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.
Open accessAbstract
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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“In addition to its role as a direct docking site for skeletal proteins, 4,5-PIP2 is also the primary substrate of phospholipase Cγ (PLCγ), which was shown to become activated upon engagement of FcγRs (Azzoni et al. 1992; Liao et al. 1992).”
From Localized Biphasic Changes in Phosphatidylinositol-4,5-Bisphosphate at Sites of Phagocytosis (2000) · cites this paper as Liao et al. 1992
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Inositol phosphates and cell signalling
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Self-citationRegulation of Polyphosphoinositide-specific Phospholipase C Activity by Purified G q
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Activation of the β1 isozyme of phospholipase C by α subunits of the Gq class of G proteins
Taylor, S. J., Chae, H. Z., Rhee, S. G., & Exton, J. H. (1991) · Nature · doi:10.1038/350516a0 · Cited by 780
Self-citationIncrease of the Catalytic Activity of Phospholipase C-γ1 by Tyrosine Phosphorylation
Nishibe, S., Wahl, M. I., Hernández‐Sotomayor, S. M. T., Tonks, N. K., Rhee, S. G., & Carpenter, G. F. (1990) · Science · doi:10.1126/science.1700866 · Cited by 635
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Self-citationHuman neutrophil Fc gamma receptor distribution and structure.
Fleit, H. B., Wright, S. D., & Unkeless, J. C. (1982) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.79.10.3275 · Cited by 568
Inhibition of tyrosine phosphorylation prevents T-cell receptor-mediated signal transduction.
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Fcγ receptors as regulators of immune responses
Nimmerjahn, F., & Ravetch, J. V. (2008) · Nature Reviews Immunology · doi:10.1038/nri2206 · Cited by 2,947
The Cell Biology of Phagocytosis
Flannagan, R. S., Jaumouillé, V., & Grinstein, S. (2011) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathol-011811-132445 · Cited by 1,100
Regulation of inositol phospholipid-specific phospholipase C isozymes.
Rhee, S. G., & Choi, K. D. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42284-3 · Cited by 741
Self-citationPhagocytosis and the actin cytoskeleton
May, R. C., & Machesky, L. M. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.6.1061 · Cited by 715
Phagocytosis: A Fundamental Process in Immunity
Rosales, C., & Uribe‐Querol, E. (2017) · BioMed Research International · doi:10.1155/2017/9042851 · Cited by 618
Metadata
- Authors
- Liao, F., Shin, H. S., & Rhee, S. G.
- Affiliations
- Johns Hopkins University (US)
- 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
- 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
- green
- europepmc.org
- 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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