Signaling pathways of the F11 receptor (F11R; a.k.a. JAM-1, JAM-A) in human platelets: F11R dimerization, phosphorylation and complex formation with the integrin GPIIIa

被引：40
|
作者：
Sobocka, MB
Sobocki, T
Babinska, A
Hartwig, JH
Li, MG
Ehrlich, YH
Kornecki, E
机构：
[1] Suny Downstate Med Ctr, Dept Anat & Cell Biol, Brooklyn, NY 11203 USA
[2] CUNY Coll Staten Isl, Dept Biol, Staten Isl, NY USA
[3] CUNY Coll Staten Isl, Neurosci Program, Staten Isl, NY USA
[4] CUNY Coll Staten Isl, Dept Chem, Staten Isl, NY USA
[5] Harvard Univ, Sch Med, Brigham & Womens Hosp, Dept Med,Div Expt Med & Hematol Oncol, Boston, MA USA
来源：
JOURNAL OF RECEPTORS AND SIGNAL TRANSDUCTION | 2004年 / 24卷 / 1-2期
关键词：
F11; receptor; F11R; junctional adhesion molecule; JAM; JAM-1; JAM-A; PI-3; kinase; calcium ions; platelet aggregation; cell adhesion molecule (CAM); F11 receptor dimerization; integrin GPIIIa;
D O I：
10.1081/RRS-120034252
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 F11 receptor (F11R) (a.k.a. Junctional Adhesion Molecule, JAM) was first identified in human platelets as a 32/35 kDa protein duplex that serves as receptor for a functional monoclonal antibody that activates platelets. We have sequenced and cloned the F11R and determined that it is a member of the immunoglobulin (Ig) superfamily of cell adhesion molecules. The signaling pathways involved in F11R-induced platelet activation were examined in this investigation. The binding of M.Ab.F11 to the platelet F11R resulted in granule secretion and aggregation.
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收藏
页码：85 / 105
页数：21
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