Reactivities of N-acetylgalactosamine-specific lectins with human IgA1 proteins.

Reactivities of N-acetylgalactosamine-specific lectins with human IgA1 proteins. Research Abstract Details 

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Reactivities of N-acetylgalactosamine-specific lectins with human IgA1 proteins. Abstract Text:

Jennifer S Moore,Rose Kulhavy,Milan Tomana,Zina Moldoveanu,Hitoshi Suzuki,Rhubell Brown,Stacy Hall,Mogens Kilian,Knud Poulsen,Jiri Mestecky,Bruce A Julian,Jan Novak,

Lectins are proteins with specificity of binding to certain monosaccharides or oligosaccharides. They can detect abnormal glycosylation patterns on immunoglobulins in patients with various chronic inflammatory diseases, including rheumatoid arthritis and IgA nephropathy (IgAN). However, lectins exhibit binding heterogeneity, depending on their source and methods of isolation. To characterize potential differences in recognition of terminal N-acetylgalactosamine (GalNAc) on IgA1, we evaluated the binding characteristics of several commercial preparations of GalNAc-specific lectins using a panel of IgA1 and, as controls, IgA2 and IgG myeloma proteins. These lectins originated from snails Helix aspersa (HAA) and Helix pomatia (HPA), and the plant Vicia villosa (VV). Only HAA and HPA bound exclusively to IgA1, with its O-linked glycans composed of GalNAc, galactose, and sialic acid. In contrast, VV reacted with sugars of both IgA subclasses and IgG, indicating that it also recognized N-linked glycans without GalNAc. Furthermore, HAA and HPA from several manufacturers differed in their ability to bind various IgA1 myeloma proteins and other GalNAc-containing glycoproteins in ELISA and Western blot. For serum samples from IgAN patients, HAA was the optimal lectin to study IgA1 glycosylation in ELISA and Western blot assays, including identification of the sites of attachment of the aberrant glycans. The galactose-deficient glycans were site-specific, localized mostly at Thr228 and/or Ser230. Because of the heterogeneity of GalNAc-specific lectins, they should be carefully characterized with appropriate substrates before undertaking any study.

Reactivities of N-acetylgalactosamine-specific lectins with human IgA1 proteins. Publishing Authors By Initials

JS Moore,R Kulhavy,M Tomana,Z Moldoveanu,H Suzuki,R Brown,S Hall,M Kilian,K Poulsen,J Mestecky,BA Julian,J Novak,

For similar proteins: lectins: plant lectins research abstracts see: proteins: lectins: plant lectins research

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Reactivities of N-acetylgalactosamine-specific lectins with human IgA1 proteins. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: Molecular immunology

VOLUME: 44

Page Numbers: 2598-604

Journal Abbreviation: Mol. Immunol.

ISSN: 0161-5890

DAY: 2

MONTH: 02

YEAR: 2007

Reactivities of N-acetylgalactosamine-specific lectins with human IgA1 proteins. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 7905289

Reactivities of N-acetylgalactosamine-specific lectins with human IgA1 proteins. Keywords Mesh Terms:

KEYWORDS: Plant Lectins

MESH TERMS: metabolism

Chemical & Substance for Abstract: Reactivities of N-acetylgalactosamine-specific lectins with human IgA1 proteins. Information

Substance Name: Acetylgalactosamine

Registry Number: 31022-50-1

Grant and Affiliation Information for Reactivities of N-acetylgalactosamine-specific lectins with human IgA1 proteins.

AFFILIATION: Department of Microbiology, University of Alabama at Birmingham, Birmingham, AL, USA.

Country: England

AGENCY: United States NCRR

GRANT: M01 RR 00032

ACRONYM: RR

MEDLINETA: Mol Immunol

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