A macrophage-derived factor induced by α1-acid glycoprotein that inhibits IL-1 comitogenic activity
Autor: | Effat Kodari, Geneviève Durand, Jean Agneray, Phuong Nhi Bories, Jean-Denis Rouzeau, Jeanne Feger |
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Rok vydání: | 1990 |
Předmět: |
Hot Temperature
medicine.medical_treatment Immunology Biology Lymphocyte Activation Biological Factors Mice medicine Animals Immunology and Allergy Secretion Phytohemagglutinins Cells Cultured Chromatography Mice Inbred C3H Molecular mass Cell growth Macrophages Biological activity Orosomucoid Thymocyte Cytokine Biochemistry Mice Inbred DBA Concanavalin A biology.protein Tumor necrosis factor alpha Interleukin-1 |
Zdroj: | Immunology Letters. 26:105-110 |
ISSN: | 0165-2478 |
Popis: | After exposure to a concanavalin A (Con A)-unreactive variant of alpha 1-acid glycoprotein (AGP), macrophages released an inhibitor of interleukin-1 (IL-1) proliferative activity in the thymocyte comitogenic assay. This effect was observed with AGP concentrations above 100 micrograms/ml in the macrophage supernatant and would appear to be mediated by the macrophages, since native AGP had no activity on thymocyte proliferation. Preliminary physicochemical characterization showed that the factor was partially resistant to heating, undialyzable, and eluted with an apparent molecular mass of 50-100 kDa when subjected to Sephacryl S-200 chromatography. Murine IL-1 and human (h) recombinant (r) IL-1 were affected by this factor to the same extent. IL-1 and IL-2 co-induced thymocyte proliferation, which is mitogen-independent, was also inhibited, whereas hrIL-2 activity was not suppressed when assayed in thymocytes with PHA at a submitogenic concentration or in CTLL cells. The factor did not interfere with TNF alpha or hrIL-6 activity when tested against their specific cell line. These data indicate that the inhibitor may act specifically against IL-1 activity and further elucidate the possible role of AGP in the modulation of IL-1 activity via the secretion of an inhibitor. |
Databáze: | OpenAIRE |
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