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Cited by 144Monoclonal and Polyclonal Antibodies ResearchProtein Kinase Regulation and GTPase SignalingReceptor Mechanisms and Signaling

The DOI matches its Crossref record; 35 of the 35 references it cites were found in a registry or an index.

Tyrosine phosphorylation of phospholipase C-gamma 1 induced by cross-linking of the high-affinity or low-affinity Fc receptor for IgG in U937 cells.

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Liao, F, Shin, H S, Rhee, S G·1992·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.89.8.3659PMC PMC48928
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Abstract

The human monocytic cell line U937 possesses two classes of the IgG Fc receptor (Fc gamma R), a high-affinity 72-kDa Fc gamma R (Fc gamma RI) and a low-affinity 40-kDa Fc gamma R (Fc gamma RII). Cross-linking of either class of Fc gamma R in U937 cells elicits an increase in the concentration of free intracellular Ca2+. A rapid rise in the concentration of inositol 1,4,5-trisphosphate (Ins-1,4,5-P3) and of several other inositol phosphates derived from Ins-1,4,5-P3 was observed after cross-linking of Fc gamma Rs in U937 cells. This result suggests that Ins-1,4,5-P3, generated by the action of phospholipase C (PLC), acts as a second messenger by which Fc gamma Rs mobilize intracellular Ca2+ in U937 cells. The mechanism by which the cross-linking of Fc gamma Rs triggers activation of PLC was studied. Cross-linking of Fc gamma RI or Fc gamma RII resulted in a rapid and transient phosphorylation of PLC-gamma 1 on tyrosine residues. It has previously been shown that phosphorylation of PLC-gamma 1 on tyrosine residues activates its enzymatic activity in cells. Prior incubation of U937 cells with a protein tyrosine kinase inhibitor, herbimycin A, prevented the tyrosine phosphorylation of PLC-gamma 1 and the hydrolysis of phosphatidylinositol 4,5-bisphosphate induced by the cross-linking of Fc gamma Rs. Thus, Fc gamma RI and Fc gamma RII appear to be functionally coupled to a nonreceptor tyrosine kinase that phosphorylates PLC-gamma 1 after receptor cross-linking, thereby causing activation of PLC-gamma 1.

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Metadata

Authors
Liao, F., Shin, H. S., & Rhee, S. G.
Affiliations
Johns Hopkins University (US)
ORCID
Venue
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences
Published
1992-04-15
Volume
89
Issue
8
Pages
3659-3663
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
DOI
10.1073/pnas.89.8.3659
PMC
PMC48928
OpenAlex
W2035439001
Cited by
144
References
35
Citations by year
2025: 2 · 2024: 1 · 2023: 2 · 2021: 2 · 2020: 1 · 2019: 1 · 2018: 2 · 2017: 2 · 2016: 6 · 2014: 3 · 2013: 5 · 2012: 5
FWCI
19.75
Type
journal article
Language
en
Open access
Locations
  • Proceedings of the National Academy of Sciences (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Immunology and Microbiology › Immunology › Monoclonal and Polyclonal Antibodies Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
Keywords
phospholipase C-gamma1, tyrosine phosphorylation, Fc gamma receptor I, Fc gamma receptor II, U937 cells, calcium mobilization, inositol 1,4,5-trisphosphate, inositol phosphates, non-receptor tyrosine kinase, herbimycin A, phosphatidylinositol 4,5-bisphosphate hydrolysis, second messenger signaling, monocytic cells
MeSH terms
Antigens, Differentiation, Arsenicals, Calcium, Cell Line, Cross-Linking Reagents, Humans, Immunoglobulin G, Inositol Phosphates, Kinetics, Phosphates, Phosphatidylinositols, Type C Phospholipases, Phosphorylation, Receptors, Fc, Tyrosine, Inositol 1,4,5-Trisphosphate, Receptors, IgG, Phosphotyrosine, Phosphatidylinositol 4,5-Diphosphate

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