Interleukin 1 and the glomerular mesangium. I. Purification and characterization of a mesangial cell-derived autogrowth factor.
Open Access
- 15 May 1986
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Immunology
- Vol. 136 (10) , 3700-3705
- https://doi.org/10.4049/jimmunol.136.10.3700
Abstract
The proteins expressing interleukin 1 (IL 1) activity from rat peritoneal macrophages and cultured glomerular mesangial cells were compared after purification to apparent homogeneity. The purified IL 1 shared a number of biochemical features including m.w., charge, and specific activity. These findings were extended by the results of proteolytic peptide mapping, which revealed similar breakdown oligopeptides, confirming the close resemblance of these two IL 1 species produced by macrophages and mesangial cells. The purified mesangial cell IL 1 acts as an autocrine or paracrine growth factor. The local release of this cytokine may be an important factor in glomerular diseases characterized by mesangial proliferation and matrix expansion.This publication has 18 references indexed in Scilit:
- A thymocyte-activating factor derived from glomerular mesangial cells.The Journal of Immunology, 1983
- Neutral proteinase activity produced in vitro by cells of the glomerular mesangiumKidney International, 1983
- Production of prostaglandin E and an interleukin-1 like factor by cultured astrocytes and C6 glioma cells.The Journal of Immunology, 1982
- Physicochemical characterization of a PMN-derived soluble fraction that enhances lymphocyte DNA synthesis.The Journal of Immunology, 1982
- Murine epidermal cell-derived thymocyte-activating factor resembles murine interleukin 1.The Journal of Immunology, 1982
- MESANGIAL DISPOSAL OF GLOMERULAR IMMUNE DEPOSITS IN ACUTE MALARIAL GLOMERULONEPHRITIS OF RATS1982
- Purification to apparent homogeneity of murine interleukin 1.The Journal of Immunology, 1981
- Two-dimensional electrophoresis of small-molecular-weight proteinsAnalytical Biochemistry, 1979
- Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis.Journal of Biological Chemistry, 1977
- A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye BindingAnalytical Biochemistry, 1976