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Amino acid racemization reveals differential protein turnover in osteoarthritic articular and meniscal cartilages.

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Date
2009
Authors
Stabler, Thomas V
Byers, Samuel S
Zura, Robert D
Kraus, Virginia Byers
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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 developed an age adjustment in order to make inferences about the state of protein turnover in cartilage and meniscus. RESULTS: In the metabolically inactive control material (n = 25, ages 13 to 80 years) and the normal metabolizing control material (n = 19, ages 17 to 83 years), only Asp + Asn (Asx), Ser, and Leu showed a significant change (increase) in racemization with age (P < 0.01). The age-adjusted proportions of racemized to total amino acid (D/D+L expressed as a percentage of the control material) for Asx, Ser, and Leu when compared with the normal articular cartilage control were 97%, 74%, and 73% in OA meniscal cartilage and 97%, 70%, and 78% in OA articular cartilage. We also observed lower amino acid content in OA articular and meniscal cartilages compared with normal articular cartilage as well as a loss of total amino acids with age in the OA meniscal but not the OA articular cartilage. CONCLUSIONS: These data demonstrate comparable anabolic responses for non-lesioned OA articular cartilage and OA meniscal cartilage but an excess of catabolism over anabolism for the meniscal cartilage.
Type
Journal article
Subject
Adult
Age Factors
Aged
Aged, 80 and over
Amino Acids
Cartilage, Articular
Chromatography, High Pressure Liquid
Dentin
Humans
Isomerism
Menisci, Tibial
Middle Aged
Osteoarthritis, Knee
Permalink
https://hdl.handle.net/10161/10861
Published Version (Please cite this version)
10.1186/ar2639
Publication Info
Stabler, Thomas V; Byers, Samuel S; Zura, Robert D; & Kraus, Virginia Byers (2009). Amino acid racemization reveals differential protein turnover in osteoarthritic articular and meniscal cartilages. Arthritis Res Ther, 11(2). pp. R34. 10.1186/ar2639. Retrieved from https://hdl.handle.net/10161/10861.
This is constructed from limited available data and may be imprecise. To cite this article, please review & use the official citation provided by the journal.
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Scholars@Duke

Kraus

Virginia Byers Kraus

Professor of Medicine
My special area of expertise is as a clinician scientist investigating osteoarthritis. Osteoarthritis is the most common form of joint disease in man and its incidence increases with age. It is a problem of increasing concern to the medical community due to the increasing longevity of the population. Trained as a molecular biologist and a Rheumatologist, I endeavor to study this disease from bedside to bench. The work in this laboratory focuses on osteoarthritis and deals w

Robert Douglas Zura

Associate Professor of Orthopaedic Surgery
This author no longer has a Scholars@Duke profile, so the information shown here reflects their Duke status at the time this item was deposited.
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