scholarly journals The src-family protein-tyrosine kinase p59hck is located on the secretory granules in human neutrophils and translocates towards the phagosome during cell activation

1995 ◽  
Vol 309 (2) ◽  
pp. 657-665 ◽  
Author(s):  
H Möhn ◽  
V Le Cabec ◽  
S Fischer ◽  
I Maridonneau-Parini
Keyword(s):  
Subcellular Localization ◽  
Tyrosine Kinase ◽  
Protein Tyrosine Kinase ◽  
Cell Activation ◽  
Secretory Granules ◽  
Human Neutrophils ◽  
Intracellular Traffic ◽  
Hl60 Cells ◽  
Protein Tyrosine ◽  
Family Protein

The src-family protein-tyrosine kinase p59hck is mainly expressed in neutrophils; however, its functional role in these cells is unknown. Several other src-family members are localized on secretory vesicles and have been proposed to regulate intracellular traffic. We have established here the subcellular localization of p59hck in human neutrophils. Immunoblotting of subcellular fractions showed that approx. 60% of the p59hck per cell is localized on the secretory granules; the other 40% is distributed equally between non-granular membranes and the cytosol. Immunofluorescence of neutrophils and HL60 cells suggests that the p59hck-positive granules are azurophil granules. Granular p59hck is highly susceptible to degradation by an azurophil-granule proteinase. Different forms of p59hck occur in the three subcellular compartments: a 61 kDa form is mainly found in the granules, a 59 kDa form is predominant in the non-granular membranes, whereas cytosolic p59hck migrates as a doublet at 63 kDa. During the process of phagocytosis-linked degranulation, induced by serum-opsonized zymosan in neutrophils or HL60 cells, granular p59hck translocates towards the phagosome. The subcellular localization of p59hck suggests that the enzyme could be involved in the regulation of the degranulation process.

Regulation of T cell receptor signaling by a src family protein-tyrosine kinase (p59fyn)

Cell ◽  
1991 ◽  
Vol 65 (2) ◽  
pp. 281-291 ◽  
Author(s):  
Michael P. Cooke ◽  
Kristin M. Abraham ◽  
Katherine A. Forbush ◽  
Roger M. Perimutter
Keyword(s):  
T Cell ◽  
Tyrosine Kinase ◽  
T Cell Receptor ◽  
Protein Tyrosine Kinase ◽  
Cell Receptor ◽  
Receptor Signaling ◽  
Protein Tyrosine ◽  
Family Protein ◽  
T Cell Receptor Signaling ◽  
Cell Receptor Signaling

Appearance and disappearance of Syk family protein-tyrosine kinase genes during metazoan evolution

Gene ◽  
1999 ◽  
Vol 239 (1) ◽  
pp. 91-97 ◽  
Author(s):  
Robert E. Steele ◽  
Nicholas A. Stover ◽  
Masahiko Sakaguchi
Keyword(s):  
Tyrosine Kinase ◽  
Protein Tyrosine Kinase ◽  
Protein Tyrosine ◽  
Metazoan Evolution ◽  
Family Protein

scholarly journals Beta 2 integrin-dependent protein tyrosine phosphorylation and activation of the FGR protein tyrosine kinase in human neutrophils.

1994 ◽  
Vol 126 (4) ◽  
pp. 1111-1121 ◽  
Author(s):  
G Berton ◽  
L Fumagalli ◽  
C Laudanna ◽  
C Sorio
Keyword(s):  
Tyrosine Kinase ◽  
Tyrosine Phosphorylation ◽  
Protein Tyrosine Kinase ◽  
Kinase Activity ◽  
Class I ◽  
Human Neutrophils ◽  
Protein Tyrosine Phosphorylation ◽  
Protein Tyrosine ◽  
Mhc Antigens ◽  
Beta 2

Stimulation of adherent human neutrophils (PMN) with tumor necrosis factor (TNF) triggers protein tyrosine phosphorylation (Fuortes, M., W. W. Jin, and C. Nathan. 1993. J. Cell Biol. 120:777-784). We investigated the dependence of this response on beta 2 integrins by using PMN isolated from a leukocyte adhesion deficiency (LAD) patient, which do not express beta 2 integrins, and by plating PMN on surface bound anti-beta 2 (CD18) antibodies. Protein tyrosine phosphorylation increased in PMN plated on fibrinogen and this phosphorylation was enhanced by TNF. Triggering of protein tyrosine phosphorylation did not occur in LAD PMN plated on fibrinogen either in the absence or the presence of TNF. Surface bound anti-CD18, but not isotype-matched anti-Class I major histocompatibility complex (MHC) antigens, antibodies triggered tyrosine phosphorylation in normal, but not in LAD PMN. As the major tyrosine phosphorylated proteins we found in our assay conditions migrated with an apparent molecular mass of 56-60 kD, we investigated whether beta 2 integrins are implicated in activation of members of the src family of intracellular protein-tyrosine kinases. We found that the fgr protein-tyrosine kinase (p58fgr) activity, and its extent of phosphorylation in tyrosine, in PMN adherent to fibrinogen, was enhanced by TNF. Activation of p58fgr in response to TNF was evident within 10 min of treatment and increased with times up to 30 min. Also other activators of beta 2 integrins such as phorbol-12-myristate 13-acetate (PMA), and formyl methionyl-leucyl-phenylalanine (FMLP), induced activation of p58fgr kinase activity. Activation of p58fgr kinase activity, and phosphorylation in tyrosine, did not occur in PMN of a LAD patient in response to TNF. Soluble anti-CD18, but not anti-Class I MHC antigens, antibodies inhibited activation of p58fgr kinase activity in PMN adherent to fibrinogen in response to TNF, PMA, and FMLP. These findings demonstrate that, in PMN, beta 2 integrins are implicated in triggering of protein tyrosine phosphorylation, and establish a link between beta 2 integrin-dependent adhesion and the protein tyrosine kinase fgr in cell signaling.

scholarly journals CD19 Regulates Src Family Protein Tyrosine Kinase Activation in B Lymphocytes through Processive Amplification

Immunity ◽  
2000 ◽  
Vol 13 (1) ◽  
pp. 47-57 ◽  
Author(s):  
Manabu Fujimoto ◽  
Yoko Fujimoto ◽  
Jonathan C Poe ◽  
Paul J Jansen ◽  
Clifford A Lowell ◽  
...  
Keyword(s):  
Tyrosine Kinase ◽  
B Lymphocytes ◽  
Protein Tyrosine Kinase ◽  
Kinase Activation ◽  
Protein Tyrosine ◽  
Family Protein

scholarly journals Lipoarabinomannans Activate the Protein Tyrosine Kinase Hck in Human Neutrophils

2000 ◽  
Vol 68 (8) ◽  
pp. 4827-4830 ◽  
Author(s):  
Catherine Astarie-Dequeker ◽  
Jérôme Nigou ◽  
Germain Puzo ◽  
Isabelle Maridonneau-Parini
Keyword(s):  
Tyrosine Kinases ◽  
Protein Tyrosine Kinase ◽  
Biological Activities ◽  
Membrane Receptors ◽  
Human Neutrophils ◽  
Target Cells ◽  
Protein Tyrosine ◽  
Family Protein ◽  
Vaccinal Strain ◽  
Plasma Membrane Receptors

ABSTRACT The mycobacterial lipoarabinomannans (LAMs) are glycosylphosphatidyl-myo-inositol-anchored lipoglycans with diverse biological activities. It has been shown that purified LAMs interact directly, or indirectly, through receptors with the plasma membrane receptors of target cells located in domains rich in glycosylphosphatidylinositol-anchored proteins that contain Src family protein tyrosine kinases. To examine whether LAMs could activate Src-related kinases, human neutrophils were exposed to mannosylated LAMs (ManLAMs) purified from the vaccinal strain Mycobacterium bovis BCG and to phosphoinositol-capped LAMs (AraLAM or PILAM) obtained from the nonpathogenic species Mycobacterium smegmatis. We report first that both ManLAMs and PILAMs activate Hck in a rapid and transient manner and second that complete deacylation of ManLAM abolished its effect on Hck activity, thereby demonstrating that acylation of LAM but not mannosylation is critical for Hck activation. These data indicate that Hck is involved in the signaling pathway of LAMs, molecules known for their ability to trigger several responses in eukaryotic cells.

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