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IgG autoantibodies against interleukin 1 alpha in sera of normal individuals

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Standard

IgG autoantibodies against interleukin 1 alpha in sera of normal individuals. / Svenson, M; Poulsen, L K; Fomsgaard, A; Bendtzen, K.

I: Scandinavian Journal of Immunology, Bind 29, Nr. 4, 04.1989, s. 489-92.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Svenson, M, Poulsen, LK, Fomsgaard, A & Bendtzen, K 1989, 'IgG autoantibodies against interleukin 1 alpha in sera of normal individuals', Scandinavian Journal of Immunology, bind 29, nr. 4, s. 489-92.

APA

Svenson, M., Poulsen, L. K., Fomsgaard, A., & Bendtzen, K. (1989). IgG autoantibodies against interleukin 1 alpha in sera of normal individuals. Scandinavian Journal of Immunology, 29(4), 489-92.

Vancouver

Svenson M, Poulsen LK, Fomsgaard A, Bendtzen K. IgG autoantibodies against interleukin 1 alpha in sera of normal individuals. Scandinavian Journal of Immunology. 1989 apr;29(4):489-92.

Author

Svenson, M ; Poulsen, L K ; Fomsgaard, A ; Bendtzen, K. / IgG autoantibodies against interleukin 1 alpha in sera of normal individuals. I: Scandinavian Journal of Immunology. 1989 ; Bind 29, Nr. 4. s. 489-92.

Bibtex

@article{baa1efafd56c482ea925f9e4342b2c7b,
title = "IgG autoantibodies against interleukin 1 alpha in sera of normal individuals",
abstract = "A pool of human sera from healthy blood donors was found to interfere competitively with the binding of 125I-labelled human recombinant interleukin 1 alpha (rIL-1 alpha) to the murine T-cell line EL4. The interference was reversible at the cellular level, and direct binding of the ligand to serum factors was therefore investigated. After preincubation of [125I]rIL-1 alpha with pooled serum, the 125I activity eluted in two peaks from a Sephadex G-75 column. The first was located in the void volume. The second eluted together with monomer rIL-1 alpha. An almost complete displacement of the high molecular weight 125I fraction was achieved with an excess of unlabelled rIL-1 alpha but not with rIL-1 beta. The serum factors binding to [125I]rIL-1 alpha were located in the molecular weight range 100,000-200,000, judged by fractionation on a Sephacryl S-400 column, and the factors were bound to immobilized protein A. Furthermore, [125I]rIL-1 alpha preincubated with serum co-precipitated with a specific rabbit anti-human IgG antibody. Screening of 29 sera from normal individuals showed similar effects in three cases. We conclude that approximately 10{\%} of normal human sera contains detectable IgG autoantibodies to IL-1 alpha.",
keywords = "Adult, Animals, Autoantibodies, Binding Sites, Antibody, Cell Line, Chromatography, Gel, Humans, Immune Sera, Immunoglobulin G, Interleukin-1, Mice, Molecular Weight, Journal Article, Research Support, Non-U.S. Gov't",
author = "M Svenson and Poulsen, {L K} and A Fomsgaard and K Bendtzen",
year = "1989",
month = "4",
language = "English",
volume = "29",
pages = "489--92",
journal = "Scandinavian Journal of Immunology",
issn = "0300-9475",
publisher = "Wiley-Blackwell",
number = "4",

}

RIS

TY - JOUR

T1 - IgG autoantibodies against interleukin 1 alpha in sera of normal individuals

AU - Svenson, M

AU - Poulsen, L K

AU - Fomsgaard, A

AU - Bendtzen, K

PY - 1989/4

Y1 - 1989/4

N2 - A pool of human sera from healthy blood donors was found to interfere competitively with the binding of 125I-labelled human recombinant interleukin 1 alpha (rIL-1 alpha) to the murine T-cell line EL4. The interference was reversible at the cellular level, and direct binding of the ligand to serum factors was therefore investigated. After preincubation of [125I]rIL-1 alpha with pooled serum, the 125I activity eluted in two peaks from a Sephadex G-75 column. The first was located in the void volume. The second eluted together with monomer rIL-1 alpha. An almost complete displacement of the high molecular weight 125I fraction was achieved with an excess of unlabelled rIL-1 alpha but not with rIL-1 beta. The serum factors binding to [125I]rIL-1 alpha were located in the molecular weight range 100,000-200,000, judged by fractionation on a Sephacryl S-400 column, and the factors were bound to immobilized protein A. Furthermore, [125I]rIL-1 alpha preincubated with serum co-precipitated with a specific rabbit anti-human IgG antibody. Screening of 29 sera from normal individuals showed similar effects in three cases. We conclude that approximately 10% of normal human sera contains detectable IgG autoantibodies to IL-1 alpha.

AB - A pool of human sera from healthy blood donors was found to interfere competitively with the binding of 125I-labelled human recombinant interleukin 1 alpha (rIL-1 alpha) to the murine T-cell line EL4. The interference was reversible at the cellular level, and direct binding of the ligand to serum factors was therefore investigated. After preincubation of [125I]rIL-1 alpha with pooled serum, the 125I activity eluted in two peaks from a Sephadex G-75 column. The first was located in the void volume. The second eluted together with monomer rIL-1 alpha. An almost complete displacement of the high molecular weight 125I fraction was achieved with an excess of unlabelled rIL-1 alpha but not with rIL-1 beta. The serum factors binding to [125I]rIL-1 alpha were located in the molecular weight range 100,000-200,000, judged by fractionation on a Sephacryl S-400 column, and the factors were bound to immobilized protein A. Furthermore, [125I]rIL-1 alpha preincubated with serum co-precipitated with a specific rabbit anti-human IgG antibody. Screening of 29 sera from normal individuals showed similar effects in three cases. We conclude that approximately 10% of normal human sera contains detectable IgG autoantibodies to IL-1 alpha.

KW - Adult

KW - Animals

KW - Autoantibodies

KW - Binding Sites, Antibody

KW - Cell Line

KW - Chromatography, Gel

KW - Humans

KW - Immune Sera

KW - Immunoglobulin G

KW - Interleukin-1

KW - Mice

KW - Molecular Weight

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

M3 - Journal article

C2 - 2785711

VL - 29

SP - 489

EP - 492

JO - Scandinavian Journal of Immunology

JF - Scandinavian Journal of Immunology

SN - 0300-9475

IS - 4

ER -

ID: 169715065