Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học General Psychiatry cung cấp cho các bạn kiến thức về ngành y đề tài: Tumor necrosis factor alpha-dependent aggrecan cleavage and release of glycosaminoglycans in the meniscus is mediated by nitrous oxide-independent aggrecanase activity in vitro. | Available online http content 11 5 R141 Research article Tumor necrosis factor alpha-dependent aggrecan cleavage and release of glycosaminoglycans in the meniscus is mediated by nitrous oxide-independent aggrecanase activity in vitro Henning Voigt Angelika K Lemke Rolf Mentlein Michael Schunke and Bodo Kurz Open Access Institute of Anatomy Christian-Albrechts-University Kiel Olshausenstr. 40 Kiel 24098 Germany Corresponding author Bodo Kurz bkurz@ Received 16 Jun 2008 Revisions requested 13 Aug 2008 Revisions received 1 Sep 2009 Accepted 24 Sep 2009 Published 24 Sep 2009 Arthritis Research Therapy 2009 11 R141 doi ar2813 This article is online at http content 11 5 R141 2009 Voigt et al. licensee BioMed Central Ltd. This is an open access article distributed under the terms of the Creative Commons Attribution License http licenses by which permits unrestricted use distribution and reproduction in any medium provided the original work is properly cited. Abstract Introduction Little is known about factors that induce meniscus damage. Since joint inflammation appears to be a causative factor for meniscal destruction we investigated the influence of tumor necrosis factor TNFa on glycosaminoglycan GAG release and aggrecan cleavage in an in vitro model. Methods Meniscal explant disks 3 mm diameter X 1 mm thickness were isolated from 2-year-old cattle. After 3 days of TNFa-treatment GAG release DMMB assay biosynthetic activity sulfate incorporation nitric oxide NO production Griess assay gene expression of matrix-degrading enzymes quantitative RT-PCR zymography and immunostaining of the aggrecan fragment NITEGE were determined. Results TNFa induced release of GAG as well as production of NO in a dose-dependent manner while sulfate incorporation was decreased. TNFa increased matrix metalloproteinase MMP -3 and a disintegrin and metalloproteinase with thrombospondin motifs ADAMTS -4
