scholarly journals Platelet Glycoprotein IIIa Gene Polymorphism (Leu33Pro) and Aspirin Resistance in a Very Elderly Chinese Population

2014 ◽  
Vol 18 (6) ◽  
pp. 389-393 ◽  
Author(s):  
Bei-Yun Wang ◽  
Shi-Jin Tan
Keyword(s):  
Gene Polymorphism ◽  
Chinese Population ◽  
Aspirin Resistance ◽  
Platelet Glycoprotein ◽  
Very Elderly ◽  
Elderly Chinese ◽  
Glycoprotein Iiia

Glycoprotein IIIA Gene (PIA) Polymorphism and Aspirin Resistance: Is There Any Correlation?

2005 ◽  
Vol 39 (6) ◽  
pp. 1013-1018 ◽  
Author(s):  
Elod Papp ◽  
Viktoria Havasi ◽  
Judit Bene ◽  
Katalin Komlosi ◽  
Laszlo Czopf ◽  
...  
Keyword(s):  
Adenosine Diphosphate ◽  
Aspirin Resistance ◽  
Platelet Glycoprotein ◽  
Control Group ◽  
Inadequate Response ◽  
Platelet Response ◽  
Vascular Events ◽  
Coronary Syndrome ◽  
Increased Risk ◽  
Glycoprotein Iiia

BACKGROUND: Platelet glycoprotein (GP) IIb/IIIa receptors play an inevitable role in platelet aggregation. The GP IIIa gene is polymorphic ( PIA1/PIA2) and the presence of a PIA2 allele might be associated with an increased risk for acute coronary syndrome (ACS). OBJECTIVE: To examine the prevalence of the PIA2 allele in patients with ACS and in subjects with or without aspirin resistance. METHODS: The prevalence of the PIA2 allele was assessed in 158 patients with ACS and PIA2 compared with its prevalence in 199 healthy volunteers. The antiplatelet efficacy of aspirin was examined in all patients with ACS, as well as in 69 individuals who had suffered ischemic stroke and in 58 high-risk subjects without any known ischemic vascular events. RESULTS: PIA2 prevalence was significantly higher in patients with ACS (59/158) than in the control group (51/199; p < 0.05). Carriers of the PIA2 allele had a significantly higher risk of developing ACS, even after an adjustment to the risk factors (OR 5.74; 95% CI 1.75 to 18.8; p = 0.004). The occurrence of the PIA2 allele was significantly higher among patients with aspirin resistance than in subjects who demonstrated an appropriate response to the drug (allele frequencies, 0.21 vs 0.14; p < 0.05). All patients homozygous for the PIA2 allele had an inadequate platelet response to aspirin. CONCLUSIONS: Our results support the hypothesis that carriers of the PIA2 allele might have an increased risk for ACS. PIA2 homozygosity was associated with an inadequate response to aspirin therapy. Our data further suggest that patients with PIA2 allele homozygosity might benefit from antiplatelet therapy based on adenosine diphosphate antagonists throughout secondary treatment for prevention of ACS.

Platelet glycoprotein IIIa Leu33Pro gene polymorphism and coronary artery disease: A meta-analysis of cohort studies

Platelets ◽  
2014 ◽  
Vol 26 (6) ◽  
pp. 530-535 ◽  
Author(s):  
Monica Verdoia ◽  
Ettore Cassetti ◽  
Alon Schaffer ◽  
Gabriella Di Giovine ◽  
Giuseppe De Luca
Keyword(s):  
Coronary Artery Disease ◽  
Coronary Artery ◽  
Gene Polymorphism ◽  
Cohort Studies ◽  
Meta Analysis ◽  
Platelet Glycoprotein ◽  
Glycoprotein Iiia ◽  
Artery Disease

Platelet glycoprotein IIIa gene polymorphism and myocardial infarction

The Lancet ◽  
1996 ◽  
Vol 348 (9037) ◽  
pp. 1309-1310 ◽  
Author(s):  
SV Osborn ◽  
KK Hampton ◽  
D Smillie ◽  
KS Channer ◽  
ME Daly
Keyword(s):  
Myocardial Infarction ◽  
Gene Polymorphism ◽  
Platelet Glycoprotein ◽  
Glycoprotein Iiia

scholarly journals Cognitive function and 3-year mortality in the very elderly Chinese population with chronic kidney disease

2018 ◽  
Vol Volume 13 ◽  
pp. 2055-2060 ◽  
Author(s):  
Kunhao Bai ◽  
Yujing Pan ◽  
Fanghong Lu ◽  
Yingxin Zhao ◽  
Fang Wang ◽  
...  
Keyword(s):  
Chronic Kidney Disease ◽  
Cognitive Function ◽  
Kidney Disease ◽  
Chinese Population ◽  
Very Elderly ◽  
Elderly Chinese

Specific Cross-reaction of IgG Anti-phospholipid Antibody with Platelet Glycoprotein IIIa

1996 ◽  
Vol 75 (01) ◽  
pp. 168-174 ◽  
Author(s):  
Shigeru Tokita ◽  
Morio Arai ◽  
Naomasa Yamamoto ◽  
Yasuhiro Katagiri ◽  
Kenjiro Tanoue ◽  
...  
Keyword(s):  
Platelet Aggregation ◽  
Heparan Sulfate ◽  
Disulfide Bonds ◽  
Dextran Sulfate ◽  
Human Platelets ◽  
Platelet Glycoprotein ◽  
Activated Platelets ◽  
Fibrinogen Binding ◽  
Dose Dependent Fashion ◽  
Glycoprotein Iiia

SummaryTo study the pathological functions of anti-phospholipid (anti-PL) antibodies, we have analyzed their effect on platelet function. We identified an IgG anti-PL mAb, designated PSG3, which cross-reacted specifically with glycoprotein (GP) IIIa in human platelets and inhibited platelet aggregation. PSG3 bound also to certain polyanionic substances, such as double-stranded DNA, heparan sulfate, dextran sulfate and acetylated-LDL, but not to other polyanionic substances. The binding of PSG3 to GPIIIa was completely inhibited by heparan sulfate and dextran sulfate, indicating that PSG3 recognizes a particular array of negative charges expressed on both GPIIIa and the specified polyanionic substances. Since neither neuraminidase- nor endoglycopeptidase F-treatment of GPIIIa had any significant effect on the binding of PSG3, this array must be located within the amino acid sequence of GPIIIa but not in the carbohydrate moiety. Reduction of the disulfide bonds in GPIIIa greatly reduced its reactivity, suggesting that the negative charges in the epitope are arranged in a particular conformation. PSG3 inhibited platelet aggregation induced by either ADP or collagen, it also inhibited fibrinogen binding to activated platelets in a dose-dependent fashion. PSG3, however, did not inhibit the binding of GRGDSP peptide to activated platelets. These results suggest that the PSG3 epitope on GPIIIa contains a particular array of negative charges, and possibly affects the fibrinogen binding to GPIIb/IIIa complex necessary for platelet aggregation.

scholarly journals Further studies on the topography of the N-terminal region of human platelet glycoprotein IIIa. Localization of monoclonal antibody epitopes and the putative fibrinogen-binding sites

1991 ◽  
Vol 274 (2) ◽  
pp. 457-463 ◽  
Author(s):  
J J Calvete ◽  
J Arias ◽  
M V Alvarez ◽  
M M Lopez ◽  
A Henschen ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Binding Sites ◽  
Human Platelet ◽  
Binding Domain ◽  
Terminal Region ◽  
Platelet Glycoprotein ◽  
Gamma Chain ◽  
Fibrinogen Binding ◽  
Glycoprotein Iiia ◽  
Membrane Bound

The precise localization of the epitopes for six monoclonal antibodies specific for the N-terminal region of human platelet glycoprotein IIIa (GPIIIa) was determined. The epitope for P37, a monoclonal antibody that inhibits platelet aggregation, was found at GPIIIa 101-109, flanked by the epitopes for P23-3 (GPIIIa 16-28), P23-4 (GPIIIa 83-91), P23-5 (GPIIIa 67-73), P23-7 (GPIIIa 114-122) and P40 (GPIIIa 262-302), and very close to the early chymotryptic cleavage site of GPIIIa in whole platelets (Phe-100). When the amino acid sequence of GPIIIa was searched for peptide sequences hydropathically complementary to the fibrinogen gamma-chain C-terminal (gamma 400-411) and A alpha-chain RGD-containing peptides, none was found for the gamma 400-411, two (GPIIIa 128-132 and 380-384) were found complementary to fibrinogen A alpha 571-575 and two (GPIIIa 109-113 and 129-133) were found for A alpha 94-99. Two of these putative fibrinogen-binding sites overlap with each other, and a third one overlaps with the epitope for P37. These findings reinforce the earlier suggestion that the N-terminal region of GPIIIa is involved in fibrinogen binding, and suggest the existence in GPIIIa of either multiple or alternative RGD-binding sites or one RGD-binding domain with several moieties. Finally, early chymotryptic cleavage of GPIIIa in whole platelets liberates to the soluble fraction the peptide stretch Ser-101-Tyr-348, which carries the epitope for P37 and the putative binding sites for fibrinogen. The rest of the molecule, together with the GPIIb-resistant moiety, remains membrane-bound. This leads us to propose that the fibrinogen-binding domain of GPIIIa is not involved in the binding to GPIIb to form the Ca2(+)-dependent GPIIb-GPIIIa complex.

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