[The content of interleukin-1 beta in the blood serum of patients with systemic lupus erythematosus and rheumatoid arthritis]. / Issledovanie soderzhaniia interleikina-1 beta v syvorotke krovi bol'nykh sistemnoi krasnoi volchankoi i revmatoidnym artritom.

The enzyme immunoassay determined serum levels of interleukin-1 beta (IL-1 beta) in 35 patients with systemic lupus erythematosus (SLE) and 18 rheumatoid arthritis (RA) patients. In high activity of both SLE and RA as well as in the presence of fever, anemia, marked skin vasculitis IL-1 beta rose high, still higher levels being reported in patients with erosive joints compared to those in RA patients with initial stage of RA. Lower IL-1 beta content often marked nephropathy in both the diseases. Corticosteroids and cytostatics resulted in IL-1 beta fall which was also established in 9 SLE and 3 RA patients in parallel with inhibition of the process activity.

Interleukin-1 and tumour necrosis factor production by human monocytoid cells: study on a single cell level.

Human IL-1 beta and TNF alpha production by normal and transformed monocytoid cells was studied using biological assays, cytokine specific ELISA and by immunocytochemical methods on a single cell level. Quiescent human blood monocytes and cultured in vitro transformed human monocytoid cell lines U-937, THP-1 and HL-60 did not contain IL-1 beta and TNF alpha in their cytoplasm. IL-1 beta synthesis and secretion was induced by LPS stimulation in nearly 90% monocytes, 15-20% U-937, 3-5% THP-1 and in no HL-60 cells. Normal human blood monocytes had a more rapid kinetics of IL-1 beta synthesis. IL-1 beta positive cells stained with antibodies to human IL-1 beta appeared at 1-2 hours after LPS application, while in monocytic cell lines only after 4-6 hours. Using immunoperoxidase staining of U-937 cells pulse labelled with 3H-thymidine, it was shown that proliferating cells did not synthetize IL-1 beta. Instead of IL-1 beta, TNF alpha could be induced by LPS in U-937 cells only after preliminary differentiation with PMA. Recombinant IL-1 beta induced a very low level of TNF alpha production in PMA-treated cells. Similarly recombinant TNF alpha alone induced IL-1 beta synthesis only in a few U-937 cells.

Purification and characterization of the immunostimulatory properties of recombinant human interleukin-1 beta.

In this study we have used a new method for human recombinant IL-1 beta (rIL-1 beta) purification and investigated its immunostimulatory biological activity. The IL-1 beta gene was cloned using a novel mRNA preparation from activated human blood monocytes. The purification protocol consists of extraction and two chromatographic steps using the new Soloza cation exchange resin. The purified protein was characterized electrophoretically, by amino acid analysis and reverse phase chromatography. The protein migrated on SDS-PAGE with a molecular weight of 18.200 but demonstrated the minor presence of aggregates (dimers and trimers). Specific activity of purified rIL-1 beta in comitogenic assay on mouse thymocytes was 10(8) U/mg protein. rIL-1 beta increased in a dose dependent manner proliferation of Con A-stimulated murine thymocytes, splenocytes, PHA-stimulated human peripheral blood lymphocytes and transformed B-cell lines. Comitogenic activity depended on the degree of lymphocyte preactivation and was similar to that of natural human IL-1 beta. rIL-1 beta enhanced IL-2 production by murine spleen cells and EL-4 cell line and IL-2 receptor expression by human peripheral blood mononuclear cells. It induced PGE2 release from human blood monocytes but had no effect on human neutrophil chemotaxis, phagocytosis and respiratory burst.

[Interleukin-1-like factor from human B-lymphocytes transformed by the Epstein-Barr virus]. / Interleikin-1-podobnyi faktor iz B-limfotsitov cheloveka, transformirovannykh virusom Epshteina--Barra.

The NC-37, EBV-transformed human B-lymphoblastoid cell line spontaneously produces interleukin (IL)-1-like factor, which is able to stimulate proliferation of mouse thymocytes and human fibroblasts. The IL-1-like factor production can be enhanced by prodigiozan and by the conditioned medium of human peripheral blood mononuclear cells. The NC-37 cells have a membrane-associated form of IL-1-like factor also. The molecular mass of the intracellular precursor of this factor determined by gel-filtration is 35-40 kDa, and that of the secretory form--18-20 kDa. The secretory form has the following isoelectric points: 4.5; 6.8; 7.2-8.4.

[Isolation and properties of interleukin 1 from human blood monocytes]. / Poluchenie i svoistva interleikina-1 iz monotsitov krovi cheloveka.

Among different tested substances LPS-containing preparations were found to be most effective inducers of secretory interleukin-1 in human peripheral blood monocytes in vitro. IL-1 from supernatant of prodigiozan- + con A-stimulated monocytes had a MM of 18-20 KD and pI of 5.2-5.4 and 6.8 revealing an equal comitogenic activity and of 6.0 (minor peak).

[Purification and partial biochemical characterization of the rabbit interleukin-1]. / Ochistka i chastichnaia biokhimicheskaia kharakteristika interleikina-1 krolika.

Rabbit interleukin-1 produced by peritoneal macrophages has been purified and partly characterized. The molecular mass of the protein as determined by gel filtration and SDS-PAAG electrophoresis is about 16-17 kD. The isoelectric points of interleukin-1 are as follows: 5.00, 6.75, 7.65, 8.75. A minor peptide possessing the interleukin-1 activity whose molecular mass determined by high performance liquid chromatography gel filtration is about 1500-3000 Da has also been discovered.