Tuyển tập các báo cáo nghiên cứu về hóa học được đăng trên tạp chí sinh học quốc tế đề tài : Multiple functions of the von Willebrand Factor A domain in matrilins: secretion, assembly, and proteolysis | Journal of Orthopaedic Surgery and Research BioMed Central Research article Multiple functions of the von Willebrand Factor A domain in matrilins secretion assembly and proteolysis Yue Zhangt1 Zheng-ke Wangt2 Jun-ming Luo2 Katsuaki Kanbe3 and Qian Chen 2 Open Access Address division of Musculoskeletal Sciences Departments of Orthopaedics and Rehabilitation The Pennsylvania State University College of Medicine Hershey Pennsylvania USA 2Cell and Molecular Biology Laboratory Department of Orthopaedics The Warren Alpert Medical School of Brown University Rhode Island Hospital Providence Rhode Island USA and 3Department of Orthopaedic Surgery Tokyo Women s Medical University Daini Hospital Tokyo Japan Email Yue Zhang - yzhang1@ Zheng-ke Wang - zhengke_wang@ Jun-ming Luo - junming_luo@ Katsuaki Kanbe - kanbeor@ Qian Chen - Qian_Chen@ Corresponding author tEqual contributors Published 2 June 2008 Received 13 November 2007 Journal of Orthopaedic Surgery and Research 2008 3 21 doi l749-799X-3-21 Accepted 2 June 2008 This article is available from http content 3 1 21 2008 Zhang 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 The von Willebrand Factor A vWF A domain is one of the most widely distributed structural modules in cell-matrix adhesive molecules such as intergrins and extracellular matrix proteins. Mutations in the vWF A domain of matrilin-3 cause multiple epiphyseal dysplasia MED however the pathological mechanism remains to be determined. Previously we showed that the vWF A domain in matrilin-1 mediates formation of a filamentous matrix network through .
