scholarly journals Signalling during hypoxia in human T lymphocytes - critical role of the src protein tyrosine kinase p56Lck in the O2sensitivity of Kv1.3 channels

2006 ◽  
Vol 573 (2) ◽  
pp. 357-370 ◽  
Author(s):  
Peter Szigligeti ◽  
Lisa Neumeier ◽  
Eugene Duke ◽  
Claire Chougnet ◽  
Koichi Takimoto ◽  
...  
Keyword(s):  
T Lymphocytes ◽  
Tyrosine Kinase ◽  
Protein Tyrosine Kinase ◽  
Critical Role ◽  
Protein Tyrosine ◽  
Human T Lymphocytes ◽  
Kv1.3 Channels

scholarly journals Molecular cloning of SKAP55, a novel protein that associates with the protein tyrosine kinase p59 in human T-lymphocytes.

1997 ◽  
Vol 272 (48) ◽  
pp. 30589
Author(s):  
Anne Marie-Cardine ◽  
Eddy Bruyns ◽  
Anne M. Verhagen ◽  
Christoph Eckerskorn ◽  
Henning Kirchgessner ◽  
...  
Keyword(s):  
T Lymphocytes ◽  
Tyrosine Kinase ◽  
Molecular Cloning ◽  
Protein Tyrosine Kinase ◽  
Protein Tyrosine ◽  
Human T Lymphocytes ◽  
Novel Protein

scholarly journals Molecular Cloning of SKAP55, a Novel Protein That Associates with the Protein Tyrosine Kinase p59fynin Human T-lymphocytes

1997 ◽  
Vol 272 (26) ◽  
pp. 16077-16080 ◽  
Author(s):  
Anne Marie-Cardine ◽  
Eddy Bruyns ◽  
Christoph Eckerskorn ◽  
Henning Kirchgessner ◽  
Stefan C. Meuer ◽  
...  
Keyword(s):  
T Lymphocytes ◽  
Tyrosine Kinase ◽  
Molecular Cloning ◽  
Protein Tyrosine Kinase ◽  
Protein Tyrosine ◽  
Human T Lymphocytes ◽  
Novel Protein

Human T lymphocytes express a protein-tyrosine kinase homologous to p56LSTRA

1986 ◽  
Vol 888 (3) ◽  
pp. 286-295 ◽  
Author(s):  
J.M. Trevillyan ◽  
Y. Lin ◽  
S.J. Chen ◽  
C.A. Phillips ◽  
C. Canna ◽  
...  
Keyword(s):  
T Lymphocytes ◽  
Tyrosine Kinase ◽  
Protein Tyrosine Kinase ◽  
Protein Tyrosine ◽  
Human T Lymphocytes

scholarly journals The CD4 receptor is complexed in detergent lysates to a protein-tyrosine kinase (pp58) from human T lymphocytes.

1988 ◽  
Vol 85 (14) ◽  
pp. 5190-5194 ◽  
Author(s):  
C. E. Rudd ◽  
J. M. Trevillyan ◽  
J. D. Dasgupta ◽  
L. L. Wong ◽  
S. F. Schlossman
Keyword(s):  
T Lymphocytes ◽  
Tyrosine Kinase ◽  
Protein Tyrosine Kinase ◽  
Protein Tyrosine ◽  
Cd4 Receptor ◽  
Human T Lymphocytes

scholarly journals Role of Protein Tyrosine Kinase p53/56lyn in Diminished Lipopolysaccharide Priming of Formylmethionylleucyl- phenylalanine-Induced Superoxide Production in Human Newborn Neutrophils

2004 ◽  
Vol 72 (11) ◽  
pp. 6455-6462 ◽  
Author(s):  
Sen Rong Yan ◽  
David M. Byers ◽  
Robert Bortolussi
Keyword(s):  
Tyrosine Kinase ◽  
Tyrosine Kinases ◽  
Protein Tyrosine Kinase ◽  
Kinase Inhibitor ◽  
Critical Role ◽  
Polymorphonuclear Neutrophils ◽  
Protein Tyrosine Kinases ◽  
Protein Tyrosine ◽  
Adult Cells

ABSTRACT Human newborns are more susceptible than adults to bacterial infection. With gram-negative bacteria, this may be due to a diminished response of newborn leukocytes to lipopolysaccharide (LPS). Since protein tyrosine kinase inhibition abolishes LPS priming in adult cells, we hypothesized that protein tyrosine kinases may have a critical role in LPS priming of polymorphonuclear neutrophils (PMNs) and that newborn PMNs may have altered protein tyrosine kinase activities. In the present study, we investigated the role of src family protein tyrosine kinases in the LPS response of newborn PMNs compared to adult cells. In a respiratory assay, the LPS-primed increase in formylmethionylleucylphenylalanine (fMLP)-triggered O2 − release by adult PMNs was greatly decreased by PP1 [4-amino-5-(4-methyphenyl)-7-(t-butyl)pyrazolo[3,4-d]pyrimidine], a src kinase inhibitor, to the level of untreated newborn PMNs, in which LPS failed to prime. LPS activated the src-like kinases p59hck (HCK) and p58fgr (FGR) in both adult and newborn PMNs but increased the activation of p53/56 lyn (LYN) only in adult cells. In newborn PMNs, LYN was highly phosphorylated independent of LPS. We evaluated subcellular fractions of PMNs and found that the phosphorylated form of LYN was mainly in the Triton-extractable, cytosolic fraction in adult PMNs, while in newborn cells it was located mainly in Triton-insoluble, granule- and membrane-associated fractions. In contrast, the phosphorylated mitogen-activated protein kinases ERK1/2 and p38 were mainly detected in the cytosol in both adult and newborn PMNs. These data indicate a role for LYN in the regulation of LPS priming. The trapping of phosphorylated LYN in the membrane-granule fraction in newborn PMNs may contribute to the deficiency of newborn cells in responding to LPS stimulation.

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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