Please use this identifier to cite or link to this item: https://ahro.austin.org.au/austinjspui/handle/1/13401
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dc.contributor.authorGavin, A Len
dc.contributor.authorWines, B Den
dc.contributor.authorPowell, Maree Sen
dc.contributor.authorHogarth, P Marken
dc.date.accessioned2015-05-16T03:14:42Z
dc.date.available2015-05-16T03:14:42Z
dc.date.issued1995-12-01en
dc.identifier.citationClinical and Experimental Immunology; 102(3): 620-5en
dc.identifier.govdoc8536382en
dc.identifier.otherPUBMEDen
dc.identifier.urihttp://ahro.austin.org.au/austinjspui/handle/1/13401en
dc.description.abstractControl of IgG immune complex formation and deposition is important in determining the nature and extent of subsequent immune effector responses, and appears to be aberrant in some autoimmune diseases. In this study we demonstrate that recombinant soluble Fc gamma RII (rsFc gamma RII) is an effective modulator of immune complex formation, delaying immune precipitation in a manner which is dose-dependent, and can be specifically inhibited by anti-Fc gamma RII MoAb Fab' fragments. This inhibitory role in immune precipitation also provides a possible mechanistic explanation for our previous demonstration of the efficacy of rsFc gamma RII as an inhibitor of immune complex-induced inflammation in the Arthus reaction in vivo. RsFc gamma RII inhibited immune complex precipitation in two different experimental systems. First, rsFc gamma RII inhibited the precipitation of 125I-bovine serum albumin (BSA)-anti-BSA complexes in a dose-dependent manner, while an irrelevant protein (soybean trypsin inhibitor) had no effect on the precipitation of the immune complexes. Moreover, rsFc gamma RII inhibited the precipitation of ovalbumin (OVA)-anti-OVA complexes as determined by turbidimetric analysis, where the inhibition of immune complex precipitation by rsFc gamma RII was dose-dependent and was specifically blocked by prior incubation with Fab' fragments of a blocking MoAb to Fc gamma RII. RsFc gamma RII could inhibit the precipitation of BSA-anti-BSA complexes in the presence of excess bystander IgG and did not inhibit complement-mediated prevention of immune precipitation, demonstrating that rsFc gamma RII did not block C1 binding to the BSA-anti-BSA complex. Unlike complement, rsFc gamma RII could not cause re-solubilization of pre-formed precipitated BSA-anti-BSA complexes. Soluble Fc gamma Rs have been detected in biological fluids of normal and inflammatory disease patients, yet the role of sFc gamma R is still unclear. However, they now play a potential role in the modulation of immune complex solubility.en
dc.language.isoenen
dc.subject.otherAnimalsen
dc.subject.otherAntigen-Antibody Complex.immunologyen
dc.subject.otherComplement System Proteins.physiologyen
dc.subject.otherHumansen
dc.subject.otherImmunoglobulin G.immunologyen
dc.subject.otherOvalbumin.immunologyen
dc.subject.otherPrecipitin Testsen
dc.subject.otherRabbitsen
dc.subject.otherReceptors, IgG.physiologyen
dc.subject.otherRecombinant Proteins.pharmacologyen
dc.titleRecombinant soluble Fc gamma RII inhibits immune complex precipitation.en
dc.typeJournal Articleen
dc.identifier.journaltitleClinical and experimental immunologyen
dc.identifier.affiliationHelen M. Schutt Laboratory for Immunology, Austin Research Institute, Austin Hospital, Heidelberg, Victoria, Australiaen
dc.description.pages620-5en
dc.relation.urlhttps://pubmed.ncbi.nlm.nih.gov/8536382en
dc.type.austinJournal Articleen
item.grantfulltextnone-
item.languageiso639-1en-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.openairetypeJournal Article-
item.fulltextNo Fulltext-
item.cerifentitytypePublications-
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