Receptor for alpha1-microglobulin on T lymphocytes : inhibition of antigen-induced interleukin-2 production
(1998) In Scandinavian Journal of Immunology 48(1). p.1-7- Abstract
The human plasma protein alpha1-microglobulin (alpha1m) was found to inhibit the antigen-induced interleukin-2 (IL-2) production of two different mouse T-helper cell hybridomas. Alpha1m isolated from human plasma and recombinant alpha1m isolated from baculovirus-infected insect cell cultures had similar inhibitory effects. Flow cytometric analysis showed a binding of plasma and recombinant alpha1m to the T-cell hybridomas as well as to a human T-cell line. Radiolabelled plasma and recombinant alpha1m bound to the T-cell hybridomas in a saturable manner and the binding could be eliminated by trypsination of the cells. The affinity constants for the cell binding were calculated to be 0.4-1 x 10(5) M(-1) using Scatchard plotting, and the... (More)
The human plasma protein alpha1-microglobulin (alpha1m) was found to inhibit the antigen-induced interleukin-2 (IL-2) production of two different mouse T-helper cell hybridomas. Alpha1m isolated from human plasma and recombinant alpha1m isolated from baculovirus-infected insect cell cultures had similar inhibitory effects. Flow cytometric analysis showed a binding of plasma and recombinant alpha1m to the T-cell hybridomas as well as to a human T-cell line. Radiolabelled plasma and recombinant alpha1m bound to the T-cell hybridomas in a saturable manner and the binding could be eliminated by trypsination of the cells. The affinity constants for the cell binding were calculated to be 0.4-1 x 10(5) M(-1) using Scatchard plotting, and the number of binding sites per cell was estimated to be 5 x 10(5)-1 x 10(6). The cell-surface proteins of one of the T-cell hybridomas were radiolabelled, the cells lysed and alpha1m-binding proteins isolated by affinity chromatography. SDS-PAGE and autoradiography analysis of the eluate revealed major bands with Mr-values around 70, 35 and 15 kDa. The results thus suggest that alpha1m binds to a specific receptor on T cells and that the binding leads to inhibition of antigen-stimulated IL-2 production by T-helper cells.
(Less)
- author
- Wester, L ; Michaëlsson, E LU ; Holmdahl, R LU ; Olofsson, T LU and Åkerström, B LU
- organization
- publishing date
- 1998-07
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Alpha-Globulins/metabolism, Animals, Antigens/immunology, Collagen/immunology, Humans, Interleukin-2/biosynthesis, Mice, Receptors, Immunologic/metabolism, T-Lymphocytes/metabolism, Tumor Cells, Cultured
- in
- Scandinavian Journal of Immunology
- volume
- 48
- issue
- 1
- pages
- 7 pages
- publisher
- Wiley-Blackwell
- external identifiers
-
- pmid:9714404
- scopus:0031594846
- ISSN
- 0300-9475
- DOI
- 10.1046/j.1365-3083.1998.00378.x
- language
- English
- LU publication?
- yes
- id
- c0cce44d-a177-4031-beeb-84674ea8f6bb
- date added to LUP
- 2019-05-22 10:13:28
- date last changed
- 2024-01-01 06:39:45
@article{c0cce44d-a177-4031-beeb-84674ea8f6bb,
abstract = {{<p>The human plasma protein alpha1-microglobulin (alpha1m) was found to inhibit the antigen-induced interleukin-2 (IL-2) production of two different mouse T-helper cell hybridomas. Alpha1m isolated from human plasma and recombinant alpha1m isolated from baculovirus-infected insect cell cultures had similar inhibitory effects. Flow cytometric analysis showed a binding of plasma and recombinant alpha1m to the T-cell hybridomas as well as to a human T-cell line. Radiolabelled plasma and recombinant alpha1m bound to the T-cell hybridomas in a saturable manner and the binding could be eliminated by trypsination of the cells. The affinity constants for the cell binding were calculated to be 0.4-1 x 10(5) M(-1) using Scatchard plotting, and the number of binding sites per cell was estimated to be 5 x 10(5)-1 x 10(6). The cell-surface proteins of one of the T-cell hybridomas were radiolabelled, the cells lysed and alpha1m-binding proteins isolated by affinity chromatography. SDS-PAGE and autoradiography analysis of the eluate revealed major bands with Mr-values around 70, 35 and 15 kDa. The results thus suggest that alpha1m binds to a specific receptor on T cells and that the binding leads to inhibition of antigen-stimulated IL-2 production by T-helper cells.</p>}},
author = {{Wester, L and Michaëlsson, E and Holmdahl, R and Olofsson, T and Åkerström, B}},
issn = {{0300-9475}},
keywords = {{Alpha-Globulins/metabolism; Animals; Antigens/immunology; Collagen/immunology; Humans; Interleukin-2/biosynthesis; Mice; Receptors, Immunologic/metabolism; T-Lymphocytes/metabolism; Tumor Cells, Cultured}},
language = {{eng}},
number = {{1}},
pages = {{1--7}},
publisher = {{Wiley-Blackwell}},
series = {{Scandinavian Journal of Immunology}},
title = {{Receptor for alpha1-microglobulin on T lymphocytes : inhibition of antigen-induced interleukin-2 production}},
url = {{http://dx.doi.org/10.1046/j.1365-3083.1998.00378.x}},
doi = {{10.1046/j.1365-3083.1998.00378.x}},
volume = {{48}},
year = {{1998}},
}