scholarly journals SRC-1, a non-receptor type of protein tyrosine kinase, controls the direction of cell and growth cone migration in C. elegans

Development ◽  
2005 ◽  
Vol 132 (23) ◽  
pp. 5161-5172 ◽  
Author(s):  
B. Itoh
Keyword(s):  
Tyrosine Kinase ◽  
Growth Cone ◽  
Protein Tyrosine Kinase ◽  
Receptor Type ◽  
Protein Tyrosine ◽  
C Elegans

scholarly journals Expression Profile of Receptor-Type Protein Tyrosine Kinase Genes in the Human Thyroid

Endocrinology ◽  
1998 ◽  
Vol 139 (3) ◽  
pp. 852-858 ◽  
Author(s):  
Kunihiko Tanaka ◽  
Yuji Nagayama ◽  
Toru Nakano ◽  
Noboru Takamura ◽  
Hiroyuki Namba ◽  
...  
Keyword(s):  
Tyrosine Kinase ◽  
Expression Profile ◽  
Protein Tyrosine Kinase ◽  
Receptor Type ◽  
Human Thyroid ◽  
Protein Tyrosine ◽  
Type Protein

Protein-tyrosine Kinase p72 syk Is Activated by Platelet Activating Factor in Platelets

1994 ◽  
Vol 72 (06) ◽  
pp. 937-941 ◽  
Author(s):  
Karim Rezaul ◽  
Shigeru Yanagi ◽  
Kiyonao Sada ◽  
Takanobu Taniguchi ◽  
Hirohei Yamamura
Keyword(s):  
Tyrosine Kinase ◽  
Tyrosine Phosphorylation ◽  
Protein Tyrosine Kinase ◽  
Kinase Inhibitor ◽  
Critical Role ◽  
Platelet Activating Factor ◽  
Kinase Assay ◽  
Potential Candidate ◽  
Protein Tyrosine ◽  
Induced Aggregation

SummaryIt has been demonstrated that activation of platelets by platelet-activating factor (PAF) results in a dramatic increase in tyrosine phosphorylation of several cellular proteins. We report here that p72 syk is a potential candidate for the protein-tyrosine phosphorylation following PAF stimulation in porcine platelets. Immunoprecipitation kinase assay revealed that PAF stimulation resulted in a rapid activation of p72 syk which peaked at 10 s. The level of activation was found to be dose dependent and could be completely inhibited by the PAF receptor antagonist, CV3988. Phosphorylation at the tyrosine residues of p72 syk coincided with activation of yllsyk. Pretreatment of platelets with aspirin and apyrase did not affect PAF induced activation of p72 syk .Furthermore, genistein, a potent protein-tyrosine-kinase inhibitor, diminished PAF-induced p72 syk activation and Ca2+ mobilization as well as platelet aggregation. These results suggest that p72 syk may play a critical role in PAF-induced aggregation, possibly through regulation of Ca2+ mobilization.

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