We describe the gene structure, regulation, signal transduction. and functions of a cytokine, interleukin (IL)-32. An IL-18 unresponsive cell was converted to a responsive cell by transfection of the IL-18 receptor beta chain, and IL-18-induced microarray revealed high expression of a cytokine-like gene. Although IL-32 does not share sequence homology with known cytokine families, IL-32 induces various cytokines, human TNFalpha, and IL-8 in THP-1 monocytic cells as well as mouse TNFalpha and MIP-2 in Raw macrophage cells. IL-32 activates typical cytokine signal pathways of nuclear factor-kappa B (NF-kappaB) and p38 mitogen-activated protein kinase. IL-32 mRNA is highly expressed in immune tissue rather than other tissues. Human IL-32 exists as four splice variants, and IL-32 from other species were found as expressed sequence tag clones in the databank. Induced in human peripheral lymphocyte cells after mitogen stimulation, in human epithelial cells by IFNgamma, and in NK cells after exposure to the combination of IL-12 plus IL-18, IL-32 may play a role in inflammatory/autoimmune diseases.

We describe the gene structure, regulation, signal transduction. and functions of a cytokine, interleukin (IL)-32. An IL-18 unresponsive cell was converted to a responsive cell by transfection of the IL-18 receptor beta chain, and IL-18-induced microarray revealed high expression of a cytokine-like gene. Although IL-32 does not share sequence homology with known cytokine families, IL-32 induces various cytokines, human TNFalpha, and IL-8 in THP-1 monocytic cells as well as mouse TNFalpha and MIP-2 in Raw macrophage cells. IL-32 activates typical cytokine signal pathways of nuclear factor-kappa B (NF-kappaB) and p38 mitogen-activated protein kinase. IL-32 mRNA is highly expressed in immune tissue rather than other tissues. Human IL-32 exists as four splice variants, and IL-32 from other species were found as expressed sequence tag clones in the databank. Induced in human peripheral lymphocyte cells after mitogen stimulation, in human epithelial cells by IFNgamma, and in NK cells after exposure to the combination of IL-12 plus IL-18, IL-32 may play a role in inflammatory/autoimmune diseases.

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Objective. To investigate the molecular mechanisms of the antiarthritic effects of bee venom (BV) and melittin (a major component of BV) in a murine macrophage cell line (Raw 264.7) and in synoviocytes obtained from patients with rheumatoid arthritis.Methods. We evaluated the antiarthritic effects of BV in a rat model of carrageenan-induced acute edema in the paw and in a rat model of chronic adjuvantinduced arthritis. The inhibitory effects of BV and melittin on inflammatory gene expression were measured by Western blotting, and the generation of prostaglandin E 2 (PGE 2 ) and nitric oxide (NO) and the intracellular calcium level were assayed. NF-B DNA binding and transcriptional activity were determined by gel mobility shift assay or by luciferase assay. Direct binding of BV and melittin to the p50 subunit of NF-B was determined with a surface plasmon resonance analyzer.Results. BV (0.8 and 1.6 g/kg) reduced the effects of carrageenan-and adjuvant-induced arthritis. This reducing effect was consistent with the inhibitory effects of BV (0.5, 1, and 5 g/ml) and melittin (5 and Conclusion. Target inactivation of NF-B by directly binding to the p50 subunit is an important mechanism of the antiarthritic effects of BV.

The evolution of structural parameters characterizing the semicrystalline morphology of poly(ary1-ether-ether-ketone) (PEEK), and its blends with poly(ary1-ether-imide) (PEI), has been determined as a function of temperature by means of small-angle (SAXS) and wide-angle (WAXS) X-ray scattering studies, using synchrotron radiation. By comparing the behavior of initially amorphous samples continuously heated in the beam and samples heated and cooled below and above their annealing temperature, a complete picture is drawn of the morphological changes occurring during the cold crystallization and subsequent heating-cooling of PEEK. Upon crystallization of an amorphous sample, new lamellae are progressively inserted in the free space left between existing ones. No decrease of the lamellar thickness is evident during this insertion mechanism. When the polymer is cooled below its last annealing temperature T,, only reversible morphological changes occur, which can be explained quantitatively by the effects of thermal expansion, provided one takes into account the existence of strains in the crystalline lamellae created by their coupling to the noncrystalline interlamellar regions. When the polymer is heated above T,, "irreversible" changes occur in the average thickness of the lamellar crystals and of the interlamellar noncrystalline regions, in the perfection of the crystals, and in the crystalline density. Cold-crystallized samples are shown to comprise a single lamellar population which undergoes a rapid melting-recrystallization process above T,. The double melting behavior of coldcrystallized PEEK results from this melting-recrystallization mechanism. IntroductionThe morphology and properties of a semicrystalline polymer depend on its thermal history. Therefore, when studying the morphology, changes in the structure as a function of the crystallization conditions and subsequent thermal treatments must be considered. Moreover, any