Endotoxic potency of the Legionella pneumophila: recent data.
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Biomedical subjects
Publications and source records attributed to D Fumarola.
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Armadillo lepromin activates human lymphocytes from normal donors to release leucocyte inhibiting factor. The above activity was expressed optimally when leucocytes were incubated with lepromin at 37 degrees C, and only partially when incubation was carried out at 30 degrees C or at 35 degrees C. The possible mechanism of the in vitro production of lymphokine from lymphocytes stimulated by armadillo lepromin is discussed.
The in vitro effect of several bacterial endotoxins on human platelets was determined. Nine different endotoxins failed to induce aggregation in platelet-rich plasma (PRP) or of platelets washed by two different methods; four of them which we studied further failed to induce [14C]serotonin release in PRP. In contrast, using recently described test systems for platelet coagulant activity, all the endotoxins shortened the latent period occurring before aggregation of a mixture of washed platelets, normal serum, and CaCl2, and the clotting time of this mixture upon addition of fibrinogen. Washed platelets obtained from PRP preincubated with endotoxin had a higher platelet coagulant activity than platelets obtained from PRP preincubated with buffer. Washed platelets contribute to thrombin generation by providing factor V, a factor X activator and possibly phospholipid. Since the endotoxins did not influence the factor V activity of platelets or the platelet factor 3 activity, either in PRP or using platelets washed by albumin density gradient centrifugation, it is suggested that they enhance the factor-X activator activity of human platelets.
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It has been demonstrated that human peripheral lymphocytes incubated in a tissue culture medium containing 0.04, 0.1, or 0.15 microgram/ml of leucogenenol form or release a factor that inhibits the migration of human peripheral PMN leukocyte. The factor is chromatographed of Sephadex G-100 and migrates on electrophoresis as an albumin, thus suggesting that it has the electric charge of an albumin. The factor is stable to neuraminidase and to heating at 56 degrees C for 30 min, but it is inactivated by heating at 80 degrees C for 60 min. Its physical and biological properties suggest that the factor is identical to the LIF reported by Rocklin.