Print Email Facebook Twitter Synthesis of collagen by bovine chondrocytes cultured in alginate; posttranslational modifications and cell-matrix interaction Title Synthesis of collagen by bovine chondrocytes cultured in alginate; posttranslational modifications and cell-matrix interaction Author Beekman, B. Verzijl, N. Bank, R.A. Von Der Mark, K. TeKoppele, J.M. TNO Preventie en Gezondheid Publication year 1997 Abstract The extracellular matrix synthesized by articular chondrocytes cultured in alginate beads was investigated. Collagen levels increased sigmoidally with time and remained constant after 2 weeks of culture. The presence of cartilage-specific type II collagen was confirmed immunohistochemically. Predominantly type H collagen was present in the alginate bead, as reflected by the unique extent of lysyl hydroxylation, glycosylation, and pyridinoline crosslink formation measured. Collagen crosslinks, predominantly hydroxylysylpyridinoline (>93%), were observed after 7 to 11 days of culture and their formation was effectively blocked by β-aminopropionitrile (BAPN). Unexpectedly, BAPN treatment resulted in a 100% increase of collagen levels, without influencing cell proliferation and proteoglycan levels. In control cultures 90% of the synthesized collagen was retained in the cell-associated matrix, while in BAPN-treated cultures half of the collagen was found in the interterritorial matrix compartment further removed from the cells. This suggests that impaired crosslinking of collagen interferes with pericellular collagen deposition, causing upregulation of collagen synthesis by impaired cell-matrix interactions. Integrins are likely to be involved in this feedback inhibition by extracellular collagen since the cyclic RGD-containing peptide CGRGDSPC downregulated collagen synthesis by 37%. Chemicals/CAS: Alginates; alginic acid, 9005-32-7; Amino Acids; Aminopropionitrile, 151-18-8; arginyl-glycyl-aspartic acid, 99896-85-2; Collagen, 9007-34-5; DNA, 9007-49-2; Glucuronic Acid, 576-37-4; glycyl-arginyl-glycyl-aspartyl-seryl-proline, 91037-75-1; Hexuronic Acids; Oligopeptides; Proteoglycans; pyridinoline, 63800-01-1 Subject BiologyBiomedical ResearchAlginate beadsArticular chondrocyteCollagenCollagen crosslinksPosttranslational modificationProteoglycan3 aminopropionitrilealginic acidcollagenintegrinpyridinolineanimal cellbinding affinitycartilage cellcell interactioncell proliferationcollagen synthesisnonhumanpriority journalprotein cross linkingprotein processingAlginatesAmino Acid SequenceAmino AcidsAminopropionitrileAnimalsCartilage, ArticularCattleCell DivisionCells, CulturedCollagenDNAExtracellular MatrixGlucuronic AcidGlycosylationHexuronic AcidsKineticsOligopeptidesProtein Processing, Post-TranslationalProteoglycansTime FactorsAnimaliaBos taurusBovinae To reference this document use: http://resolver.tudelft.nl/uuid:738daaf5-854e-4ce9-b7ce-4bff632e1e2f DOI https://doi.org/10.1006/excr.1997.3771 TNO identifier 234127 ISSN 0014-4827 Source Experimental Cell Research, 237 (1), 135-141 Document type article Files To receive the publication files, please send an e-mail request to TNO Library.