1: Glycoconj J. 2006 Nov;23(7/8):463/71.
Galactosylation of IgG from rheumatoid arthritis (RA) patients//changes during
therapy.
Pasek M, Duk M, Podbielska M, Sokolik R, Szechiński J, Lisowska E, Krotkiewski H.
Ludwik Hirszfeld Institute of Immunology & Experimental Therapy, Polish Academy
of Sciences, R. Weigla 12, 53/114, Wroclaw, Poland.
It is well documented that serum IgG from rheumatoid arthritis (RA) patients
exhibits decreased galactosylation of its conservative N/glycans (Asn/297) in CH2
domains of the heavy chains; it has been shown that this agalactosylation is
proportional to disease severity. In the present investigation we analyzed
galactosylation of IgG derived from the patients using a modified ELISA/plate
test, biosensor BIAcore and total sugar analysis (GC/MS). For ELISA and BIAcore
the binding of IgG preparations, purified from the patients' sera, to two
lectins: Ricinus communis (RCA/I) and Griffonia simplicifolia (GSL/II) was
applied. Based on ELISA/plate test an agalactosylation factor (AF, a relative
ratio of GSL/II/RCA/I binding) was calculated, which was proportional to actual
disease severity. Repeated testing of several patients before and after treatment
with methotrexate (MTX) alone or in combination with Remicade (a chimeric
antibody anti/TNF/alpha) supplied results indicating an increase of IgG
galactosylation during the treatment. This introductory observation suggests that
IgG galactosylation may be an additional indicator of the RA patients'
improvement.
PMID: 17006638 [PubMed / indexed for MEDLINE]
Related Links
Effect of infliximab on the glycosylation of IgG of patients with rheumatoid
arthritis. [J Clin Lab Anal. 2007] PMID:17847113
Influence of methotrexate, TNF blockers and prednisolone on antibody responses to
pneumococcal polysaccharide vaccine in patients with rheumatoid arthritis.
[Rheumatology (Oxford). 2006] PMID:16287919
Analysis of agalacto/IgG in rheumatoid arthritis using surface plasmon resonance.
[Glycoconj J. 2000] PMID:11261841
IgG and IgM anticardiolipin antibodies following treatment with infliximab plus
methotrexate in patients with early rheumatoid arthritis. [Arthritis Rheum. 2006]
PMID:16948115
Aberrant lectin/binding activity of immunoglobulin G in serum from rheumatoid
arthritis patients. [Clin Chem. 1989] PMID:2758632
2: J Rheumatol. 2001 Jul;28(7):1531/6.
Characterization of changes in IgG associated oligosaccharide profiles in
rheumatoid arthritis, psoriatic arthritis, and ankylosing spondylitis using
fluorophore linked carbohydrate electrophoresis.
Martin K, Talukder R, Hay FC, Axford JS.
Department of Biochemistry and Immunology, St. George's Hospital Medical School,
London, United Kingdom.
OBJECTIVE: To investigate fluorophore linked carbohydrate electrophoresis (FCE)
as a method of analyzing serum immunoglobulin G (IgG) oligosaccharides in healthy
individuals and those with rheumatic disease and compare with lectin binding
assays of carbohydrate composition. METHODS: IgG was isolated from patients with
rheumatoid arthritis (RA) (n = 21), ankylosing spondylitis (AS) (n = 20),
psoriatic arthritis (PsA) (n = 20), and healthy adults (n = 36). IgG
oligosaccharides were released enzymatically, fluorescently labelled using 8
aminonaphthalene/136 trisulfonic acid; and identification of the oligosaccharide
bands was by stepwise enzymatic degradation. Comparison of FCE was made with
lectin binding analysis in which the lectins Ricinus communis (RCA1) and
Bandeiraea simplicifolia (BSII) were used to detect galactose (Gal) and
N/acetylglucosamine (GlcNAc), respectively. RESULTS: Each disease could be
differentiated from healthy adults on the basis of Band 1 asialodigalacto core
fucosylated oligosaccharide (gf2) intensity (p = 0.001), but not from each other.
Reduced levels of different sugars were associated with specific diseases:
reduced gf2 with RA (p < 0.001), PsA (p < 0.001) and AS (p < 0.02), reduced Band
5 disialo/digalacto core fucosylated (a2f) oligosaccharide with AS (p < 0.001),
reduced Band 6 disialo/digalacto (a2) oligosaccharide with AS (p < 0.001) and PsA
(p = 0.021). All diseases were associated with a significant increase in Band 4
asialo/agalacto core fucosylated oligosaccharide (g0f) (p < 0.001). In RA, FCE
band intensities correlated with sugar quantity when identified using lectin
binding analysis (p < 0.003). In contrast, there was no correlation between the
same bands in healthy individuals. CONCLUSION: FCE is an accurate method of
analyzing IgG associated oligosaccharides and reveals unique band patterns or
sugar prints associated with healthy adults and patients with RA, PsA, and AS,
and comparison with lectin binding analysis suggests undetected RA glycoprotein
structural differences. FCE has potential in the early diagnosis and
differentiation of rheumatic diseases.
PMID: 11469458 [PubMed / indexed for MEDLINE]
Related Links
Sugar printing rheumatic diseases: a potential method for disease differentiation
using immunoglobulin G oligosaccharides. [Arthritis Rheum. 1999] PMID:10446868
Rheumatic disease differentiation using immunoglobulin G sugar printing by high
density electrophoresis. [J Rheumatol. 2003] PMID:14719191
Immunoglobulin G glycosylation and clinical outcome in rheumatoid arthritis
during pregnancy. [J Rheumatol. 2000] PMID:10852257
Antibodies to tissue transglutaminase and Saccharomyces cerevisiae in ankylosing
spondylitis and psoriatic arthritis. [J Rheumatol. 2004] PMID:15124251
Aberrant lectin/binding activity of immunoglobulin G in serum from rheumatoid
arthritis patients. [Clin Chem. 1989] PMID:2758632
3: Glycoconj J. 1998 Sep;15(9):929/34.
Detection of disease/specific augmentation of abnormal immunoglobulin G in sera
of patients with rheumatoid arthritis.
Tang W, Matsumoto A, Shikata K, Takeuchi F, Konishi T, Nakata M, Mizuochi T.
Department of Applied Chemistry, Tokai University, Hiratsuka, Kanagawa, Japan.
Galactose/free immunoglobulin G (IgG), which is known to be higher in the sera of
patients with rheumatoid arthritis, was prepared from IgG of healthy volunteers
using enzymes. Its reactivity to lectins was analyzed. The galactose/free IgG
showed no reactivity to Ricinus communis agglutinin 120 but displayed greater
reactivity to concanavalin A and Lens culinaris lectin than did intact human IgG.
Then, IgG in serum samples was bound to protein A immobilized on a nitrocellulose
membrane, and its reactivity to biotinylated concanavalin A was measured with
streptavidin/conjugated horseradish peroxidase. When the reactivity to
concanavalin A of IgG in sera from healthy individuals and patients with
rheumatoid arthritis (RA), osteoarthritis, systemic lupus erythematosus, or
hepatic disease was compared, higher levels were shown in patients with RA,
notably in 60% of the seronegative patients and 80% of the early phase patients.
Therefore, it was suggested that augmentation of the abnormal IgG in sera was
highly specific to patients with RA and that this novel serum test could be very
useful for an accurate diagnosis of this disease.
PMID: 10052597 [PubMed / indexed for MEDLINE]
Related Links
Aberrant lectin/binding activity of immunoglobulin G in serum from rheumatoid
arthritis patients. [Clin Chem. 1989] PMID:2758632
Characterization of changes in IgG associated oligosaccharide profiles in
rheumatoid arthritis, psoriatic arthritis, and ankylosing spondylitis using
fluorophore linked carbohydrate electrophoresis. [J Rheumatol. 2001]
PMID:11469458
Increased concanavalin A/binding capacity of immunoglobulin G purified from sera
of patients with rheumatoid arthritis. [Clin Exp Immunol. 1987] PMID:3652523
Autoantibody activity of IgG rheumatoid factor increases with decreasing levels
of galactosylation and sialylation. [J Biochem. 2000] PMID:11011144
Alterations in the carbohydrate structures of an abnormal protein from sera of
patients with rheumatoid arthritis. [Arch Biochem Biophys. 1993] PMID:8239648
4: Glycobiology. 1998 Dec;8(12):1215/20.
The effect on IgG glycosylation of altering beta1, 4/galactosyltransferase/1
activity in B cells.
Keusch J, Lydyard PM, Delves PJ.
Department of Immunology, University College London, Windeyer Building, 46
Cleveland Street, London W1P 6DB, UK.
An absence of galactose on the N/linked oligosaccharides of immunoglobulin G
(IgG) has been shown to affect the functional activity of the antibody molecule.
In patients with rheumatoid arthritis there is an increased proportion of IgG
which lacks galactose and correspondingly lower levels of beta1,
4/galactosyltransferase (beta4Gal/T) activity. The recent demonstration of
several expressed beta4Gal/T genes in man raises the possibility that the enzyme
responsible for the decreased IgG galactose is not the "classical" beta4Gal/T
(beta4Gal/T1). To directly address the question of whether reduced beta4Gal/T1
would lead to reduced IgG galactose, the level of beta4Gal/T1 in a human
IgG/secreting B cell line was specifically altered using stable transfection with
sense (SpcDNA3/Gal/T1) or antisense (ASpcDNA3/Gal/T1) human beta4Gal/T1 cDNA.
SpcDNA3/Gal/T1 B cell transfectants expressed up to a 2.5/fold higher level of
beta4Gal/T enzyme activity for the exogenous neoglycoconjugate acceptor
GlcNAc/pITC/BSA than did ASpcDNA3/Gal/T1 transfectants. Flow cytometric analysis
with Ricinus communis agglutinin I (RCAI) revealed an overall greater number of
Galbeta1,4GlcNAc structures in the fixed and permeabilized SpcDNA3/Gal/T1 B cell
transfectants compared with the ASpcDNA3/Gal/T1 transfectants. Moreover, there
was increased galactosylation of IgG secreted from the SpcDNA3/Gal/T1
transfectants relative to the ASpcDNA3/Gal/T1 B cell transfectants. Alteration of
the level of the "classical" beta4Gal/T (beta4Gal/T1) in B cells therefore
affects IgG glycosylation.
PMID: 9858643 [PubMed / indexed for MEDLINE]
Related Links
Glycoengineering of therapeutic glycoproteins: in vitro galactosylation and
sialylation of glycoproteins with terminal N/acetylglucosamine and galactose
residues. [Biochemistry. 2001] PMID:11467948
Cloning of a novel member of the UDP/galactose:beta/N/acetylglucosamine
beta1,4/galactosyltransferase family, beta4Gal/T4, involved in glycosphingolipid
biosynthesis. [J Biol Chem. 1998] PMID:9792633
A family of human beta4/galactosyltransferases. Cloning and expression of two
novel UDP/galactose:beta/n/acetylglucosamine beta1, 4/galactosyltransferases,
beta4Gal/T2 and beta4Gal/T3. [J Biol Chem. 1997] PMID:9405390
Ammonium alters N/glycan structures of recombinant TNFR/IgG: degradative versus
biosynthetic mechanisms. [Biotechnol Bioeng. 2000] PMID:10799988
Oligosaccharide preferences of beta1,4/galactosyltransferase/I: crystal
structures of Met340His mutant of human beta1,4/galactosyltransferase/I with a
pentasaccharide and trisaccharides of the N/glycan moiety. [J Mol Biol. 2005]
PMID:16157350
5: J Immunol Methods. 1998 Apr 15;213(2):113/30.
Quantitation of the oligosaccharides of human serum IgG from patients with
rheumatoid arthritis: a critical evaluation of different methods.
Routier FH, Hounsell EF, Rudd PM, Takahashi N, Bond A, Hay FC, Alavi A, Axford
JS, Jefferis R.
Department of Biochemistry and Molecular Biology, University College London, UK.
Several different chromatographic methods and a lectin/based assay have been
compared for the quantitation of oligosaccharides released from immunoglobulin G
(IgG). The analysis of a series of IgG samples purified from the serum of
rheumatoid arthritis patients was carried out by these methods to evaluate the
percentage of the glycoforms having 0, 1 or 2 galactose residues (G0, G1 and G2)
in order to (a) identify the method that can be most widely used for
quantitation, (b) accurately define the range of G0 values found in patients with
rheumatoid arthritis, and (c) make available a series of characterised standards
for distribution to clinical chemistry laboratories. The chromatographic methods
involved: release of oligosaccharides by glycoamidase A after protease digestion
followed by HPLC analysis of aminopyridine derivatives on reverse phase and
normal phase columns; hydrazinolysis treatment with exoglycosidases (G0 mix) and
Biogel P4 chromatography of 2/aminobenzamide (2/AB) derivatives; hydrazinolysis
and weak anion exchange or normal phase HPLC of 2/AB derivatives; release of
oligosaccharides by PNGase F and either Biogel P4 chromatography of 2/AB
derivatives or HPAEC/PAD analysis of native oligosaccharides. The G0 values given
by these methods compared favourably with each other and a dot blot assay of
denatured IgG interaction with Ricinus communis agglutinin and Bandeiraea
simplicifolialectin II. The HPLC and HPAEC methods give additional information
that may be important in less routine assays.
PMID: 9692845 [PubMed / indexed for MEDLINE]
Related Links
Autoantibody activity of IgG rheumatoid factor increases with decreasing levels
of galactosylation and sialylation. [J Biochem. 2000] PMID:11011144
Characterization of changes in IgG associated oligosaccharide profiles in
rheumatoid arthritis, psoriatic arthritis, and ankylosing spondylitis using
fluorophore linked carbohydrate electrophoresis. [J Rheumatol. 2001]
PMID:11469458
Alterations in the carbohydrate structures of an abnormal protein from sera of
patients with rheumatoid arthritis. [Arch Biochem Biophys. 1993] PMID:8239648
Detection of disease/specific augmentation of abnormal immunoglobulin G in sera
of patients with rheumatoid arthritis. [Glycoconj J. 1998] PMID:10052597
Structural changes in the oligosaccharide moiety of human IgG with aging.
[Glycoconj J. 1998] PMID:9881774
6: Clin Chem Lab Med. 1998 Feb;36(2):99/102.
Fucosylation and galactosylation of IgG heavy chains differ between acute and
remission phases of juvenile chronic arthritis.
Flögel M, Lauc G, Gornik I, Macek B.
Department of Biochemistry and Molecular Biology, Faculty of Pharmacy and
Biochemistry, University of Zagreb, Croatia.
Oligosaccharide structures are attached to nearly all membrane and serum
proteins, and their composition changes significantly in many diseases. We have
analysed glycosylation of IgG heavy chains in 34 patients with juvenile chronic
arthritis and 13 control individuals. IgG was purified from 0.7 ml of serum,
separated by electrophoresis and transferred on to polyvinylidene difluoride
(PVDF) membrane. Ricinus communis agglutinin (RCA I) and Bandeirea simplicifolia
(BSA II) and Ulex europaeus (UEA I) lectins were used to measure galactose,
N/acetylglucosamine and fucose, respectively. While there was no significant
difference in average levels of galactose and N/acetylglucosamine, patients with
juvenile chronic arthritis had 2.4 times more fucose attached to IgG heavy chains
than control individuals. A different picture emerged when patients were divided
into those with acute disease and those in remission. Patients in whom juvenile
chronic arthritis was currently active had significantly lower levels of
galactose than those in remission, in whom galactose levels were comparable to
the control group. Fucose levels in both groups of patients were significantly
higher than in the control group. These results show that whereas
de/galactosylation is a good test to detect and measure the activity of juvenile
chronic arthritis, increased fucosylation is a much more reliable measure for
diagnosis of the disease itself.
PMID: 9594046 [PubMed / indexed for MEDLINE]
Related Links
Fucosylation of IgG heavy chains is increased in rheumatoid arthritis. [Clin
Biochem. 1999] PMID:10638942
The relationship between exposed galactose and N/acetylglucosamine residues on
IgG in rheumatoid arthritis (RA), juvenile chronic arthritis (JCA) and Sjögren's
syndrome (SS). [Clin Exp Immunol. 1996] PMID:8697643
Glycoengineering of therapeutic glycoproteins: in vitro galactosylation and
sialylation of glycoproteins with terminal N/acetylglucosamine and galactose
residues. [Biochemistry. 2001] PMID:11467948
A detailed lectin analysis of IgG glycosylation, demonstrating disease specific
changes in terminal galactose and N/acetylglucosamine. [J Autoimmun. 1997]
PMID:9080302
Reduction in IgG galactose in juvenile and adult onset rheumatoid arthritis
measured by a lectin binding method and its relation to rheumatoid factor. [Ann
Rheum Dis. 1991] PMID:1929582
7: Br J Rheumatol. 1996 Apr;35(4):335/41.
Agalactosyl IgG in aggregates from the rheumatoid joint.
Leader KA, Lastra GC, Kirwan JR, Elson CJ.
Department of Pathology and Microbiology, School of Medical Sciences, Bristol.
It has been postulated that agalactosyl immunoglobulin G (IgG) self/associates to
form pathological aggregates in the rheumatoid joint. To examine this hypothesis,
IgG aggregates from synovial fluid (SF) of 22 patients with RA were prepared by
precipitation with polyethylene glycol (PEG) 6000. The PEG precipitates and SFs
were reduced with 2/mercaptoethanol (2ME) and bound to protein G. This procedure
isolated the IgG in the PEG precipitates from other contaminating glycosylated
proteins. The levels of galactose and N/acetylglucosamine (GlcNAc) residues
present on the reduced IgG were quantified by their ability to bind the lectins
Ricinus communis (RCA)120 and Bandeiraea simplicifolia (BS) II. Proportionally
less galactose (expressed as a ratio of bound RCA120 to BS II) was present on the
IgG from the PEG precipitates than on the IgG in the paired SF (P = 0.001).
However, in many cases more RCA120 as well as BS II bound to IgG from PEG
precipitates than from the corresponding SF. It is considered that agalactosyl
IgG occurs preferentially in RA SF PEG precipitates and that this IgG may also
exhibit increased Fab glycosylation.
PMID: 8624636 [PubMed / indexed for MEDLINE]
Related Links
Isolation and analysis of complement activating aggregates from synovial fluid of
patients with rheumatoid arthritis using monoclonal anti/C3d antibodies. [Ann
Rheum Dis. 1987] PMID:3492971
Immune complexes from rheumatoid arthritis synovial fluid induce FcgammaRIIa
dependent and rheumatoid factor correlated production of tumour necrosis
factor/alpha by peripheral blood mononuclear cells. [Arthritis Res Ther. 2006]
PMID:16569263
Depressed degranulation response of synovial fluid polymorphonuclear leucocytes
from patients with rheumatoid arthritis to IgG aggregates. [Clin Exp Immunol.
1990] PMID:2155727
Asialylated IgG in the serum and synovial fluid of patients with rheumatoid
arthritis. [J Rheumatol. 1992] PMID:1512760
Immunoglobulin G glycosylation and clinical outcome in rheumatoid arthritis
during pregnancy. [J Rheumatol. 2000] PMID:10852257
8: J Immunol Methods. 1993 Nov 5;166(1):27/33.
Human IgG preparations isolated by ion/exchange or protein G affinity
chromatography differ in their glycosylation profiles.
Bond A, Jones MG, Hay FC.
Department of Cellular and Molecular Sciences, St. George's Hospital Medical
School, London, UK.
IgG from patients with rheumatoid arthritis (RA) is abnormally glycosylated in
the Fc region, with sialic acid and galactose levels lower than normal. Protein G
and DEAE purify populations which are differentially glycosylated. Significantly
increased exposure of sialic acid was detected in normal IgG compared with that
of RA IgG when ion exchange was used to prepare samples. However, when the same
samples were prepared using protein G, no difference in the detection of sialic
acid was seen between the two groups. When examining the heavy chain of IgG, more
sialic acid, galactose and N/acetylglucosamine were detected in DEAE purified IgG
compared with that prepared by protein G Detection of sialic acid and
N/acetylglucosamine was also increased on light chains from IgG prepared by ion
exchange chromatography. Since this occurs notably on rheumatoid light chains it
would appear that this arrangement would contribute to the overall glycosylation
changes in IgG. In the case of molecules lacking galactose the discrimination
between the RA and normal IgG is significantly improved when ion exchange
chromatography is used. Since differentiation between disease and normal groups
relies on the purification technique used, we recommend that more than one method
is employed before undertaking an analysis of glycosylation changes.
PMID: 8228286 [PubMed / indexed for MEDLINE]
Related Links
Detection of glycosylation abnormality in rheumatoid IgG using
N/acetylglucosamine/specific Psathyrella velutina lectin. [J Immunol. 1993]
PMID:8335895
Fucosylation of IgG heavy chains is increased in rheumatoid arthritis. [Clin
Biochem. 1999] PMID:10638942
Glycan analysis of monoclonal antibodies secreted in deposition disorders
indicates that subsets of plasma cells differentially process IgG glycans.
[Arthritis Rheum. 2006] PMID:17075835
Alterations in carbohydrate composition of serum IgG from patients with
rheumatoid arthritis and from pregnant women. [Ann Rheum Dis. 1988] PMID:3355256
Detection of immunoglobulin G glycosylation changes in patients with rheumatoid
arthritis by means of isoelectric focusing and lectin/affinoblotting.
[Electrophoresis. 1995] PMID:7588567
9: J Rheumatol. 1992 Jul;19(7):1070/4.
Asialylated IgG in the serum and synovial fluid of patients with rheumatoid
arthritis.
Casburn/Budd R, Youinou P, Hager H, Elkington D, Baxter I, Berthelot JM, Le Goff
P, Isenberg DA.
Department of Research and Development, Cambridge Life Sciences Place, Ely,
Cambridgeshire, UK.
A novel enzyme linked immunosorbent assay has been developed that detects an
asialylation change in the IgG molecules from patients with rheumatoid arthritis
(RA) by the binding of biotinylated RCA 1 (ricin) to capture IgG. Elevated levels
of asialylated IgG were detected in paired serum and synovial fluids (SF) of
patients with RA. When compared with healthy controls, particularly in the SF (p
less than 0.05) correlations of the asialylation change were found in paired
samples (p less than 0.01) and between asialylated IgG and rheumatoid factors (p
less than 0.01), C/reactive protein (p less than 0.02) and the Lee and Ritchie
indices p less than 0.02 and 0.05, respectively. We found the proportion of
asialylated IgG was higher in DR4 positive patients, indicating a possible
association of these individuals to a sialyl transferase abnormality.
PMID: 1512760 [PubMed / indexed for MEDLINE]
Related Links
Immunoglobulin G and A antibody responses to Bacteroides forsythus and Prevotella
intermedia in sera and synovial fluids of arthritis patients. [Clin Diagn Lab
Immunol. 2003] PMID:14607865
Clinical and laboratory parameters which affect soluble interleukin/2 receptor
levels in the serum and synovial fluids of patients with rheumatoid arthritis.
[Ann Rheum Dis. 1993] PMID:8311539
Detection of glycosylation abnormality in rheumatoid IgG using
N/acetylglucosamine/specific Psathyrella velutina lectin. [J Immunol. 1993]
PMID:8335895
Tiopronine/induced reduction of rheumatoid factor functional affinity and
asialylated IgG in patients with rheumatoid arthritis. [Clin Exp Rheumatol. 1992]
PMID:1395217
Galactose terminating oligosaccharides of IgG in patients with primary Sjögren's
syndrome. [J Autoimmun. 1992] PMID:1388642
10: J Autoimmun. 1992 Jun;5(3):393/400.
Galactose terminating oligosaccharides of IgG in patients with primary Sjögren's
syndrome.
Youinou P, Pennec YL, Casburn/Budd R, Dueymes M, Letoux G, Lamour A.
Laboratory of Immunology, Brest University Medical School, France.
Using a simple but novel ELISA, we have screened 40 serum samples from patients
with primary Sjögren's syndrome and 34 normal controls for IgG glycosylation
deficiencies, identified by their specific ricin binding. Elevated levels of
asialylated IgG were detected in 24 patients. The extent of asialylation was
significantly higher in the patients with extraglandular manifestations than in
the others. Interestingly, the correlation of asialylated IgG was apparent only
with Raynaud's phenomenon and arthritis, and not other extraglandular
manifestations. Strong correlations (P less than 0.01) were noted between
asialylated IgG and rheumatoid factor or IgA/containing immune complexes.
PMID: 1388642 [PubMed / indexed for MEDLINE]
Related Links
Detection of anti/SS/A/Ro and anti/SS/B/La antibodies of IgA and IgG isotypes in
saliva and sera of patients with Sjögren's syndrome. [Nihon Rinsho Meneki Gakkai
Kaishi. 2003] PMID:14752936
Anti/agalactosyl IgG antibodies and isotype profiles of rheumatoid factors in
Sjögren's syndrome and rheumatoid arthritis. [Clin Exp Rheumatol. 1998]
PMID:9844764
Increased N/linked glycosylation leading to oversialylation of monomeric
immunoglobulin A1 from patients with Sjögren's syndrome. [Scand J Immunol. 2000]
PMID:10736100
IgA/containing immune complexes in the circulation of patients with primary
Sjögren's syndrome. [J Autoimmun. 1991] PMID:2031660
IgA glycosylation abnormalities in the serum of patients with primary Sjögren's
syndrome. [Clin Exp Rheumatol. 1995] PMID:7656472
11: J Immunol Methods. 1990 Jul 20;131(1):127/36.
Analysis of glycosylation changes in IgG using lectins.
Sumar N, Bodman KB, Rademacher TW, Dwek RA, Williams P, Parekh RB, Edge J, Rook
GA, Isenberg DA, Hay FC, et al.
Department of Immunology, University College and Middlesex School of Medicine,
London, U.K.
A simple rapid assay based on the ability of lectins to bind carbohydrates has
been developed to analyse changes in the oligosaccharide chains of IgG.
Bandeiraea simplicifolia lectin and Ricinus communis agglutinin have been used to
detect terminal N/acetylglucosamine and galactose moieties respectively in IgG
using immunodot/blotting. IgG samples (approximately 1 micrograms) were
dot/blotted onto nitrocellulose followed by boiling of the blots to expose the
carbohydrate moieties. The blots were then treated with biotinylated lectins
followed by either streptavidin/biotin/hydrogen peroxidase conjugate or
125I/labelled streptavidin. The colour was developed using chloronaphthol and the
blots read on a densitometer. The labelled blots were cut and read on a gamma
counter. The use of a monoclonal antibody to N/acetylglucosamine is also
discussed. The results obtained using this method are comparable to those
obtained by structural analysis.
PMID: 2199577 [PubMed / indexed for MEDLINE]
Related Links
Detection of immunoglobulin G glycosylation changes in patients with rheumatoid
arthritis by means of isoelectric focusing and lectin/affinoblotting.
[Electrophoresis. 1995] PMID:7588567
Characterization of changes in IgG associated oligosaccharide profiles in
rheumatoid arthritis, psoriatic arthritis, and ankylosing spondylitis using
fluorophore linked carbohydrate electrophoresis. [J Rheumatol. 2001]
PMID:11469458
Detection of glycosylation abnormality in rheumatoid IgG using
N/acetylglucosamine/specific Psathyrella velutina lectin. [J Immunol. 1993]
PMID:8335895
Glycosylation of IgG, immune complexes and IgG subclasses in the MRL/lpr/lpr
mouse model of rheumatoid arthritis. [Eur J Immunol. 1990] PMID:2242757
Analysis of different glycosylation states in IgG subclasses. [Clin Chim Acta.
1996] PMID:8853562
12: Clin Chem. 1989 Aug;35(8):1638/43.
Aberrant lectin/binding activity of immunoglobulin G in serum from rheumatoid
arthritis patients.
Parkkinen J.
Department of Gynecology & Obstetrics, University Central Hospital, Helsinki,
Finland.
Structural studies of oligosaccharide chains of immunoglobulin G (IgG) in serum
have revealed a specific galactosylation deficiency associated with rheumatoid
arthritis (RA). Using a two/site lectin/immunofluorometric assay, I studied the
interaction of IgG with immobilized lectins. Compared with control IgG, IgG
purified from RA patients' sera bound up to 40/fold more strongly to immobilized
Bandeiraea simplicifolia agglutinin II, a lectin that specifically binds agalacto
forms of other glycoproteins. However, inhibition studies and treatment of IgG
with glycosidase suggested that only a minor part of this binding was mediated by
agalacto oligosaccharides of IgG. Furthermore, these IgG samples bound even more
intensively to some other immobilized lectins, including Ricinus communis
agglutinin (RCA). The binding to RCA was not inhibited by lactose, a hapten sugar
of RCA, whereas other lectin species in solution effectively inhibited it.
Compared with intact RA IgG, isolated F(ab')2 fragments displayed only low
RCA/binding activity. These results indicate the existence of a
carbohydrate/nondependent interaction between RA IgG and different plant lectins.
With use of immobilized RCA, the lectin/immunofluorometric assay was rapid and
reproducible for measuring the aberrant lectin/binding activity of IgG directly
in diluted serum samples.
PMID: 2758632 [PubMed / indexed for MEDLINE]
Related Links
Characterization of changes in IgG associated oligosaccharide profiles in
rheumatoid arthritis, psoriatic arthritis, and ankylosing spondylitis using
fluorophore linked carbohydrate electrophoresis. [J Rheumatol. 2001]
PMID:11469458
Detection of disease/specific augmentation of abnormal immunoglobulin G in sera
of patients with rheumatoid arthritis. [Glycoconj J. 1998] PMID:10052597
Detection of glycosylation abnormality in rheumatoid IgG using
N/acetylglucosamine/specific Psathyrella velutina lectin. [J Immunol. 1993]
PMID:8335895
Analysis of agalacto/IgG in rheumatoid arthritis using surface plasmon resonance.
[Glycoconj J. 2000] PMID:11261841
Glycobiology: 'the function of sugar in the IgG molecule'. [J Anat. 1995]
PMID:7591992
