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dc.contributor.authorKielty, Cen
dc.contributor.authorKwan, Aen
dc.contributor.authorHolmes, Den
dc.contributor.authorSchor, Seth Len
dc.contributor.authorGrant, Men
dc.date.accessioned2010-12-02T17:09:00Z
dc.date.available2010-12-02T17:09:00Z
dc.date.issued1985-04-15
dc.identifier.citationType X collagen, a product of hypertrophic chondrocytes. 1985, 227 (2):545-54 Biochem Jen
dc.identifier.issn0264-6021
dc.identifier.pmid4004779
dc.identifier.urihttp://hdl.handle.net/10541/116973
dc.description.abstractThe synthesis of collagen types IX and X by explants of chick-embryo cartilages was investigated. When sternal cartilage labelled for 24h with [3H]proline was extracted with 4M-guanidinium chloride, up to 20% of the 3H-labelled collagen laid down in the tissue could be accounted for by the low-Mr collagenous polypeptides (H and J chains) of type IX collagen; but no type X collagen could be detected. Explants of tibiotarsal and femoral cartilages were found to synthesize type IX collagen mainly in zones 1 and 2 of chondrocyte proliferation and elongation, whereas type X collagen was shown to be a product of the hypertrophic chondrocytes in zone 3. Pulse-chase experiments with tibiotarsal (zone-3) explants demonstrated a time-dependent conversion of type X procollagen into a smaller species whose polypeptides were of Mr 49 000. The processed chains [alpha 1(X) chains] were shown by peptide mapping techniques to share a common identity with the pro alpha 1(X) chains of Mr 59 000. No evidence for processing of type IX collagen was obtained in analogous pulse-chase experiments with sternal tissue. When chondrocytes from tibiotarsal cartilage (zone 3) were cultured on plastic under standard conditions for 4-10 weeks they released large amounts of type X procollagen into the medium. However, 2M-MgCl2 extracts of the cell layer were found to contain mainly the processed collagen comprising alpha 1(X) chains. The native type X procollagen purified from culture medium was shown by rotary shadowing to occur as a short rod-like molecule 148 nm in length with a terminal globular extension, whereas the processed species comprising alpha 1(X) chains of Mr 49 000 was detected by electron microscopy as the linear 148 nm segment.
dc.language.isoenen
dc.subject.meshAnimals
dc.subject.meshCartilage
dc.subject.meshChick Embryo
dc.subject.meshCollagen
dc.subject.meshElectrophoresis, Polyacrylamide Gel
dc.subject.meshHypertrophy
dc.subject.meshMicroscopy, Electron
dc.subject.meshOrgan Culture Techniques
dc.subject.meshPeptide Fragments
dc.subject.meshProcollagen
dc.subject.meshProline
dc.titleType X collagen, a product of hypertrophic chondrocytes.en
dc.typeArticleen
dc.contributor.departmentDepartment of Biochemistry and Depsrtment of Medical Biophysics, Medical School, University of Manchester, Oxford Road, Manchester M13 9PLen
dc.identifier.journalBiochemical Journalen
html.description.abstractThe synthesis of collagen types IX and X by explants of chick-embryo cartilages was investigated. When sternal cartilage labelled for 24h with [3H]proline was extracted with 4M-guanidinium chloride, up to 20% of the 3H-labelled collagen laid down in the tissue could be accounted for by the low-Mr collagenous polypeptides (H and J chains) of type IX collagen; but no type X collagen could be detected. Explants of tibiotarsal and femoral cartilages were found to synthesize type IX collagen mainly in zones 1 and 2 of chondrocyte proliferation and elongation, whereas type X collagen was shown to be a product of the hypertrophic chondrocytes in zone 3. Pulse-chase experiments with tibiotarsal (zone-3) explants demonstrated a time-dependent conversion of type X procollagen into a smaller species whose polypeptides were of Mr 49 000. The processed chains [alpha 1(X) chains] were shown by peptide mapping techniques to share a common identity with the pro alpha 1(X) chains of Mr 59 000. No evidence for processing of type IX collagen was obtained in analogous pulse-chase experiments with sternal tissue. When chondrocytes from tibiotarsal cartilage (zone 3) were cultured on plastic under standard conditions for 4-10 weeks they released large amounts of type X procollagen into the medium. However, 2M-MgCl2 extracts of the cell layer were found to contain mainly the processed collagen comprising alpha 1(X) chains. The native type X procollagen purified from culture medium was shown by rotary shadowing to occur as a short rod-like molecule 148 nm in length with a terminal globular extension, whereas the processed species comprising alpha 1(X) chains of Mr 49 000 was detected by electron microscopy as the linear 148 nm segment.


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