Linked Life Data

15613921

Source:http://linkedlifedata.com/resource/pubmed/id/15613921

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
2004-12-22
pubmed:abstractText
Histidine-proline-rich glycoprotein (HPRG) has long been known to associate with plasminogen (Plg) in solution, but the consequences of this interaction have not been defined. Here we show that HPRG adsorbed to a glycosaminoglycan (GAG) surface also binds Plg with a Kd value of 0.7 micromol/l. Moreover, we present evidence that HPRG acts as a modulator of the activation of Plg by tissue-type Plg activator. Specifically, Plg complexed with HPRG on a GAG surface is more readily activated by tissue-type Plg activator than free Plg, with a 10-fold difference in apparent catalytic efficiency (kcat/Km). HPRG also augments the increase in Plg activation caused by fibrinogen fragments either in solution or on GAG surfaces. In contrast, HPRG abrogates the stimulatory effects of fibrinogen on Plg activation in solution. These observations demonstrate that HPRG can act as either a positive or negative effector of Plg activation in vitro and may serve as a modulator of fibrinolysis in vivo.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0957-5235
pubmed:author
pubmed:issnType
Print
pubmed:volume
15
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
663-72
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Effects of histidine-proline-rich glycoprotein on plasminogen activation in solution and on surfaces.
pubmed:affiliation
Division of Molecular Biology and Biochemistry, School of Biological Sciences, University of Missouri-Kansas City, Kansas City, Missouri 64110-2499, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't