PHOTOAFFINITY-LABELING OF INTEGRIN ALPHA-IIB-BETA-3 (GLYCOPROTEIN IIB-IIIA) ON INTACT PLATELETS WITH 8-AZIDO-[GAMMA-P-32]ATP

被引：14
|
作者：
MAYINGER, P [1 ]
GAWAZ, M [1 ]
机构：
[1] UNIV MUNICH,KLINIKUM GROSSHADERN,MED 1 KLIN,MARCHIONINISTR 15,W-8000 MUNICH 70,GERMANY
来源：
BIOCHIMICA ET BIOPHYSICA ACTA | 1992年 / 1137卷 / 01期
关键词：
PLATELET; GPIIB-IIIA; INTEGRIN ALPHA-IIB-BETA-3; NUCLEOTIDE BINDING; PHOTOAFFINITY LABELING; 8-AZIDO-ATP;
D O I：
10.1016/0167-4889(92)90103-I
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The fibrinogen receptor GPIIb-IIIa plays a crucial role in platelet aggregation. Here we show that the adenine nucleotide, 8-azido-ATP, inhibits ADP-induced conformational change of the platelet fibrinogen receptor GPIIb-IIIa (integrin alphaIIbbeta3). Photoaffinity labeling of intact platelets with 8-azido-[gamma-P-32]ATP exclusively modifies two plasma-membrane glycoproteins which are identical with both subunits of GPIIb-IIIa. The presence of adenine-nucleotide-binding sites on GPIIb-IIIa implies that the platelet fibrinogen receptor is directly regulated by extracellular adenine nucleotides.
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页码：77 / 81
页数：5
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