Factors influencing proteoglycan size in rachitic-chick growth cartilage.
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ABSTRACT:
SUBMITTER: Roughley P
PROVIDER: S-EPMC1161266 | biostudies-other | 1980 Jan
REPOSITORIES: biostudies-other
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Project description:1. Proteoglycan was isolated from growth cartilage of normal and rachitic chicks. 2. The proteoglycan from normal cartilage showed differences in chemical composition and physical properties from a comparable fraction isolated from bovine nasal cartilage. 3. The proteoglycan from rachitic-chick cartilage was of smaller size than tis normal counterpart, though of similar average chemical composition. 4. Differences between proteoglycan from normal and rachitic cartilages can be explained in terms of limited proteolytic cleavage.
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Project description:Teeth are mineralized organs composed of three unique hard tissues, enamel, dentin, and cementum, and supported by the surrounding alveolar bone. Although odontogenesis differs from osteogenesis in several respects, tooth mineralization is susceptible to similar developmental failures as bone. Here we discuss conditions fitting under the umbrella of rickets, which traditionally referred to skeletal disease associated with vitamin D deficiency but has been more recently expanded to include newly identified factors involved in endocrine regulation of vitamin D, phosphate, and calcium, including phosphate-regulating endopeptidase homolog, X-linked, fibroblast growth factor 23, and dentin matrix protein 1. Systemic mineral metabolism intersects with local regulation of mineralization, and factors including tissue nonspecific alkaline phosphatase are necessary for proper mineralization, where rickets can result from loss of activity of tissue nonspecific alkaline phosphatase. Individuals suffering from rickets often bear the additional burden of a defective dentition, and transgenic mouse models have aided in understanding the nature and mechanisms involved in tooth defects, which may or may not parallel rachitic bone defects. This report reviews dental effects of the range of rachitic disorders, including discussion of etiologies of hereditary forms of rickets, a survey of resulting bone and tooth mineralization disorders, and a discussion of mechanisms, known and hypothesized, involved in the observed dental pathologies. Descriptions of human pathology are augmented by analysis of transgenic mouse models, and new interpretations are brought to bear on questions of how teeth are affected under conditions of rickets. In short, the rachitic tooth will be revealed.
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Project description:BackgroundAlthough proteoglycan (PG) is one of the major components of cartilage matrices, its biological function is not fully elucidated.MethodsThe objectives of this study were to investigate the proliferation and differentiation of chondrocytes embedded in atelocollagen gel with exogenous cartilage PG (PG-atelocollagen gel) in vitro, and also to evaluate the repair of cartilage defects by PG-atelocollagen gel in vivo. In the in vitro study, rabbit chondrocytes were cultured in the PG-atelocollagen gel. Cell proliferation and mRNA expression levels were measured, and gels were histologically evaluated. In the in vivo study, cultured PG-atelocollagen gel containing chondrocytes were transplanted into full-thickness articular cartilage defects in rabbit knees, and evaluated macroscopically and histologically.ResultsFor the in vitro study, chondrocyte proliferation in 5.0 mg/ml PG-atelocollagen gel was enhanced, and the gene expression of Col2a1 and Aggrecan were decreased. In contrast, chondrocyte proliferation in 0.1 and 1.0 mg/ml PG-atelocollagen gel was not enhanced. The gene expression of Aggrecan in 0.1 and 1.0 mg/ml PG-atelocollagen gel was increased. For the in vivo study, the histological average total score of the 0.1 mg/ml PG-atelocollagen gel was significantly better than that of the group without PG.ConclusionsAlthough the appropriate concentration of PG has not been defined, this study suggests the efficacy of PG for cartilage repair.
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Project description:The hydrodynamic frictional resistance to water flow exerted by articular cartilage proteoglycan is shown to be similar to that of proteoglycan isolated from Swarm rat chondrosarcoma, and independent of the state of aggregation of the proteoglycan. Frictional resistance is dependent, however, on the chain segments of the constituent chondroitin-sulphate and keratan-sulphate chains of the proteoglycan. Frictional resistance offered by chondroitin sulphate was independent of pH over the range 3.2-8.7. This confirms previous studies, associated with varying ionic strength and chemical modification of ionic groups of chondroitin sulphate, which showed that the frictional resistance offered by this molecule is independent of electrostatic factors. Water-structure-breaking and hydrogen-bond-breaking solvents were also without major effects on the flow resistance offered by chondroitin sulphate. An overall secondary structure of chondroitin sulphate was not evident, as it showed no significant difference to dextran in terms of its temperature dependence of relative viscosity. Local regions of rigid secondary structure, as manifested through inter-residue hydrogen bonding between sugar residues, is likely to control flow resistance as periodate-oxidized chondroitin sulphate and periodate-oxidized and reduced preparations showed a significant decrease in their frictional resistance to water.
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Project description:BackgroundRheumatoid arthritis (RA) is an autoimmune disease of the synovial joints. The autoimmune character of RA is underscored by prominent production of autoantibodies such as those against IgG (rheumatoid factor), and a broad array of joint tissue-specific and other endogenous citrullinated proteins. Anti-citrullinated protein antibodies (ACPA) can be detected in the sera and synovial fluids of RA patients and ACPA seropositivity is one of the diagnostic criteria of RA. Studies have demonstrated that RA T cells respond to citrullinated peptides (epitopes) of proteoglycan (PG) aggrecan, which is one of the most abundant macromolecules of articular cartilage. However, it is not known if the PG molecule is citrullinated in vivo in human cartilage, and if so, whether citrulline-containing neoepitopes of PG (CitPG) can contribute to autoimmunity in RA.MethodsCitPG was detected in human cartilage extracts using ACPA+ RA sera in dot blot and Western blot. Citrullination status of in vitro citrullinated recombinant G1 domain of human PG (rhG1) was confirmed by antibody-based and chemical methods, and potential sites of citrullination in rhG1 were explored by molecular modeling. CitPG-specific serum autoantibodies were quantified by enzyme-linked immunosorbent assays, and CitPG was localized in osteoarthritic (OA) and RA cartilage using immunohistochemistry.FindingsSera from ACPA+ RA patients reacted with PG purified from normal human cartilage specimens. PG fragments (mainly those containing the G1 domain) from OA or RA cartilage extracts were recognized by ACPA+ sera but not by serum from ACPA- individuals. ACPA+ sera also reacted with in vitro citrullinated rhG1 and G3 domain-containing fragment(s) of PG. Molecular modeling suggested multiple sites of potential citrullination within the G1 domain. The immunohistochemical localization of CitPG was different in OA and RA cartilage.ConclusionsCitPG is a new member of citrullinated proteins identified in human joints. CitPG could be found in both normal and diseased cartilage specimens. Antibodies against CitPG may trigger or augment arthritis by forming immune complexes with this autoantigen in the joints of ACPA+ RA patients.
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