheading:7827067-Kinetics,
pubmed-meshheading:7827067-Phosphatidylcholines,
pubmed-meshheading:7827067-Phosphatidylserines,
pubmed-meshheading:7827067-Phospholipids,
pubmed-meshheading:7827067-Protease Nexins,
pubmed-meshheading:7827067-Receptors, Cell Surface,
pubmed-meshheading:7827067-Swine
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pubmed:year |
1995
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pubmed:articleTitle |
Factor IXa inhibition by protease nexin-2/amyloid beta-protein precursor on phospholipid vesicles and cell membranes.
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pubmed:affiliation |
Department of Internal Medicine, University of Michigan, Ann Arbor 48109-0724.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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