Báo cáo y học: "Amino acid racemization reveals differential protein turnover in osteoarthritic articular and meniscal cartilages"

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: Amino acid racemization reveals differential protein turnover in osteoarthritic articular and meniscal cartilages. | Available online http content 11 2 R34 Research article Amino acid racemization reveals differential protein turnover in osteoarthritic articular and meniscal cartilages Thomas V Stabler1 Samuel S Byers2 Robert D Zura3 and Virginia Byers Kraus1 Open Access 1 Department of Medicine Duke University Medical Center Box 3416 Durham NC 27710 USA department of Dentistry Case Western Reserve University 10900 Euclid Avenue Cleveland OH 44104 USA department of Surgery Duke University Medical Center Box 3205 Durham NC 27710 USA Corresponding author Thomas V Stabler tvs@ Received 1 May 2008 Revisions requested 29 May 2008 Revisions received 24 Dec 2008 Accepted 6 Mar 2009 Published 6 Mar 2009 Arthritis Research Therapy 2009 11 R34 doi ar2639 This article is online at http content 11 2 R34 2009 Stabler 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 Certain amino acids within proteins have been reported to change from the L form to the D form over time. This process is known as racemization and is most likely to occur in long-lived low-turnover tissues such as normal cartilage. We hypothesized that diseased tissue as found in an osteoarthritic OA joint would have increased turnover reflected by a decrease in the racemized amino acid content. Methods Using high-performance liquid chromatography methods we quantified the L and D forms of amino acids reported to racemize in vivo on a biological timescale alanine aspartate Asp asparagine Asn glutamate glutamine isoleucine leucine Leu and serine Ser . Furthermore using a metabolically inactive control material tooth dentin and a control material with normal metabolism normal articular cartilage we .

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