{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,12]],"date-time":"2026-11-12T23:55:44Z","timestamp":1794527744147,"version":"4.9.1"},"reference-count":22,"publisher":"Oxford University Press (OUP)","issue":"9","license":[{"start":{"date-parts":[[1997,9,1]],"date-time":"1997-09-01T00:00:00Z","timestamp":873072000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/open_access\/funder_policies\/chorus\/standard_publication_model"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[1997,9,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>In Paget's disease of bone, the normal lamellar bone is replaced by a woven structure with an irregular arrangement of collagen fibers. In this study, we investigated whether the degree of \u03b2-isomerization within C-telopeptide of \u03b11 chain of type I collagen was altered in Paget's disease compared with other bone diseases with no alteration of bone structure. In Paget's disease (n = 26), but not in patients with primary hyperparathyroidism (n = 6) or hyperthyroidism (n = 17), the urinary excretion of nonisomerized (\u03b1) fragments derived from degradation of type I collagen C-telopeptide (CTX) was markedly increased compared with \u03b2-isomerized CTX (+ 13-fold vs. + 3.5-fold over controls) resulting in an urinary \u03b1 CTX\/\u03b2 CTX ratio 3-fold higher than in controls (2.6 \u00b1 1.0 vs. 0.8 \u00b1 0.3, p &amp;lt; 0.001). In five pagetic patients in complete remission, as demonstrated by normal total alkaline phosphatase activity, the \u03b1 CTX\/\u03b2 CTX ratio was normal. The immunohistochemistry of normal and pagetic human bone sections showed a preferential distribution of \u03b1 CTX within woven structure, while lamellar bone was intensely stained with an anti\u2013\u03b2 CTX antibody, suggesting a lower degree of \u03b2-isomerization of type I collagen in the woven pagetic bone. In collagenase digest of human bone specimens, we found a lower proportion of \u03b2-isomerized type I collagen molecules in pagetic bone (40% of \u03b2 CTX) than in normal bone taken from trabecular (68%) and cortical compartments (71%). In conclusion, we found that in Paget's disease the \u03b1 CTX\/\u03b2 CTX ratio in bone and in urine is markedly increased. This altered \u03b2 isomerization can be accurately detected in vivo by measuring urinary degradation products arising from bone resorption.<\/jats:p>","DOI":"10.1359\/jbmr.1997.12.9.1407","type":"journal-article","created":{"date-parts":[[2006,4,26]],"date-time":"2006-04-26T22:34:26Z","timestamp":1146090866000},"page":"1407-1415","source":"Crossref","is-referenced-by-count":85,"title":["Decreased \u03b2-Isomerization of the C-Terminal Telopeptide of Type I Collagen \u03b11 Chain in Paget's Disease of Bone"],"prefix":"10.1093","volume":"12","author":[{"given":"Patrick","family":"Garnero","sequence":"first","affiliation":[{"name":"INSERM Unit 403, H\u00f4pital E. Herriot, Lyon, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christian","family":"Fledelius","sequence":"additional","affiliation":[{"name":"Osteometer Biotech, Herlev, Denmark"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Evelyne","family":"Gineyts","sequence":"additional","affiliation":[{"name":"INSERM Unit 403, H\u00f4pital E. Herriot, Lyon, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Claire-Marie","family":"Serre","sequence":"additional","affiliation":[{"name":"INSERM Unit 403, H\u00f4pital E. Herriot, Lyon, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Emanuelle","family":"Vignot","sequence":"additional","affiliation":[{"name":"INSERM Unit 403, H\u00f4pital E. Herriot, Lyon, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pierre D.","family":"Delmas","sequence":"additional","affiliation":[{"name":"INSERM Unit 403, H\u00f4pital E. Herriot, Lyon, France"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2009,12,4]]},"reference":[{"key":"2024020712015830600_bib1","first-page":"1075","volume-title":"Osteoporosis","author":"Delmas","year":"1996"},{"key":"2024020712015830600_bib2","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1016\/0076-6879(87)44176-1","article-title":"Collagen crosslinking amino-acids","volume":"144","author":"Eyre","year":"1987","journal-title":"Meth Enzymol"},{"key":"2024020712015830600_bib3","doi-asserted-by":"crossref","first-page":"1133","DOI":"10.1093\/oxfordjournals.jbchem.a134457","article-title":"Analysis of pyridinoline, a cross-linking compound of collagen fibres, in human urine","volume":"94","author":"Fujimoto","year":"1983","journal-title":"J Biochem"},{"key":"2024020712015830600_bib4","author":"Eyre","year":"1988"},{"key":"2024020712015830600_bib5","doi-asserted-by":"crossref","first-page":"635","DOI":"10.1002\/jbmr.5650080515","article-title":"Immunoassay for urinary pyridinoline: The new marker of bone resorption","volume":"8","author":"Seyedin","year":"1993","journal-title":"J Bone Miner Res"},{"key":"2024020712015830600_bib6","doi-asserted-by":"crossref","first-page":"1643","DOI":"10.1002\/jbmr.5650091019","article-title":"Direct, enzyme-linked immunoassay for urinary deoxypyridinoline as a specific marker for measuring bone resorption","volume":"9","author":"Robins","year":"1994","journal-title":"J Bone Miner Res"},{"key":"2024020712015830600_bib7","doi-asserted-by":"crossref","first-page":"2022","DOI":"10.1093\/clinchem\/40.11.2022","article-title":"Immunoassay for quantifying type I collagen degradation products in urine evaluated","volume":"40","author":"Bonde","year":"1994","journal-title":"Clin Chem"},{"key":"2024020712015830600_bib8","doi-asserted-by":"crossref","first-page":"1251","DOI":"10.1002\/jbmr.5650071119","article-title":"A specific immunoassay for monitoring human bone resorption: Quantitation of type I collagen cross-linked N-telopeptides in urine","volume":"11","author":"Hanson","year":"1992","journal-title":"J Bone Miner Res"},{"key":"2024020712015830600_bib9","doi-asserted-by":"crossref","first-page":"643","DOI":"10.1002\/jbmr.5650080516","article-title":"Immunoassay of pyridinoline crosslink excretion in normal adults and in Paget's disease","volume":"8","author":"Delmas","year":"1993","journal-title":"J Bone Miner Res"},{"key":"2024020712015830600_bib10","first-page":"780","article-title":"Assessment of bone resorption with a new marker of collagen degradation in patients with metabolic bone disease","volume":"79","author":"Garnero","year":"1994","journal-title":"J Clin Endocrinol Metab"},{"key":"2024020712015830600_bib11","first-page":"1693","article-title":"Comparison of new biochemical markers of bone turnover in late postmenopausal osteoporotic women in response to alendronate therapy","volume":"79","author":"Garnero","year":"1994","journal-title":"J Clin Endocrinol Metab"},{"key":"2024020712015830600_bib12","first-page":"564","article-title":"Applications of an enzyme immunoassay for a new marker of bone resorption (Crosslaps): Follow-up on hormone replacement therapy and osteoporosis risk assessment","volume":"80","author":"Bonde","year":"1995","journal-title":"J Clin Endocrinol Metab"},{"key":"2024020712015830600_bib13","doi-asserted-by":"crossref","first-page":"9755","DOI":"10.1074\/jbc.272.15.9755","article-title":"Characterization of urinary degradation products derived from type I collagen: Identification of a \u03b2-isomerized aspartyl residue within the C-telopeptide (\u03b11) region","volume":"272","author":"Fledelius","year":"1997","journal-title":"J Biol Chem"},{"key":"2024020712015830600_bib14","first-page":"103","article-title":"Does the chemical instability of aspartyl and asparaginyl residues in proteins contribute to erythrocyte aging?","volume":"14","author":"Lowenson","year":"1988","journal-title":"Blood Cells"},{"key":"2024020712015830600_bib15","doi-asserted-by":"crossref","first-page":"3072","DOI":"10.1016\/S0021-9258(18)53661-9","article-title":"Structural alterations in the peptide backbone of \u03b2 amyloid core protein may account for its deposition and stability in Alzheimer Disease","volume":"268","author":"Roher","year":"1993","journal-title":"J Biol Chem"},{"key":"2024020712015830600_bib16","doi-asserted-by":"crossref","first-page":"1639","DOI":"10.1093\/clinchem\/42.10.1639","article-title":"Coated tube radioimmunoassay for C. telopeptides of type I collagen to assess bone resorption","volume":"42","author":"Bonde","year":"1996","journal-title":"Clin Chem"},{"key":"2024020712015830600_bib17","first-page":"375","volume-title":"Primer on the Metabolic Bone Diseases and Disorders of the Mineral Metabolism","author":"Siris","year":"1993"},{"key":"2024020712015830600_bib18","doi-asserted-by":"crossref","first-page":"1073","DOI":"10.1002\/art.1780231005","article-title":"Bone histomorphometry in Paget's disease: Quantitative and dynamic analysis of pagetic and non-pagetic bone tissue","volume":"23","author":"Meunier","year":"1980","journal-title":"Arth Rheum"},{"key":"2024020712015830600_bib19","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1097\/00003086-198704000-00006","article-title":"Skeletal distribution and biochemical parameters of Paget's disease","volume":"217","author":"Meunier","year":"1987","journal-title":"Clin Orthop"},{"key":"2024020712015830600_bib20","first-page":"759","article-title":"Analyse des perturbations des voies principales du m\u00e9tabolisme calcique dans la maladie de Paget: Effets de l'administration de calcitonine","volume":"42","author":"Coutris","year":"1975","journal-title":"Rev Rheum"},{"key":"2024020712015830600_bib21","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1016\/0169-6009(91)90143-N","article-title":"Urinary excretion of pyridinium crosslinks: A new marker of bone resorption in metabolic bone disease","volume":"8","author":"Uebelhart","year":"1990","journal-title":"Bone Miner"},{"key":"2024020712015830600_bib22","doi-asserted-by":"crossref","first-page":"785","DOI":"10.1016\/S0021-9258(19)75855-4","article-title":"Deamination, isomerization, and racemization at asparaginyl and aspartyl residues in peptides","volume":"262","author":"Geiger","year":"1987","journal-title":"J Biol Chem"}],"container-title":["Journal of Bone and Mineral Research"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.wiley.com\/onlinelibrary\/tdm\/v1\/articles\/10.1359%2Fjbmr.1997.12.9.1407","content-type":"unspecified","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/academic.oup.com\/jbmr\/article-pdf\/12\/9\/1407\/56594771\/5650120911.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/academic.oup.com\/jbmr\/article-pdf\/12\/9\/1407\/56594771\/5650120911.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,3,13]],"date-time":"2024-03-13T14:55:33Z","timestamp":1710341733000},"score":1,"resource":{"primary":{"URL":"https:\/\/academic.oup.com\/jbmr\/article\/12\/9\/1407-1415\/7514079"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1997,9,1]]},"references-count":22,"journal-issue":{"issue":"9","published-online":{"date-parts":[[2009,12,4]]},"published-print":{"date-parts":[[1997,9,1]]}},"URL":"https:\/\/doi.org\/10.1359\/jbmr.1997.12.9.1407","relation":{},"ISSN":["0884-0431","1523-4681"],"issn-type":[{"value":"0884-0431","type":"print"},{"value":"1523-4681","type":"electronic"}],"subject":[],"published-other":{"date-parts":[[1997,9,1]]},"published":{"date-parts":[[1997,9,1]]}}}