Enhanced serum interferon-lambda 1/interleukin-29 levels in patients with psoriasis vulgaris

Abstract Background: Interferon (IFN)-λ1, also named Interleukin (IL)-29, is a new member of the Type III IFN or IFN-λ family. IL-29 plays an important role in the pathogenesis of many types of autoimmune and inflammatory diseases. Objective: To study the role of IL-29 in the pathogenesis of psoriasis vulgaris. Methods: The authors detected the serum levels of IL-29 in forty-one patients with psoriasis vulgaris, twenty-three patients with atopic dermatitis and thirty-eight age and gender-matched controls by sandwich Enzyme-Linked Immunosorbent Assay (ELISA). The effects of IL-29 on the expression of cytokines, such as IL-6, IL-17, IL-8, IL-4, IL10, Interferon (IFN-γ) and Tumor Necrosis Factor-α (TNF-α), in PBMCs and HaCat cells were determined by real-time quantitative PCR. Results: Our data indicated that serum IL-29 levels were significantly elevated in patients with psoriasis vulgaris when compared with atopic dermatitis patients and the control group. Moreover, Serum levels of IL-29 were closely associated with the severity of psoriasis vulgaris. Furthermore, IL-29 up-regulated the mRNA expression levels of IL-6, IL-17 and TNF-α in PBMCs from psoriasis vulgaris patients. In addition, IL-29 enhanced the IL-6 and IL-8 expression from the HaCat cells. Conclusion: This study provides the first observations on the association of IL-29 and psoriasis vulgaris and showed elevated IL-29 serum levels. The authors suggest that IL-29 may play a role in the pathogenesis of psoriasis vulgaris.

Fisetin Prevented Amyloid Formation of Insulin and Attenuated Fibril-induced Cytotoxicity.

Natural polyphenols are major constituents of plant foods and herbs. Numerous reports demonstrated that these compounds inhibited amyloid formation and destabilized the preformed amyloid fibrils. The present study, utilizing bovine insulin as a model peptide, examined the antiamyloidogenic effects of fisetin (3,7,3',4'-tetrahydroxyflavone). Fluorescent probes, transmission electron microscopy and hemolytic assay were utilized to determine the roles of fisetin on amyloidogenesis of insulin. The results demonstrated that fisetin dose-dependently inhibited amyloid formation of insulin. Moreover, fisetin disaggregated the preformed insulin fibrils and transformed the fibrils into non-amyloid structures. Hemolysis was observed when erythrocytes were co-incubated with insulin fibrils. Fisetin inhibited fibril-induced hemolysis in a dose-dependent manner. Hydrophobic interaction is suggested to be a key driving force in the anti-amyloidogenic and fibril-disaggregating effects of fisetin. The results of the present work suggest that fisetin is an effective anti-amyloidogenic compound and may serve as a lead structure for the design of novel drugs for the treatment of amyloid diseases.