Linked Life Data

15136586

Source:http://linkedlifedata.com/resource/pubmed/id/15136586

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2004-7-27
pubmed:abstractText
There are important differences in signaling between the Fc receptor for immunoglobulin G (IgG) FcgammaRIIA, which uses the Ig tyrosine-activating motif (ITAM) within its own cytoplasmic domain, and FcgammaRI, which transmits signals by means of an ITAM located within the cytoplasmic domain of its associated gamma-chain. For example, in transfected epithelial cells and COS-1 cells, FcgammaRIIA mediates phagocytosis of IgG-coated red blood cells more efficiently than does FcgammaRI/gamma, and enhancement of phagocytosis by Syk kinase is more pronounced for FcgammaRI/gamma than for FcgammaRIIA. In addition, structure/function studies indicate that the gamma-chain ITAM and the FcgammaRIIA ITAM have different requirements for mediating the phagocytic signal. To study the differences between FcgammaRIIA and FcgammaRI/gamma, we examined the interaction of FcgammaRIIA and the FcgammaRI/gamma chimera FcgammaRI-gamma-gamma (extracellular domain-transmembrane domain-cytoplasmic domain) with Syk kinase and with the Src-related tyrosine kinases (SRTKs) Hck and Lyn in transfected COS-1 cells. Our data indicate that FcgammaRIIA interacts more readily with Syk than does FcgammaRI-gamma-gamma and suggest that one consequence may be the greater phagocytic efficiency of FcgammaRIIA compared with FcgammaRI/gamma. Furthermore, individual SRTKs affect the efficiency of phagocytosis differently for FcgammaRI-gamma-gamma and FcgammaRIIA and also influence the ability of these receptors to interact with Syk kinase. Taken together, the data suggest that differences in signaling by FcgammaRIIA and FcgammaRI-gamma-gamma are related in part to interaction with Syk and Src kinases and that individual SRTKs play different roles in FcgammaR-mediated phagocytosis.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/3,3',4,5'-tetrahydroxystilbene, http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD, http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Precursors, http://linkedlifedata.com/resource/pubmed/chemical/FCGR1A protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Fc gamma receptor IIA, http://linkedlifedata.com/resource/pubmed/chemical/Fcgr1 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides..., http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, IgG, http://linkedlifedata.com/resource/pubmed/chemical/Stilbenes, http://linkedlifedata.com/resource/pubmed/chemical/Syk kinase, http://linkedlifedata.com/resource/pubmed/chemical/src-Family Kinases
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0741-5400
pubmed:author
pubmed:issnType
Print
pubmed:volume
76
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
491-9
pubmed:dateRevised
2011-11-2
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
The monocyte Fcgamma receptors FcgammaRI/gamma and FcgammaRIIA differ in their interaction with Syk and with Src-related tyrosine kinases.
pubmed:affiliation
University of Pennsylvania, School of Medicine, Hematology and Oncology Division, Biomedical Research Building II/III, Room 705, 421 Curie Blvd., Philadelphia, PA 19104, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.