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      Is Open Access

      Experimental study of tissue-engineered cartilage allograft with RNAi chondrocytes in vivo

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          Abstract

          Purpose

          To determine the effects of RNA interference (RNAi) on chondrocyte proliferation, function, and immunological rejection after allogenic tissue-engineered cartilage transplantation within bone matrix gelatin scaffolds.

          Methods

          Seven million rat normal and RNAi chondrocytes were harvested and separately composited with fibrin glue to make the cell suspension, and then transplanted subcutaneously into the back of Sprague Dawley rats after being cultured for 10 days in vitro. Untransplanted animals served as the control group. The allograft and immunological response were examined at 1, 2, 4, 8, and 12 months postoperatively with hematoxylin and eosin histochemical staining, immunohistochemical staining (aggrecan, type II collagen, class I and II major histocompatibility complex), and flow cytometry for peripheral blood cluster of differentiation 4 + (CD4 +) and CD8 + T-cells.

          Results

          There was no infection or death in the rats except one, which died in the first week. Compared to the control group, the RNAi group had fewer eukomonocytes infiltrated, which were only distributed around the graft. The ratio of CD4 +/CD8 + T-cells in the RNAi group was significantly lower than the normal one ( P<0.05). There were many more positively stained chondrocytes and positively stained areas around the cells in the RNAi group, which were not found in the control group.

          Conclusion

          The aggrecanase-1 and aggrecanase-2 RNAi for chondrocytes decreased the immunological rejection effect.

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          Most cited references 9

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          Review: tissue engineering for regeneration of articular cartilage.

          Joint pain due to cartilage degeneration is a serious problem, affecting people of all ages. Although many techniques, often surgical, are currently employed to treat this affliction, none have had complete success. Recent advances in biology and materials science have pushed tissue engineering to the forefront of new cartilage repair techniques. This review seeks to condense information for the biomaterialist interested in developing materials for this application. Articular cartilage anatomy, types of injury, and current repair methods are explained. The need for biomaterials, current commonly used materials for tissue-engineered cartilage, and considerations in scale-up of cell-biomaterial constructs are summarized.
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            The structure of aggrecan fragments in human synovial fluid. Evidence that aggrecanase mediates cartilage degradation in inflammatory joint disease, joint injury, and osteoarthritis.

            To determine the proteolytic fragmentation patterns and N-terminal sequence of aggrecan fragments in human synovial fluid from patients with inflammatory arthritides, joint injury, or osteoarthritis (OA). Knee synovial fluid was obtained from patients with joint injury, OA, acute pyrophosphate arthritis (pseudogout), reactive arthritis, psoriatic arthritis, or juvenile rheumatoid arthritis. Chondroitin sulfate-substituted aggrecan fragments present in the fluid were purified by cesium chloride gradient centrifugation and enzymatically deglycosylated. Core protein species were determined by N-terminal analysis and by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) with electroblotting and detection with monoclonal antibody 3B3. Samples from patients with joint injury, OA, and inflammatory joint disease all showed a similar 3-band pattern, with core sizes of approximately 200 kd, 170 kd, and 135 kd. In all samples, diffuse immunoreactive products were also seen, with an apparent size of > 250 kd. N-terminal analysis of core preparations of all samples showed a consistent single predominant sequence, beginning at alanine 374 of the human aggrecan core protein. The aggrecan fragments present in joint fluids from patients with various inflammatory arthritides, joint injury, or OA result from a predominant cleavage of the human aggrecan core protein at the glutamate 373-alanine 374 bond within the interglobular domain, between the G1 and G2 domains. The consistent pattern of fragments seen on SDS-PAGE and the single predominant N-terminal sequence suggest a common degradative mechanism of aggrecan in these different joint conditions. The identity of the proteolytic agent (aggrecanase), however, remains unknown. These results appear to have important implications with regard to the development of therapies to protect cartilage from degradation in patients with joint disease.
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              Immunogenicity of allograft articular cartilage.

               H F Langer,  A Gross (1974)
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                Author and article information

                Journal
                Ther Clin Risk Manag
                Ther Clin Risk Manag
                Therapeutics and Clinical Risk Management
                Therapeutics and Clinical Risk Management
                Dove Medical Press
                1176-6336
                1178-203X
                2014
                08 May 2014
                : 10
                : 335-340
                Affiliations
                [1 ]Department of Otolaryngology – Head and Neck Surgery, The Second Hospital, Xi’an Jiaotong University, Xi’an, People’s Republic of China
                [2 ]Department of Dermatology, The Second Hospital, Xi’an Jiaotong University, Xi’an, People’s Republic of China
                [3 ]Department of Orthopedics, The Second Hospital, Xi’an Jiaotong University, Xi’an, People’s Republic of China
                [4 ]Department of Plastic and Burns Surgery, The First Hospital, Xi’an Jiaotong University, Xi’an, People’s Republic of China
                [5 ]Department of Oral and Maxillofacial Plastic Surgery, The Stomatological Hospital, Xi’an Jiaotong University, Xi’an, People’s Republic of China
                Author notes
                Correspondence: Baojun Wu; Min Xu, Department of Otolaryngology – Head and Neck Surgery, The Second Hospital, Xi’an Jiaotong University, Xi Wu Road, Xi’an 710004, People’s Republic of China, Email wubaojun_bone@ 123456163.com ; ent551205@ 123456163.com
                Article
                tcrm-10-335
                10.2147/TCRM.S51518
                4020888
                © 2014 Wang et al. This work is published by Dove Medical Press Limited, and licensed under Creative Commons Attribution – Non Commercial (unported, v3.0) License

                The full terms of the License are available at http://creativecommons.org/licenses/by-nc/3.0/. Non-commercial uses of the work are permitted without any further permission from Dove Medical Press Limited, provided the work is properly attributed.

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                Original Research

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