Role of Src protein tyrosine kinases in late preconditioning against myocardial infarction

2002 ◽  
Vol 283 (2) ◽  
pp. H549-H556 ◽  
Author(s):  
Buddhadeb Dawn ◽  
Hitoshi Takano ◽  
Xian-Liang Tang ◽  
Eitaro Kodani ◽  
Supratim Banerjee ◽  
...  
Keyword(s):  
Myocardial Infarction ◽  
Tyrosine Kinases ◽  
Coronary Occlusion ◽  
Group Iv ◽  
Protein Tyrosine Kinases ◽  
Protein Tyrosine ◽  
Group Iii ◽  
Late Preconditioning ◽  
Conscious Rabbits

Although Src protein tyrosine kinases (PTKs) have been shown to be essential in late preconditioning (PC) against myocardial stunning, their role in triggering versus mediating late PC against myocardial infarction remains unclear. Four groups of conscious rabbits were subjected to a 30-min coronary occlusion on day 2, with or without PC ischemia on day 1. Administration of the Src PTK inhibitor lavendustin A (LD-A; 1 mg/kg iv) before the PC ischemia on day 1 ( group III, n = 7) failed to block the delayed protective effect against myocardial infarction 24 h later. Late PC against infarction, however, was completely abrogated when LD-A was given 24 h after the PC ischemia, prior to the 30-min occlusion on day 2 ( group IV, n = 8). We conclude that, in conscious rabbits, Src PTK activity is necessary for the mediation of late PC protection against myocardial infarction on day 2, but not for the initiation of this phenomenon on day 1. Taken together with previous studies in the setting of stunning, these findings reveal heretofore unrecognized differences in the roles of Src PTKs in late PC against stunning versus late PC against infarction.

scholarly journals Bifunctional Role of Protein Tyrosine Kinases in Late Preconditioning Against Myocardial Stunning in Conscious Rabbits

1999 ◽  
Vol 85 (12) ◽  
pp. 1154-1163 ◽  
Author(s):  
Buddhadeb Dawn ◽  
Yu-Ting Xuan ◽  
Yumin Qiu ◽  
Hitoshi Takano ◽  
Xian-Liang Tang ◽  
...  
Keyword(s):  
Tyrosine Kinases ◽  
Myocardial Stunning ◽  
Protein Tyrosine Kinases ◽  
Protein Tyrosine ◽  
Late Preconditioning ◽  
Conscious Rabbits

Role of protein tyrosine kinases in CD40/interleukin-4-mediated isotype switching to IgE

1994 ◽  
Vol 94 (4) ◽  
pp. 784-792 ◽  
Author(s):  
Richard K.S. Loh ◽  
Haifa H. Jabara ◽  
Clement L. Ren ◽  
Shu Man Fu ◽  
Raif S. Geha
Keyword(s):  
Tyrosine Kinases ◽  
Protein Tyrosine Kinases ◽  
Interleukin 4 ◽  
Isotype Switching ◽  
Protein Tyrosine

scholarly journals Role of non-receptor protein tyrosine kinases in spermatid transport during spermatogenesis

2014 ◽  
Vol 30 ◽  
pp. 65-74 ◽  
Author(s):  
H.T. Wan ◽  
Dolores D. Mruk ◽  
Elizabeth I. Tang ◽  
Xiang Xiao ◽  
Yan-Ho Cheng ◽  
...  
Keyword(s):  
Tyrosine Kinases ◽  
Protein Tyrosine Kinases ◽  
Receptor Protein ◽  
Protein Tyrosine ◽  
Receptor Protein Tyrosine Kinases

scholarly journals FAK and PYK2 are specifically associated with the activated phagocytic receptor complexes from human U937 cells.

2021 ◽  
Author(s):  
Marwan G. AbidAlthagafi
Keyword(s):  
Cell Surface ◽  
Tyrosine Kinases ◽  
Laser Scanning ◽  
Surface Proteins ◽  
Protein Tyrosine Kinases ◽  
Macrophage Cell ◽  
Protein Tyrosine ◽  
Surface Receptors ◽  
Receptor Complexes

The innate immune system is the first shield against foreign attack inside the human body, and it is usually carried out with phagocytosis. An essential macrophage cell surface protein is the Fc receptor which contributes to the engulfment of unknown antigens. One of the important members of Fc receptors is the gamma receptor that binds to the immunoglobulin G (IgG) ligand. Another key receptor in this study is the CD36 receptor, which plays a crucial role in the progression of atherosclerosis, the hardening of arteries, with its ligand oxidized low-density lipoprotein (OxLDL). In this report, protein tyrosine kinase enzymes have been detected in the involvement of receptor complexes with human U937 macrophages, specifically PTK2 and PTK2b genes. Protein tyrosine kinases were known to promote cell migration as a main player in intracellular signal transduction cascades in relation to extracellular stimuli. Cell surface proteins are essential for the immunization of various diseases; yet, the molecular machinery of surface receptors remains unclear. This research primarily examined the dynamic nature of protein tyrosine kinases in an ongoing investigation of macrophage cell surface receptors, particularly the role of Fc γ and CD36 receptors with their ligands IgG and oxLDL coated beads in phagocytosis. Our report demonstrates a novel role of PTK2 and PTK2b functions in relation to U937 CD36-mediated phagocytosis. The Phagocytic efficiency of U937 macrophages was analyzed using laser scanning confocal microscope after silencing the cells with siRNA followed by quantitative counting of phagocytosis. The PF drug FAK inhibitor was also introduced to compare the phagocytic efficiency of siRNA cells.

Pleiotropic role of lyn kinase in leukotriene B4–induced eosinophil activation

Blood ◽  
2000 ◽  
Vol 95 (11) ◽  
pp. 3541-3547
Author(s):  
Oonagh T. Lynch ◽  
Mark A. Giembycz ◽  
Ian Daniels ◽  
Peter J. Barnes ◽  
Mark A. Lindsay
Keyword(s):  
Tyrosine Kinases ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Leukotriene B4 ◽  
Protein Tyrosine Kinases ◽  
Reduced Form ◽  
Intact Cells ◽  
Protein Tyrosine ◽  
Lyn Kinase ◽  
Eosinophil Activation

The authors have examined the role of the src-family of protein tyrosine kinases in leukotriene B4(LTB4)–induced activation of guinea-pig eosinophils. Western blot analysis identified the src-like protein tyrosine kinases p53lyn, p56lyn, p56/59hck, p55fgr, and p56lck whereas p60src, p62yes, p55blk, and p59fyn were not detected. LTB4 promoted a rapid increase in p53/56lyn activity in eosinophils, which peaked at 5 seconds and remained elevated at 60 seconds; hck, fgr, and lck were not activated. A role for p53/56lyn in eosinophil activation was investigated with the use of the src-selective inhibitor PP1 (1 μmol/L to 10 μmol/L), which attenuated LTB4-stimulated p53/56lyn activity and the phosphorylation of extracellular signal-regulated kinase–2 in intact cells. At comparable concentrations, PP1 was also shown to attenuate LTB4-induced nicotinamide adenine dinucleotide phosphate (reduced form) (NADPH) oxidase activation, chemotaxis, and Ca++-dependent [3H]arachidonic acid (AA) release. Moreover, an inhibitor of mitogen-activated protein kinase kinase-1, PD 098059, significantly inhibited LTB4-induced chemotaxis but had no effect on oxidant production or [3H]AA release. Collectively, these results implicate lyn kinase in LTB4-induced eosinophil activation through the recruitment of divergent cell-signaling pathways.

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