Source:http://linkedlifedata.com/resource/pubmed/id/12945873
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
|
pubmed:dateCreated |
2003-8-29
|
pubmed:abstractText |
Nitric oxide (NO) is known to modulate platelet adhesion and aggregation, which are both mediated by fibrinogen receptor glycoprotein (GP)IIb/IIIa. To investigate effects of NO on GPIIb/IIIa activation and inactivation, platelets were exposed to NO donor 3-morpholino-sydnonimine (SIN-1) before and after stimulation with different agonists: thromboxane analog U-46619, epinephrine, adenosine diphosphate, human a-thrombin, and phorbol-12-myristate-13-acetate (0.02 micromol/l). (1) Flow cytometry analysis of SIN-1-pre-incubated samples using PAC-1 monoclonal antibody revealed an inhibition of receptor activation by 80.9 +/- 1.2, 71.3 +/- 1.8, 56 +/- 4.9, 87 +/- 3.4, and 56 +/- 5% (mean +/- SEM, relative to baseline). (2) Administration of SIN-1 after stimulation reversed receptor activation by 55 +/- 5.2, 56 +/- 2.0, 53 +/- 5.4, 42 +/- 4.3, and 44 +/- 5%, respectively. With 0.1 micromol/l phorbol-12-myristate-13-acetate, GPIIb/IIIa activation was irreversible. (3) SIN-1 effects could completely be blocked by equimolar addition of guanylyl cyclase inhibitor 1H(1,2,4)oxadiazolo(4,3-alpha)quinoxalin-1-on. (4) Spontaneous receptor closure after activation with human alpha-thrombin and adenosine diphosphate was not due to platelet-derived NO; SIN-1, however accelerated spontaneous receptor inactivation. (5) SIN-1-inactivated receptors still responded to stimulation. In conclusion, SIN-1 or NO modulates GPIIb/IIIa conformational change in vitro via guanosine 3',5'-monophosphate-dependent pathways. Whereas spontaneous receptor inactivation may be enhanced by exogenous NO, platelet-derived NO is not involved in receptor inactivation.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/3-morpholino-sydnonimine,
http://linkedlifedata.com/resource/pubmed/chemical/Molsidomine,
http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide Donors,
http://linkedlifedata.com/resource/pubmed/chemical/Platelet Aggregation Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Platelet Glycoprotein GPIIb-IIIa...
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jun
|
pubmed:issn |
0957-5235
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
14
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
327-34
|
pubmed:dateRevised |
2007-11-15
|
pubmed:meshHeading |
pubmed-meshheading:12945873-Blood Platelets,
pubmed-meshheading:12945873-Flow Cytometry,
pubmed-meshheading:12945873-Humans,
pubmed-meshheading:12945873-Molsidomine,
pubmed-meshheading:12945873-Nitric Oxide Donors,
pubmed-meshheading:12945873-Platelet Aggregation Inhibitors,
pubmed-meshheading:12945873-Platelet Glycoprotein GPIIb-IIIa Complex,
pubmed-meshheading:12945873-Statistics as Topic,
pubmed-meshheading:12945873-Time Factors
|
pubmed:year |
2003
|
pubmed:articleTitle |
Inactivation of platelet glycoprotein IIb/IIIa receptor by nitric oxide donor 3-morpholino-sydnonimine.
|
pubmed:affiliation |
Department of Anaesthesiology, Charité Campus Virchow-Klinikum, Berlin, Germany. didier.keh@charite.de
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|