scholarly journals Membrane glycoprotein IV (CD36) is physically associated with the Fyn, Lyn, and Yes protein-tyrosine kinases in human platelets.

1991 ◽  
Vol 88 (17) ◽  
pp. 7844-7848 ◽  
Author(s):  
M. M. Huang ◽  
J. B. Bolen ◽  
J. W. Barnwell ◽  
S. J. Shattil ◽  
J. S. Brugge
1995 ◽  
Vol 270 (47) ◽  
pp. 28029-28036 ◽  
Author(s):  
Tatsuo Ichinohe ◽  
Hiroshi Takayama ◽  
Yasuharu Ezumi ◽  
Shigeru Yanagi ◽  
Hirohei Yamamura ◽  
...  

1996 ◽  
Vol 76 (05) ◽  
pp. 640-650 ◽  
Author(s):  
Shaun P Jackson ◽  
Simone M Schoenwaeider ◽  
Yuping Yuan ◽  
Hatem H Salem ◽  
Prasad Cooray

1990 ◽  
Vol 10 (7) ◽  
pp. 3806-3809
Author(s):  
J S Gutkind ◽  
P M Lacal ◽  
K C Robbins

Recent studies have shown that ligand-activated growth factor receptors as well as transforming versions of nonreceptor protein-tyrosine kinases physically associate with phosphatidylinositol-3 kinase (PI-3 kinase). Reasoning that PI-3 kinase might also play a role in the normal functions of nonreceptor kinases, we sought to determine whether association with PI-3 kinase might serve as a measure of nonreceptor protein-tyrosine kinase activation under physiological conditions. We found that p60c-src as well as p59fyn, the product of another member of the src family of proto-oncogenes, physically associated with a PI kinase activity within 5 s after exposure to thrombin. Furthermore, PI kinase reaction products generated in p60v-src, p60c-src or p59fyn containing immunoprecipitates were indistinguishable, demonstrating the identity of the associated enzyme as PI-3 kinase. These findings demonstrate a thrombin-dependent interaction between p60c-src or p59fyn and PI-3 kinase and suggest a role for nonreceptor protein-tyrosine kinases in human platelet signal transduction.


1990 ◽  
Vol 10 (7) ◽  
pp. 3806-3809 ◽  
Author(s):  
J S Gutkind ◽  
P M Lacal ◽  
K C Robbins

Recent studies have shown that ligand-activated growth factor receptors as well as transforming versions of nonreceptor protein-tyrosine kinases physically associate with phosphatidylinositol-3 kinase (PI-3 kinase). Reasoning that PI-3 kinase might also play a role in the normal functions of nonreceptor kinases, we sought to determine whether association with PI-3 kinase might serve as a measure of nonreceptor protein-tyrosine kinase activation under physiological conditions. We found that p60c-src as well as p59fyn, the product of another member of the src family of proto-oncogenes, physically associated with a PI kinase activity within 5 s after exposure to thrombin. Furthermore, PI kinase reaction products generated in p60v-src, p60c-src or p59fyn containing immunoprecipitates were indistinguishable, demonstrating the identity of the associated enzyme as PI-3 kinase. These findings demonstrate a thrombin-dependent interaction between p60c-src or p59fyn and PI-3 kinase and suggest a role for nonreceptor protein-tyrosine kinases in human platelet signal transduction.


Planta Medica ◽  
2008 ◽  
Vol 74 (03) ◽  
Author(s):  
Y Ye ◽  
LG Lin ◽  
H Xie ◽  
HL Li ◽  
HL Jiang ◽  
...  

1998 ◽  
Vol 246 (2) ◽  
pp. 375-377 ◽  
Author(s):  
Marek Pawlikowski ◽  
Lilla Lachowicz ◽  
Jolanta Kunert-Radek ◽  
Katarzyna Winczyk ◽  
Grażyna Janiszewska ◽  
...  

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