Structural and functional aspects of IgA Transcytosis
- 1 January 1989
- journal article
- research article
- Published by Taylor & Francis in Immunological Investigations
- Vol. 18 (1-4) , 287-297
- https://doi.org/10.3109/08820138909112243
Abstract
One of the cornerstones of mucosal immunology has been the study of the selective secretion of polymeric IgA at the mucosal epithelium. We have focussed on the structural features which govern the association of polymeric immunoglobulin and its receptor. We have also described some of the features which distinguish the transcytotic pathway in the rat liver from the well known degradative pathway taken typically by asialoglycoproteins (1).Keywords
This publication has 47 references indexed in Scilit:
- Deletion of the cytoplasmic domain of the polymeric immunoglobulin receptor prevents basolateral localization and endocytosisCell, 1986
- Computer models of the human immunoglobulins: Binding sites and molecular interactionsImmunology Today, 1986
- Diacytosis of human asialotransferrin type 3 in the rat liver is due to the sequential engagement of two receptorsExperimental Cell Research, 1985
- Low level transport of IgA to bile via the asialoglycoprotein receptorFEBS Letters, 1985
- The Mechanism of Biliary Excretion of α1–Acid Glycoprotein in the Rat: Evidence for A Molecular Weight–Dependent, Nonreceptor–Mediated PathwayHepatology, 1982
- Comparison of human, bovine and rabbit secretory component-immunoglobulin interactionsImmunochemistry, 1978
- Human secretory component—VI: Immunoglobulin-binding propertiesImmunochemistry, 1977
- Isolation of human secretory component by affinity chromatography on IgM-SepharoseImmunochemistry, 1977
- Does J chain mediate the combination of 19S IgM and dimeric IgA with the secretory component rather than being necessary for their polymerization?Immunochemistry, 1974
- Studies on human secretory immunoglobulin A—III. J chainImmunochemistry, 1972