BETA(3) INTEGRIN DERIVED PEPTIDE-217-230 INHIBITS FIBRINOGEN BIDING AND PLATELET-AGGREGATION - SIGNIFICANCE OF RGD SEQUENCES AND FIBRINOGEN-A ALPHA-CHAIN

被引：22

作者：

LASZ, EC

MCLANE, MA

TRYBULEC, M

KOWALSKA, MA

KHAN, S

BUDZYNSKI, AZ

NIEWIAROWSKI, S

机构：

[1] TEMPLE UNIV,HLTH SCI CTR,SCH MED,DEPT PHYSIOL,PHILADELPHIA,PA 19140

[2] TEMPLE UNIV,HLTH SCI CTR,SCH MED,DEPT BIOCHEM,PHILADELPHIA,PA 19140

[3] TEMPLE UNIV,HLTH SCI CTR,SCH MED,SOL SHERRY THROMBOSIS RES CTR,PHILADELPHIA,PA 19140

[4] WISTAR INST,PHILADELPHIA,PA 19104

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1993年 / 190卷 / 01期

关键词：

D O I：

10.1006/bbrc.1993.1019

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：

β3 integrin derived peptides 217-230 (DAPEGGFDAIMQAT) and 217-231(Y) (DAPEGGFDAIMQATVY) at 100 μM inhibited 125I-fibrinogen binding to ADP-stimulated platelets and platelet aggregation. Peptide 217-231(Y) (100 μM) significantly inhibited the binding of 125I-albolabrin (a disintegrin with a single RGD sequence) to ADP and thrombin-activated platelets while it had only a slight effect on albolabrin binding to resting platelets. The 125I-β3 217-231(Y) cross-linked selectively to the fibrinogen Aα-chain. The interaction of the RGD sequence in the Aα-chain of fibrinogen with β3 217-231 sequence appears to play a significant role in the events leading to platelet aggregation. © 1993 Academic Press, Inc.

引用

页码：118 / 124

页数：7

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