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Cross-linking of collagen. Location of pyridinoline in bovine articular cartilage at two sites of the molecule
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Zeitschriftentitel: | Biochemical Journal |
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Personen und Körperschaften: | , |
In: | Biochemical Journal, 215, 1983, 1, S. 175-182 |
Format: | E-Article |
Sprache: | Englisch |
veröffentlicht: |
Portland Press Ltd.
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Schlagwörter: |
author_facet |
Robins, S P Duncan, A Robins, S P Duncan, A |
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author |
Robins, S P Duncan, A |
spellingShingle |
Robins, S P Duncan, A Biochemical Journal Cross-linking of collagen. Location of pyridinoline in bovine articular cartilage at two sites of the molecule Cell Biology Molecular Biology Biochemistry |
author_sort |
robins, s p |
spelling |
Robins, S P Duncan, A 0264-6021 Portland Press Ltd. Cell Biology Molecular Biology Biochemistry http://dx.doi.org/10.1042/bj2150175 <jats:p>The location of pyridinoline in 18-month-old bovine articular cartilage was investigated by fractionation of CNBr-derived peptides by ion-exchange chromatography and gel filtration. Two peptides, PCP1 and PCP2, were isolated and were shown to contain stoichiometric amounts of pyridinoline. From its amino acid composition and sequence studies, peptide PCP1 was shown to comprise two C-terminal non-helical chains (CB14) linked through pyridinoline to the alpha 1(II)-CB12 portion of the helix. The CB14 chains appeared to be labile at their C-terminal ends, resulting in lower-than-expected amounts of homoserine, and only the N-terminal portion of the peptide was sequenced. Similar studies of peptide PCP2 showed that it contained two N-terminal non-helical chains (CB4) linked to the alpha 1(II)-CB9,7 portion of the helix. The isolated peptides therefore confirmed the function of pyridinoline in stabilizing the 4D stagger of adjacent molecules. The possibility that the cross-link could act both as an intra- and an inter-microfibrillar cross-link was considered. A mechanism of formation of pyridinoline was postulated that, together with other evidence, appears to support the view that, in cartilage, pyridinoline acts primarily as an intramicrofibrillar cross-link and does not contribute to increased stability during maturation through lateral aggregation and bonding of filaments.</jats:p> Cross-linking of collagen. Location of pyridinoline in bovine articular cartilage at two sites of the molecule Biochemical Journal |
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10.1042/bj2150175 |
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Portland Press Ltd., 1983 |
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Portland Press Ltd., 1983 |
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1983 |
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Portland Press Ltd. |
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Biochemical Journal |
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49 |
title |
Cross-linking of collagen. Location of pyridinoline in bovine articular cartilage at two sites of the molecule |
title_unstemmed |
Cross-linking of collagen. Location of pyridinoline in bovine articular cartilage at two sites of the molecule |
title_full |
Cross-linking of collagen. Location of pyridinoline in bovine articular cartilage at two sites of the molecule |
title_fullStr |
Cross-linking of collagen. Location of pyridinoline in bovine articular cartilage at two sites of the molecule |
title_full_unstemmed |
Cross-linking of collagen. Location of pyridinoline in bovine articular cartilage at two sites of the molecule |
title_short |
Cross-linking of collagen. Location of pyridinoline in bovine articular cartilage at two sites of the molecule |
title_sort |
cross-linking of collagen. location of pyridinoline in bovine articular cartilage at two sites of the molecule |
topic |
Cell Biology Molecular Biology Biochemistry |
url |
http://dx.doi.org/10.1042/bj2150175 |
publishDate |
1983 |
physical |
175-182 |
description |
<jats:p>The location of pyridinoline in 18-month-old bovine articular cartilage was investigated by fractionation of CNBr-derived peptides by ion-exchange chromatography and gel filtration. Two peptides, PCP1 and PCP2, were isolated and were shown to contain stoichiometric amounts of pyridinoline. From its amino acid composition and sequence studies, peptide PCP1 was shown to comprise two C-terminal non-helical chains (CB14) linked through pyridinoline to the alpha 1(II)-CB12 portion of the helix. The CB14 chains appeared to be labile at their C-terminal ends, resulting in lower-than-expected amounts of homoserine, and only the N-terminal portion of the peptide was sequenced. Similar studies of peptide PCP2 showed that it contained two N-terminal non-helical chains (CB4) linked to the alpha 1(II)-CB9,7 portion of the helix. The isolated peptides therefore confirmed the function of pyridinoline in stabilizing the 4D stagger of adjacent molecules. The possibility that the cross-link could act both as an intra- and an inter-microfibrillar cross-link was considered. A mechanism of formation of pyridinoline was postulated that, together with other evidence, appears to support the view that, in cartilage, pyridinoline acts primarily as an intramicrofibrillar cross-link and does not contribute to increased stability during maturation through lateral aggregation and bonding of filaments.</jats:p> |
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author | Robins, S P, Duncan, A |
author_facet | Robins, S P, Duncan, A, Robins, S P, Duncan, A |
author_sort | robins, s p |
container_issue | 1 |
container_start_page | 175 |
container_title | Biochemical Journal |
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description | <jats:p>The location of pyridinoline in 18-month-old bovine articular cartilage was investigated by fractionation of CNBr-derived peptides by ion-exchange chromatography and gel filtration. Two peptides, PCP1 and PCP2, were isolated and were shown to contain stoichiometric amounts of pyridinoline. From its amino acid composition and sequence studies, peptide PCP1 was shown to comprise two C-terminal non-helical chains (CB14) linked through pyridinoline to the alpha 1(II)-CB12 portion of the helix. The CB14 chains appeared to be labile at their C-terminal ends, resulting in lower-than-expected amounts of homoserine, and only the N-terminal portion of the peptide was sequenced. Similar studies of peptide PCP2 showed that it contained two N-terminal non-helical chains (CB4) linked to the alpha 1(II)-CB9,7 portion of the helix. The isolated peptides therefore confirmed the function of pyridinoline in stabilizing the 4D stagger of adjacent molecules. The possibility that the cross-link could act both as an intra- and an inter-microfibrillar cross-link was considered. A mechanism of formation of pyridinoline was postulated that, together with other evidence, appears to support the view that, in cartilage, pyridinoline acts primarily as an intramicrofibrillar cross-link and does not contribute to increased stability during maturation through lateral aggregation and bonding of filaments.</jats:p> |
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imprint | Portland Press Ltd., 1983 |
imprint_str_mv | Portland Press Ltd., 1983 |
institution | DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1 |
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source_id | 49 |
spelling | Robins, S P Duncan, A 0264-6021 Portland Press Ltd. Cell Biology Molecular Biology Biochemistry http://dx.doi.org/10.1042/bj2150175 <jats:p>The location of pyridinoline in 18-month-old bovine articular cartilage was investigated by fractionation of CNBr-derived peptides by ion-exchange chromatography and gel filtration. Two peptides, PCP1 and PCP2, were isolated and were shown to contain stoichiometric amounts of pyridinoline. From its amino acid composition and sequence studies, peptide PCP1 was shown to comprise two C-terminal non-helical chains (CB14) linked through pyridinoline to the alpha 1(II)-CB12 portion of the helix. The CB14 chains appeared to be labile at their C-terminal ends, resulting in lower-than-expected amounts of homoserine, and only the N-terminal portion of the peptide was sequenced. Similar studies of peptide PCP2 showed that it contained two N-terminal non-helical chains (CB4) linked to the alpha 1(II)-CB9,7 portion of the helix. The isolated peptides therefore confirmed the function of pyridinoline in stabilizing the 4D stagger of adjacent molecules. The possibility that the cross-link could act both as an intra- and an inter-microfibrillar cross-link was considered. A mechanism of formation of pyridinoline was postulated that, together with other evidence, appears to support the view that, in cartilage, pyridinoline acts primarily as an intramicrofibrillar cross-link and does not contribute to increased stability during maturation through lateral aggregation and bonding of filaments.</jats:p> Cross-linking of collagen. Location of pyridinoline in bovine articular cartilage at two sites of the molecule Biochemical Journal |
spellingShingle | Robins, S P, Duncan, A, Biochemical Journal, Cross-linking of collagen. Location of pyridinoline in bovine articular cartilage at two sites of the molecule, Cell Biology, Molecular Biology, Biochemistry |
title | Cross-linking of collagen. Location of pyridinoline in bovine articular cartilage at two sites of the molecule |
title_full | Cross-linking of collagen. Location of pyridinoline in bovine articular cartilage at two sites of the molecule |
title_fullStr | Cross-linking of collagen. Location of pyridinoline in bovine articular cartilage at two sites of the molecule |
title_full_unstemmed | Cross-linking of collagen. Location of pyridinoline in bovine articular cartilage at two sites of the molecule |
title_short | Cross-linking of collagen. Location of pyridinoline in bovine articular cartilage at two sites of the molecule |
title_sort | cross-linking of collagen. location of pyridinoline in bovine articular cartilage at two sites of the molecule |
title_unstemmed | Cross-linking of collagen. Location of pyridinoline in bovine articular cartilage at two sites of the molecule |
topic | Cell Biology, Molecular Biology, Biochemistry |
url | http://dx.doi.org/10.1042/bj2150175 |