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Jens Christian Jensenius

Calcium-dependent and calcium-independent signals in the conglutinin-binding assay (KgBa) for immune complexes. Influence of anti-collagen-antibodies

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Calcium-dependent and calcium-independent signals in the conglutinin-binding assay (KgBa) for immune complexes. Influence of anti-collagen-antibodies. / Holmskov, Uffe Laurits; Haas, Henning de; Teisner, Børge; Andersen, Ove; Jensenius, Jens Christian.

In: Journal of Immunological Methods, Vol. 148, No. 1-2, 1992, p. 225-32.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Holmskov, UL, Haas, HD, Teisner, B, Andersen, O & Jensenius, JC 1992, 'Calcium-dependent and calcium-independent signals in the conglutinin-binding assay (KgBa) for immune complexes. Influence of anti-collagen-antibodies', Journal of Immunological Methods, vol. 148, no. 1-2, pp. 225-32.

APA

Holmskov, U. L., Haas, H. D., Teisner, B., Andersen, O., & Jensenius, J. C. (1992). Calcium-dependent and calcium-independent signals in the conglutinin-binding assay (KgBa) for immune complexes. Influence of anti-collagen-antibodies. Journal of Immunological Methods, 148(1-2), 225-32.

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MLA

Vancouver

Author

Holmskov, Uffe Laurits ; Haas, Henning de ; Teisner, Børge ; Andersen, Ove ; Jensenius, Jens Christian. / Calcium-dependent and calcium-independent signals in the conglutinin-binding assay (KgBa) for immune complexes. Influence of anti-collagen-antibodies. In: Journal of Immunological Methods. 1992 ; Vol. 148, No. 1-2. pp. 225-32.

Bibtex

@article{341aa81054304ea7b613f90182856258,
title = "Calcium-dependent and calcium-independent signals in the conglutinin-binding assay (KgBa) for immune complexes. Influence of anti-collagen-antibodies",
abstract = "A solid phase ELISA conglutinin-binding assay (KgBa) was evaluated for the detection of circulating immune complexes. ELISA wells were coated with purified bovine conglutinin and incubated with test sera. Bound IgG was detected with enzyme labelled anti-immunoglobulin. Heat aggregated IgG which had been {"}solubilized{"} (i.e., complement treated by incubation with serum) was employed as a reference. The binding of the complement-reacted IgG to solid phase conglutinin was found to be calcium-dependent and inhibitable with N-acetyl-D-glucosamine (GlcNAc). Prolonged incubation (4 days) of aggregated IgG with serum at 37 degrees C abolished the binding to conglutinin, a finding consistent with the complete degradation of deposited C3b to C3c and C3d. The solubilized IgG that bound to solid phase conglutinin was found by gel chromatography to be of high molecular weight (greater than 600 kDa). Binding of IgG to solid phase bovine conglutinin was also observed to a variable degree in normal and pathological sera. However, in this situation the IgG binding was largely calcium-independent, was not inhibited by GlcNAc and did not decrease after prolonged incubation of the serum at 37 degrees C. The reactive IgG eluted on gel chromatography at the position of monomeric IgG suggesting binding via the antigen binding sites. Binding of this IgG was inhibited by both collagen type II and purified conglutinin. These observations suggest that the assay detects cross-reacting autoantibodies against collagen epitopes, or, alternatively, antibodies against the dietary antigen, bovine conglutinin.",
keywords = "Acetylgalactosamine, Acetylglucosamine, Antigen-Antibody Complex, Antigen-Antibody Reactions, Autoantibodies, Calcium, Chromatography, Gel, Collagen, Complement Fixation Tests, Cross Reactions, Dose-Response Relationship, Immunologic, Enzyme-Linked Immunosorbent Assay, Humans, Immunoglobulin G",
author = "Holmskov, {Uffe Laurits} and Haas, {Henning de} and B{\o}rge Teisner and Ove Andersen and Jensenius, {Jens Christian}",
year = "1992",
language = "English",
volume = "148",
pages = "225--32",
journal = "Journal of Immunological Methods",
issn = "0022-1759",
publisher = "Elsevier BV",
number = "1-2",

}

RIS

TY - JOUR

T1 - Calcium-dependent and calcium-independent signals in the conglutinin-binding assay (KgBa) for immune complexes. Influence of anti-collagen-antibodies

AU - Holmskov, Uffe Laurits

AU - Haas, Henning de

AU - Teisner, Børge

AU - Andersen, Ove

AU - Jensenius, Jens Christian

PY - 1992

Y1 - 1992

N2 - A solid phase ELISA conglutinin-binding assay (KgBa) was evaluated for the detection of circulating immune complexes. ELISA wells were coated with purified bovine conglutinin and incubated with test sera. Bound IgG was detected with enzyme labelled anti-immunoglobulin. Heat aggregated IgG which had been "solubilized" (i.e., complement treated by incubation with serum) was employed as a reference. The binding of the complement-reacted IgG to solid phase conglutinin was found to be calcium-dependent and inhibitable with N-acetyl-D-glucosamine (GlcNAc). Prolonged incubation (4 days) of aggregated IgG with serum at 37 degrees C abolished the binding to conglutinin, a finding consistent with the complete degradation of deposited C3b to C3c and C3d. The solubilized IgG that bound to solid phase conglutinin was found by gel chromatography to be of high molecular weight (greater than 600 kDa). Binding of IgG to solid phase bovine conglutinin was also observed to a variable degree in normal and pathological sera. However, in this situation the IgG binding was largely calcium-independent, was not inhibited by GlcNAc and did not decrease after prolonged incubation of the serum at 37 degrees C. The reactive IgG eluted on gel chromatography at the position of monomeric IgG suggesting binding via the antigen binding sites. Binding of this IgG was inhibited by both collagen type II and purified conglutinin. These observations suggest that the assay detects cross-reacting autoantibodies against collagen epitopes, or, alternatively, antibodies against the dietary antigen, bovine conglutinin.

AB - A solid phase ELISA conglutinin-binding assay (KgBa) was evaluated for the detection of circulating immune complexes. ELISA wells were coated with purified bovine conglutinin and incubated with test sera. Bound IgG was detected with enzyme labelled anti-immunoglobulin. Heat aggregated IgG which had been "solubilized" (i.e., complement treated by incubation with serum) was employed as a reference. The binding of the complement-reacted IgG to solid phase conglutinin was found to be calcium-dependent and inhibitable with N-acetyl-D-glucosamine (GlcNAc). Prolonged incubation (4 days) of aggregated IgG with serum at 37 degrees C abolished the binding to conglutinin, a finding consistent with the complete degradation of deposited C3b to C3c and C3d. The solubilized IgG that bound to solid phase conglutinin was found by gel chromatography to be of high molecular weight (greater than 600 kDa). Binding of IgG to solid phase bovine conglutinin was also observed to a variable degree in normal and pathological sera. However, in this situation the IgG binding was largely calcium-independent, was not inhibited by GlcNAc and did not decrease after prolonged incubation of the serum at 37 degrees C. The reactive IgG eluted on gel chromatography at the position of monomeric IgG suggesting binding via the antigen binding sites. Binding of this IgG was inhibited by both collagen type II and purified conglutinin. These observations suggest that the assay detects cross-reacting autoantibodies against collagen epitopes, or, alternatively, antibodies against the dietary antigen, bovine conglutinin.

KW - Acetylgalactosamine

KW - Acetylglucosamine

KW - Antigen-Antibody Complex

KW - Antigen-Antibody Reactions

KW - Autoantibodies

KW - Calcium

KW - Chromatography, Gel

KW - Collagen

KW - Complement Fixation Tests

KW - Cross Reactions

KW - Dose-Response Relationship, Immunologic

KW - Enzyme-Linked Immunosorbent Assay

KW - Humans

KW - Immunoglobulin G

M3 - Journal article

C2 - 1564328

VL - 148

SP - 225

EP - 232

JO - Journal of Immunological Methods

JF - Journal of Immunological Methods

SN - 0022-1759

IS - 1-2

ER -