Tuyển tập báo cáo các nghiên cứu khoa học quốc tế ngành y học dành cho các bạn tham khảo đề tài: Early NAC and DTT promote TGF-β1 monomer formation: demonstration of competitive binding. | Journal of Inflammation BioMed Central Research NAC and DTT promote TGF-P1 monomer formation demonstration of competitive binding Frank J Lichtenberger III Christine R Montague Melissa Hunter Gwyn Frambach and Clay B Marsh Open Access Address Department of Internal Medicine Division of Pulmonary and Critical Care Dorothy M. Davis Heart and Lung Research Institute The Ohio State University Columbus OH USA Email Frank J Lichtenberger-Lichtenberger-1@ Christine Montague - Roos-1@ Melissa Hunter - hunter- 4@ Gwyn Frambach - Frambach-1@ Clay B Marsh - Corresponding author Published II April 2006 Received 08 August 2005 Accepted 1 1 April 2006 Journal of Inflammation 2006 3 7 doi 1476-9255-3-7 This article is available from http content 3 1 7 2006 Lichtenberger 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 TGF-P plays an important role in the genesis and progression of pulmonary fibrosis. We sought to determine the role of mononuclear phagocytes in the activation of TGF-P and found that freshly isolated peripheral blood monocytes spontaneously released TGF-p. Stimulating these monocytes with GM-CSF or LPS but not MCSF augmented the activation of TGF-p. In human monocytes the free thiol compounds DTT and NAC decreased the activity of TGF-P without affecting TGF-P mRNA transcription. Both NAC and DTT lessened the biological activity of recombinant active TGF-p in a cell-free system. We found that NAC and DTT reduced dimeric active TGF-p from a 25 kDa protein to kDa inactive monomer. This conversion was reversed using the oxidizing agent diamide. Diamide also restored biological activity to NAC or .
