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Báo cáo y học: ": Colocalization of endogenous TNF with a functional intracellular splice form of human TNF receptor type 2."

Tuyển tập báo cáo các nghiên cứu khoa học quốc tế ngành y học dành cho các bạn tham khảo đề tài: Colocalization of endogenous TNF with a functional intracellular splice form of human TNF receptor type 2. | Journal of Inflammation BioMed Central Research Open Access Colocalization of endogenous TNF with a functional intracellular splice form of human TNF receptor type 2 Christoph Scherubl1 Wulf Schneider-Brachert2 Stephan Schutze3 Thomas Hehlgans1 and Daniela N Mannel 1 Address University of Regensburg Institute of Immunology 2Institute of Medical Microbiology and Hygiene D-93042 Regensburg and 3University Hospital of Schleswig-Holstein Campus Kiel Institute of Immunology D-24105 Kiel Germany Email Christoph Scherubl - christoph.scheruebl@klinik.uni-regensburg.de Wulf Schneider-Brachert - wulf.schneider@klinik.uni-regensburg.de Stephan Schutze - schuetze@immunologie.uni-kiel.de Thomas Hehlgans - thomas.hehlgans@klinik.uni-regensburg.de Daniela N Mannel - daniela.maennel@klinik.uni-regensburg.de Corresponding author Published 04 July 2005 Journal of Inflammation 2005 2 7 doi 10.1 186 1476-9255-2-7 Received 31 March 2005 Accepted 04 July 2005 This article is available from http www.journal-inflammation.cOm content 2 1 7 2005 Scherubl et al licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License http creativecommons.org licenses by 2.0 which permits unrestricted use distribution and reproduction in any medium provided the original work is properly cited. Abstract Background Tumor necrosis factor TNF is a pleiotropic cytokine involved in a broad spectrum of inflammatory and immune responses including proliferation differentiation and cell death. The biological effects of TNF are mediated via two cell surface TNF receptors p55TNFR TNFR1 CD120a and p75TNFR TNFR2 CD120b . Soluble forms of these two receptors consisting of the extracellular domains are proteolytically cleaved from the membrane and act as inhibitors. A novel p75TNFR isoform generated by the use of an additional transcriptional start site has been described and was termed hicp75TNFR. We focused on the characterization of this new .