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      Radiocarbon dating reveals minimal collagen turnover in both healthy and osteoarthritic human cartilage.

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          Abstract

          The poor regenerative capacity of articular cartilage presents a major clinical challenge and may relate to a limited turnover of the cartilage collagen matrix. However, the collagen turnover rate during life is not clear, and it is debated whether osteoarthritis (OA) can influence it. Using the carbon-14 ((14)C) bomb-pulse method, life-long replacement rates of collagen were measured in tibial plateau cartilage from 23 persons born between 1935 and1997 (15 and 8 persons with OA and healthy cartilage, respectively). The (14)C levels observed in cartilage collagen showed that, virtually, no replacement of the collagen matrix happened after skeletal maturity and that neither OA nor tissue damage, per se, influenced collagen turnover. Regional differences in (14)C content across the joint surface showed that cartilage collagen located centrally on the joint surface is formed several years earlier than collagen located peripherally. The collagen matrix of human articular cartilage is an essentially permanent structure that has no significant turnover in adults, even with the occurrence of disease.

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          Collagen turnover in the adult femoral mid-shaft: modeled from anthropogenic radiocarbon tracer measurements.

          Robert Hedges, John Clement, C Thomas … (2007)
          We have measured the (14)C content of human femoral mid-shaft collagen to determine the dynamics of adult collagen turnover, using the sudden doubling and subsequent slow relaxation of global atmospheric (14)C content due to nuclear bomb testing in the 1960s and 1970s as a tracer. (14)C measurements were made on bone collagen from 67 individuals of both sexes who died in Australia in 1990-1993, spanning a range of ages at death from 40 to 97, and these measurements were compared with values predicted by an age-dependent turnover model. We found that the dataset could constrain models of collagen turnover, with the following outcomes: 1) Collagen turnover rate of females decreases, on average, from 4%/yr to 3%/yr from 20 to 80 years. Male collagen turnover rates average 1.5-3%/yr over the same period. 2) For both sexes the collagen turnover rate during adolescent growth is much higher (5-15%/yr at age 10-15 years), with males having a significantly higher turnover rate than have females, by up to a factor of 2. 3) Much of the variation in residual bomb (14)C in a person's bone can be attributed to individual variation in turnover rate, but of no more than about 30% of the average values for adults. 4) Human femoral bone collagen isotopically reflects an individual's diet over a much longer period of time than 10 years, including a substantial portion of collagen synthesised during adolescence.
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            Effect of collagen turnover on the accumulation of advanced glycation end products.

            Nicole Verzijl, Jeroen DeGroot, Suzanne R Thorpe … (2000)
            Collagen molecules in articular cartilage have an exceptionally long lifetime, which makes them susceptible to the accumulation of advanced glycation end products (AGEs). In fact, in comparison to other collagen-rich tissues, articular cartilage contains relatively high amounts of the AGE pentosidine. To test the hypothesis that this higher AGE accumulation is primarily the result of the slow turnover of cartilage collagen, AGE levels in cartilage and skin collagen were compared with the degree of racemization of aspartic acid (% d-Asp, a measure of the residence time of a protein). AGE (N(epsilon)-(carboxymethyl)lysine, N(epsilon)-(carboxyethyl)lysine, and pentosidine) and % d-Asp concentrations increased linearly with age in both cartilage and skin collagen (p < 0.0001). The rate of increase in AGEs was greater in cartilage collagen than in skin collagen (p < 0.0001). % d-Asp was also higher in cartilage collagen than in skin collagen (p < 0.0001), indicating that cartilage collagen has a longer residence time in the tissue, and thus a slower turnover, than skin collagen. In both types of collagen, AGE concentrations increased linearly with % d-Asp (p < 0.0005). Interestingly, the slopes of the curves of AGEs versus % d-Asp, i.e. the rates of accumulation of AGEs corrected for turnover, were identical for cartilage and skin collagen. The present study thus provides the first experimental evidence that protein turnover is a major determinant in AGE accumulation in different collagen types. From the age-related increases in % d-Asp the half-life of cartilage collagen was calculated to be 117 years and that of skin collagen 15 years, thereby providing the first reasonable estimates of the half-lives of these collagens.
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              Cell-based tissue engineering strategies used in the clinical repair of articular cartilage.

              Brian Huang, Jerry Hu, Kyriacos Athanasiou (2016)
              One of the most important issues facing cartilage tissue engineering is the inability to move technologies into the clinic. Despite the multitude of current research in the field, it is known that 90% of new drugs that advance past animal studies fail clinical trials. The objective of this review is to provide readers with an understanding of the scientific details of tissue engineered cartilage products that have demonstrated a certain level of efficacy in humans, so that newer technologies may be developed upon this foundation. Compared to existing treatments, such as microfracture or autologous chondrocyte implantation, a tissue engineered product can potentially provide more consistent clinical results in forming hyaline repair tissue and in filling the entirety of the defect. The various tissue engineering strategies (e.g., cell expansion, scaffold material, media formulations, biomimetic stimuli, etc.) used in forming these products, as collected from published literature, company websites, and relevant patents, are critically discussed. The authors note that many details about these products remain proprietary, not all information is made public, and that advancements to the products are continuously made. Nevertheless, by understanding the design and production processes of these emerging technologies, one can gain tremendous insight into how to best use them and also how to design the next generation of tissue engineered cartilage products.
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                Author and article information

                Journal
                Journal ID (iso-abbrev): Sci Transl Med
                Title: Science translational medicine
                Publisher: American Association for the Advancement of Science (AAAS)
                ISSN (Electronic): 1946-6242
                ISSN (Print): 1946-6234
                Publication date (Electronic): Jul 06 2016
                Volume: 8
                Issue: 346
                Affiliations
                [1 ] Institute of Sports Medicine, Department of Orthopaedic Surgery M, Bispebjerg Hospital, Center for Healthy Aging, Faculty of Health and Medical Sciences, University of Copenhagen, 2400 Copenhagen NV, Denmark. Department of Biomedical Sciences, Center for Healthy Aging, Faculty of Health and Medical Sciences, University of Copenhagen, 2200 Copenhagen N, Denmark.
                [2 ] Institute of Sports Medicine, Department of Orthopaedic Surgery M, Bispebjerg Hospital, Center for Healthy Aging, Faculty of Health and Medical Sciences, University of Copenhagen, 2400 Copenhagen NV, Denmark.
                [3 ] AMS C Dating Centre, Department of Physics and Astronomy, Aarhus University, 8000 Aarhus C, Denmark.
                [4 ] Section for Sports Traumatology M51, Department of Orthopaedic Surgery M, Bispebjerg-Frederiksberg Hospital, 2400 Copenhagen NV, Denmark.
                [5 ] Musculoskeletal Tumor Section, Department of Orthopaedic Surgery, Rigshospitalet, Faculty of Health and Medical Sciences, University of Copenhagen, 2100 Copenhagen O, Denmark.
                [6 ] Institute of Sports Medicine, Department of Orthopaedic Surgery M, Bispebjerg Hospital, Center for Healthy Aging, Faculty of Health and Medical Sciences, University of Copenhagen, 2400 Copenhagen NV, Denmark. michaelkjaer@sund.ku.dk.
                Article
                Publisher Item ID: 8/346/346ra90
                DOI: 10.1126/scitranslmed.aad8335
                PubMed ID: 27384346
                SO-VID: 4b538029-df83-45da-ac9f-ae59ff598c8e
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