D. Geiling, H.G. Geiling, K.J. Halbhuber, R. Fröber, G. Geyer
{"title":"Rat endo- and mesothelium lack Fc receptors","authors":"D. Geiling, H.G. Geiling, K.J. Halbhuber, R. Fröber, G. Geyer","doi":"10.1016/S0014-4908(79)80025-3","DOIUrl":null,"url":null,"abstract":"<div><p>The present study is concerned with the interaction of rat endo- and mesothelium with homologous erythrocytes under various conditions of pretreatment and incubation. Its findings show rat endo- and mesothelial cells</p><p></p><ul><li><span>a)</span><span><p>nonadhesive to native or pretreated erythrocytes irrespective of the presence of gamma-globulin in the medium,</p></span></li><li><span>b)</span><span><p>devoid of primary or cryptic receptors sensitive to the Fc segment of the IgG molecule, and</p></span></li><li><span>c)</span><span><p>provided with binding sites at the oxidized glycocalyx which together with receptor groups of modified erythrocytes share the same class of IgG.</p></span></li></ul></div>","PeriodicalId":75841,"journal":{"name":"Experimentelle Pathologie","volume":"17 3","pages":"Pages 171-175"},"PeriodicalIF":0.0000,"publicationDate":"1979-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0014-4908(79)80025-3","citationCount":"3","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Experimentelle Pathologie","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0014490879800253","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 3
Abstract
The present study is concerned with the interaction of rat endo- and mesothelium with homologous erythrocytes under various conditions of pretreatment and incubation. Its findings show rat endo- and mesothelial cells
a)
nonadhesive to native or pretreated erythrocytes irrespective of the presence of gamma-globulin in the medium,
b)
devoid of primary or cryptic receptors sensitive to the Fc segment of the IgG molecule, and
c)
provided with binding sites at the oxidized glycocalyx which together with receptor groups of modified erythrocytes share the same class of IgG.