We investigated serum levels of interleukin-6 (IL-6), interferon-gamma (IFN-gamma), and tumor necrosis factor alpha (TNF alpha) from patients with systemic lupus erythematosus (SLE) and its various clinical manifestations of disease and from patients with rheumatoid arthritis (RA) and other rheumatic diseases. The serum levels of IL-6 and IFN-gamma were highly elevated from patients with SLE associated with lymphadenopathy (LN) or nephrotic syndrome (NS). On the contrary, the serum levels of TNF alpha were elevated from most patients with SLE associated with thrombocytopenia (TP). However, serum levels of TNF alpha were in the normal range from patients with SLE associated with NS, LN, or central nervous system disease. Of interest, patients with SLE associated with humoral immunodeficiency disorder, hypogammaglobulinemia, had highly elevated levels of serum IL-6. The concanavalin A-stimulated mononuclear cells (MNC) of patients with SLE associated with TP secreted highly elevated levels of TNF alpha compared to other patient groups. We suggest that abnormal production of various cytokines in SLE is an intrinsic defect of MNC and the immune system that may be the key element for a variety of clinical manifestations of this disease.

No abstract

Lipopolysaccharides (LPS) of two isolates of Microcystis aeruginosa were extracted with phenol/water and purified. Cesium chloride gradient ultracentrifugation of these preparations yielded only one fraction. The LPS contained significant amounts of 3-deoxy-~-manno-octulosonic acid, glucose, 3-deoxy sugars, glucosamine, fatty acids, fatty acid esters, hexoses, and phosphate. Heptose, a characteristic sugar component of the polysaccharide moiety of LPS of most gram-negative bacteria was absent. Lipopolysaccharides and lipid A hydrolysate of LPS preparations were active in mouse lethality and Limufus lysate gelation. The lipid A moiety was slightly less active in toxicity and Limulus lysate gelation assays than the intact LPS. The LPS and lipid A moiety of the two isolates of M . aeruginosa were less active in toxicity in mice and Limulus test than LPS of Salmonella abortus equi.Lipopolysaccharides (LPS) are characteristic components of gram-negative bacteria [l]. They are usually toxic, highly inflammatory agents, responsible for the activation of numerous immunological, cellular and humoral-mediated systems [2-41. Chemical studies over two decades have established a detailed structure of many bacterial LPS. The LPS are amphiphilic compounds comprised of lipid A and polysaccharide moieties with lipid A being the toxic principle [5].While a great deal of information exists about LPS and lipid A moieties, there are only a limited number of studies conducted on the LPS compositions of the cyanobacteria [6-91. No studies have been conducted on the LPS of the cyanobacterium Microcystis aeruginosa although it is often the major organism in water blooms of eutrophic lakes and reservoirs [lo], it occurs world wide, causes serious water management problems and is correlated with domestic and wild-animal poisoning [lo]. To what extent the LPS contributes to the pathogenic or toxic properties of this organism is unknown. Here we report our preliminary findings on the isolation, composition and biological activities of the LPS contents of two isolates of M . aeruginosa. MATERIALS AND METHODS Orpanisms and culture Isolation of lipopolysaccharidesThe LPS were extracted by the hot phenollwater procedure of Westphal et al. [13]. A suspension of lyophilized cells (10 g/200 ml) in deionized water was heated at 68 "C and mixed with an equal volume of hot 90% phenol. After vigorously mixing for 20 min, at 68 "C, the mixture was cooled in an ice bath and separated into the aqueous and phenol phases by centrifugation at 3000 rev./min for 30 min. The upper (aqueous) phase was recovered and replaced with an equal volume of deionized water. The mixture was again heated at 68 "C for 20min, cooled and centrifuged to separate the phases. The aqueous phases were pooled and dialyzed against deionized water for 48 h and then centrifuged at 85000 x g for 5 h. The resulting pellet was suspended in 0.1 M Tris/HCl buffer, pH 7.4; ribonuclease A (Sigma Chemical Co., St Louis, MO) was added at a concentration of 25pg/ml. The mixture was incubated at...

No abstract