The FcγRII receptor triggers pp125(FAK) phosphorylation in platelets

Beatrice Haimovich, Cathy Regan, Lou DiFazio, Ernest Ginalis, Ping Ji, Uma Purohit, R. Bruce Rowley, Joseph Bolen, Ralph Greco

Research output: Contribution to journalArticle

37 Citations (Scopus)

Abstract

Platelets express a single low affinity receptor for immunoglobulin, FcγRII, that triggers multiple cellular responses upon interaction with multivalent immune complexes. In this study we show that immobilized IgG is also a potent stimulant of platelet activation triggering adhesion, aggregation, massive dense granule secretion, and thromboxane production. Platelet adhesion to IgG was blocked by the FcγRII receptor-specific monoclonal antibody, IV.3. Pretreatment of the platelets with cytochalasin D to inhibit actin polymerization similarly prevented cell binding to IgG having no effect on platelet binding to fibrinogen. Platelet adhesion to IgG also led to the induction of tyrosine phosphorylation of multiple proteins including pp125(FAK) and p72(SYK). These proteins were also tyrosine- phosphorylated in α(IIb)β 3-deficient IgG-adherent platelets from patients with Glanzmann's thrombasthenia. These data demonstrate that FcγRII mediates pp125(FAK) phosphorylation and platelet adhesion to IgG independent of the integrin α(IIb)β 3. Treatment of the platelets with bisindolylmaleimide to inhibit protein kinase C prevented phosphorylation of pp125(FAK) as well as several other proteins, but not p72(SYK) phosphorylation. This study establishes that the FcγRII receptor mediates ppt25(FAK) phosphorylation via protein kinase C.

Original languageEnglish (US)
Pages (from-to)16332-16337
Number of pages6
JournalJournal of Biological Chemistry
Volume271
Issue number27
DOIs
StatePublished - Jul 29 1996

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Phosphorylation
Platelets
Blood Platelets
Immunoglobulin G
Adhesion
Protein Kinase C
Tyrosine
Thrombasthenia
Cytochalasin D
Proteins
Thromboxanes
Platelet Activation
Antigen-Antibody Complex
Integrins
Polymerization
Fibrinogen
Immunoglobulins
Actins
Monoclonal Antibodies
Agglomeration

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Biochemistry
  • Cell Biology

Cite this

Haimovich, B., Regan, C., DiFazio, L., Ginalis, E., Ji, P., Purohit, U., ... Greco, R. (1996). The FcγRII receptor triggers pp125(FAK) phosphorylation in platelets. Journal of Biological Chemistry, 271(27), 16332-16337. https://doi.org/10.1074/jbc.271.27.16332
Haimovich, Beatrice ; Regan, Cathy ; DiFazio, Lou ; Ginalis, Ernest ; Ji, Ping ; Purohit, Uma ; Bruce Rowley, R. ; Bolen, Joseph ; Greco, Ralph. / The FcγRII receptor triggers pp125(FAK) phosphorylation in platelets. In: Journal of Biological Chemistry. 1996 ; Vol. 271, No. 27. pp. 16332-16337.
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Haimovich, B, Regan, C, DiFazio, L, Ginalis, E, Ji, P, Purohit, U, Bruce Rowley, R, Bolen, J & Greco, R 1996, 'The FcγRII receptor triggers pp125(FAK) phosphorylation in platelets', Journal of Biological Chemistry, vol. 271, no. 27, pp. 16332-16337. https://doi.org/10.1074/jbc.271.27.16332

The FcγRII receptor triggers pp125(FAK) phosphorylation in platelets. / Haimovich, Beatrice; Regan, Cathy; DiFazio, Lou; Ginalis, Ernest; Ji, Ping; Purohit, Uma; Bruce Rowley, R.; Bolen, Joseph; Greco, Ralph.

In: Journal of Biological Chemistry, Vol. 271, No. 27, 29.07.1996, p. 16332-16337.

Research output: Contribution to journalArticle

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T1 - The FcγRII receptor triggers pp125(FAK) phosphorylation in platelets

AU - Haimovich, Beatrice

AU - Regan, Cathy

AU - DiFazio, Lou

AU - Ginalis, Ernest

AU - Ji, Ping

AU - Purohit, Uma

AU - Bruce Rowley, R.

AU - Bolen, Joseph

AU - Greco, Ralph

PY - 1996/7/29

Y1 - 1996/7/29

N2 - Platelets express a single low affinity receptor for immunoglobulin, FcγRII, that triggers multiple cellular responses upon interaction with multivalent immune complexes. In this study we show that immobilized IgG is also a potent stimulant of platelet activation triggering adhesion, aggregation, massive dense granule secretion, and thromboxane production. Platelet adhesion to IgG was blocked by the FcγRII receptor-specific monoclonal antibody, IV.3. Pretreatment of the platelets with cytochalasin D to inhibit actin polymerization similarly prevented cell binding to IgG having no effect on platelet binding to fibrinogen. Platelet adhesion to IgG also led to the induction of tyrosine phosphorylation of multiple proteins including pp125(FAK) and p72(SYK). These proteins were also tyrosine- phosphorylated in α(IIb)β 3-deficient IgG-adherent platelets from patients with Glanzmann's thrombasthenia. These data demonstrate that FcγRII mediates pp125(FAK) phosphorylation and platelet adhesion to IgG independent of the integrin α(IIb)β 3. Treatment of the platelets with bisindolylmaleimide to inhibit protein kinase C prevented phosphorylation of pp125(FAK) as well as several other proteins, but not p72(SYK) phosphorylation. This study establishes that the FcγRII receptor mediates ppt25(FAK) phosphorylation via protein kinase C.

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