Involvement of p72syk, a protein-tyrosine kinase, in Fc gamma receptor signaling

Agarwal, Alka; Salem, Patrick; Robbins, K C

doi:10.1016/s0021-9258(18)82337-7

Cited by 123 publications

(14 citation statements)

References 37 publications

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“…Amino acid sequence data indicate that Fc-yRI and FcyRII do not contain domains with PTK activity (3,39). Therefore, these receptors on monocytes must be coupled with a nonreceptor PTK, as reported for PTK p72sYk in signaling through FcyR in HL60 cells (1).…”

Section: Discussionmentioning

confidence: 86%

“…This conclusion is based on two lines of evidence. First, two selective PTK inhibitors, which act through entirely different mechanisms (2,26), inhibited the Fc-yR-mediated intracellular killing of S. aureus by monocytes and the increase in the intracellular Ins (1,4,5)P3 concentration in these cells.…”

Section: Discussionmentioning

confidence: 99%

“…Ins (1,4,5)P3 concentrations in monocytes which had been incubated with anti-Fc-yRI MAb 197 or anti-Fc-yRII MAb IV-3 for 3 min were determined 20 s after the addition of F(ab')2-GAM IgG. The changes in the [Ca2+]i in FURA-2/AM-loaded monocytes were monitored as previously described ( 45), expressed as maximum [Ca2+]i and the lag time of the increase in the [Ca2+]j.…”

Section: Effects Of Ptk Inhibitors On Changes In the Intracellularmentioning

confidence: 99%

“…One of the main intracellular signaling pathways involved in the stimulation of phagocytes via FcyR cross-linking is hydrolysis of phosphoinositol (4,5)-bisphosphate by phospholipase C (PLC), resulting in the formation of two second messengers: inositol (1,4,5)-trisphosphate [Ins (1,4,5)P3] and diacylglycerol (6,43). Ins(1,4,5)P3 causes an increase in the cytosolic free calcium concentration ([Ca2+]i) whereas diacylglycerol is an endogenous activator of protein kinase C (6, 7).…”

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confidence: 99%

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Protein tyrosine kinase activity is essential for Fc gamma receptor-mediated intracellular killing of Staphylococcus aureus by human monocytes

et al. 1994

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Our previous study revealed that the intracellular killing of Staphylococcus aureus by human monocytes after cross-linking Fc gamma receptor I (Fc gamma RI) or Fc gamma RII is a phospholipase C (PLC)-dependent process. The aim of the present study was to investigate whether protein tyrosine kinase (PTK) activity plays a role in the Fc gamma R-mediated intracellular killing of bacteria and activation of PLC in these cells. The results showed that phagocytosis of bacteria by monocytes was not affected by the PTK inhibitors genistein and tyrphostin-47. The intracellular killing of S. aureus by monocytes after cross-linking Fc gamma RII or Fc gamma RII with anti-Fc gamma R monoclonal antibody and a bridging antibody or with human immunoglobulin G (IgG) was inhibited by these compounds in a dose-dependent fashion. The production of O2- by monocytes after stimulation with IgG or IgG-opsonized S. aureus was almost completely blocked by the PTK inhibitor. These results indicate that inhibition of PTK impairs the oxygen-dependent bactericidal mechanisms of monocytes. Genistein and tyrphostin-47, which do not affect the enzymatic activity of purified PLC, prevented activation of PLC after cross-linking Fc gamma RI or Fc gamma RII, measured as an increase in the intracellular inositol 1,4,5-trisphosphate concentration. Cross-linking Fc gamma RI or Fc gamma RII induced rapid tyrosine phosphorylation of several proteins in monocytes, one of which was identified as PLC-gamma 1, and the phosphorylation could be completely blocked by PTK inhibitors, leading to the conclusion that activation of PLC after cross-linking Fc gamma R in monocytes is regulated by PTK activity. Together, these results demonstrate that PTK activity is essential for the activation of PLC which is involved in the Fc gamma R-mediated intracellular killing of S. aureus by human monocytes.

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Section: Discussionmentioning

confidence: 86%

Section: Discussionmentioning

confidence: 99%

Section: Effects Of Ptk Inhibitors On Changes In the Intracellularmentioning

confidence: 99%

mentioning

confidence: 99%

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Protein tyrosine kinase activity is essential for Fc gamma receptor-mediated intracellular killing of Staphylococcus aureus by human monocytes

et al. 1994

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“…Syk couples with the IgE and IgM receptors in mast cells and B cells, respectively, is activated after engaging with the respective receptor, and thereby plays a critical role in mediating cellular responses [1,[6][7][8][9][10][11][12][13]. Syk is also activated following engagement of Fcy receptors in myelomonocytic cells [14].…”

Section: Introductionmentioning

confidence: 99%

Solution structure of the C-terminal SH2 domain of the human tyrosine kinase Syk complexed with a phosphotyrosine pentapeptide

Narula¹,

Yuan²,

Adams³

et al. 1995

Structure

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Syk-C resembles other SH2 domains in its peptide-binding interactions and overall topology, a result that is consistent with its ability to function as an independent SH2 domain in vitro. This result suggests that Syk-C plays a unique role in the intact Syk protein. The determinants of the binding affinity and selectivity of Syk-C may reside in the least-conserved structural elements that comprise the phosphotyrosine- and leucine-binding sites. These structural features can be exploited for the design of Syk-selective SH2 antagonists for the treatment of allergic disorders and asthma.

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Tyrosine phosphorylation/dephosphorylation controls capping of Fc? receptor II in U937 cells

Kwiatkowska

Sobota

1999

Cell Motil. Cytoskeleton

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Involvement of p72syk, a protein-tyrosine kinase, in Fc gamma receptor signaling

Cited by 123 publications

References 37 publications

Protein tyrosine kinase activity is essential for Fc gamma receptor-mediated intracellular killing of Staphylococcus aureus by human monocytes

Protein tyrosine kinase activity is essential for Fc gamma receptor-mediated intracellular killing of Staphylococcus aureus by human monocytes

Solution structure of the C-terminal SH2 domain of the human tyrosine kinase Syk complexed with a phosphotyrosine pentapeptide

Tyrosine phosphorylation/dephosphorylation controls capping of Fc? receptor II in U937 cells

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