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Lectin receptors on IgA isotypes.

Artikel i vetenskaplig tidskrift
Författare Agnes E Wold
C Motas
C Svanborg
J Mestecky
Publicerad i Scandinavian journal of immunology
Volym 39
Nummer/häfte 2
Sidor 195-201
ISSN 0300-9475
Publiceringsår 1994
Publicerad vid Institutionen för laboratoriemedicin, Avdelningen för klinisk immunologi
Sidor 195-201
Språk en
Länkar www.ncbi.nlm.nih.gov/entrez/query.f...
Ämnesord Carbohydrate Sequence, Galactose, metabolism, Humans, Immunoglobulin A, chemistry, metabolism, Immunoglobulin A, Secretory, chemistry, metabolism, Immunoglobulin Isotypes, chemistry, metabolism, Lectins, metabolism, Mannose, metabolism, Molecular Sequence Data, Myeloma Proteins, chemistry, Oligosaccharides, chemistry, Receptors, Mitogen, analysis, chemistry, metabolism, Secretory Component, chemistry, metabolism
Ämneskategorier Immunologi inom det medicinska området, Immunologi

Sammanfattning

It has been shown previously that secretory IgA interacts with the mannose-specific lectin of Escherichia coli. The purpose of the study described here was to evaluate whether the N-linked oligosaccharide chains of the human IgA isotypes IgA1 and IgA2 differ in lectin receptor activity. A range of plant lectins specific for N-linked oligosaccharide chains were tested for their ability to precipitate IgA1 and IgA2 myeloma proteins, secretory IgA and free secretory component. IgA2 myeloma proteins reacted more strongly than IgA1 with the mannose-specific lectin ConA, whereas IgA1 myeloma proteins reacted more strongly than IgA2 with two galactose-specific lectins, Ricinus communis agglutinin I and Abrus precatorius agglutinin. This suggests that IgA2 possesses a larger proportion of short truncated complex type oligosaccharide chains and/or oligomannose type chains than IgA1. Further, IgA2 reacted more strongly than IgA1 myeloma proteins with Lens culinaris (lentil) lectin, and Pisum sativum (pea) lectin, suggesting that IgA2 exposes more of short, complex type chains fucosylated on the core than IgA1. The differences demonstrated in receptor activity between IgA1 and IgA2 may be important in their interaction with the microbial flora, as well with endogenous lectins, such as phagocyte receptors.

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