Nonreceptor Protein-Tyrosine Kinases in Neutrophil Activation

Methods ◽  
1996 ◽  
Vol 9 (3) ◽  
pp. 607-618 ◽  
Author(s):  
Heidi Welch ◽  
Corinne Mauran ◽  
Isabelle Maridonneau-Parini
Keyword(s):  
Tyrosine Kinases ◽  
Neutrophil Activation ◽  
Protein Tyrosine Kinases ◽  
Protein Tyrosine ◽  
Nonreceptor Protein Tyrosine Kinases

Thrombin-dependent association of phosphatidylinositol-3 kinase with p60c-src and p59fyn in human platelets

1990 ◽  
Vol 10 (7) ◽  
pp. 3806-3809
Author(s):  
J S Gutkind ◽  
P M Lacal ◽  
K C Robbins
Keyword(s):  
Tyrosine Kinases ◽  
Protein Tyrosine Kinase ◽  
Human Platelets ◽  
Protein Tyrosine Kinases ◽  
Reaction Products ◽  
Phosphatidylinositol 3 Kinase ◽  
Protein Tyrosine ◽  
Nonreceptor Protein Tyrosine Kinases ◽  
Pi Kinase ◽  
Phosphatidylinositol 3

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.

scholarly journals The FER gene is evolutionarily conserved and encodes a widely expressed member of the FPS/FES protein-tyrosine kinase family.

1989 ◽  
Vol 9 (12) ◽  
pp. 5722-5725 ◽  
Author(s):  
T Pawson ◽  
K Letwin ◽  
T Lee ◽  
Q L Hao ◽  
N Heisterkamp ◽  
...  
Keyword(s):  
Tyrosine Kinase ◽  
Gene Product ◽  
Tyrosine Kinases ◽  
Protein Tyrosine Kinase ◽  
Protein Tyrosine Kinases ◽  
Protein Tyrosine ◽  
New Family ◽  
Evolutionarily Conserved ◽  
Conserved Gene ◽  
Nonreceptor Protein Tyrosine Kinases

We have recently isolated human and rat cDNAs (designated FER and flk, respectively) which encode nonreceptor protein-tyrosine kinases which are very similar to one another and related in sequence and domain structure to the c-fps/fes gene product. We show that FER and flk are human and rat counterparts of an evolutionarily conserved gene, hereafter termed FER regardless of species. The human and rat FER genes encode a widely expressed 94-kilodalton protein-tyrosine kinase which is antigenically related to the fps/fes protein-tyrosine kinase. The structural and antigenic similarities between the FER and fps/fes proteins suggest that they are members of a new family of nonreceptor protein-tyrosine kinases.

scholarly journals Thrombin-dependent association of phosphatidylinositol-3 kinase with p60c-src and p59fyn in human platelets.

1990 ◽  
Vol 10 (7) ◽  
pp. 3806-3809 ◽  
Author(s):  
J S Gutkind ◽  
P M Lacal ◽  
K C Robbins
Keyword(s):  
Tyrosine Kinases ◽  
Protein Tyrosine Kinase ◽  
Human Platelets ◽  
Protein Tyrosine Kinases ◽  
Reaction Products ◽  
Phosphatidylinositol 3 Kinase ◽  
Protein Tyrosine ◽  
Nonreceptor Protein Tyrosine Kinases ◽  
Pi Kinase ◽  
Phosphatidylinositol 3

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.

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