{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,22]],"date-time":"2026-09-22T17:50:36Z","timestamp":1790099436163,"version":"4.0.1"},"reference-count":38,"publisher":"Wiley","issue":"6","license":[{"start":{"date-parts":[[2017,6,20]],"date-time":"2017-06-20T00:00:00Z","timestamp":1497916800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/100000069","name":"National Institute of Arthritis and Musculoskeletal and Skin Diseases","doi-asserted-by":"publisher","award":["AR037318"],"award-info":[{"award-number":["AR037318"]}],"id":[{"id":"10.13039\/100000069","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000069","name":"National Institute of Arthritis and Musculoskeletal and Skin Diseases","doi-asserted-by":"publisher","award":["AR036794"],"award-info":[{"award-number":["AR036794"]}],"id":[{"id":"10.13039\/100000069","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["J of Periodontal Research"],"published-print":{"date-parts":[[2017,12]]},"abstract":"Background and Objective<\/jats:title>Specifics of the biochemical pathways that modulate collagen cross\u2010links in the periodontal ligament (PDL<\/jats:styled-content>) are not fully defined. Better knowledge of the collagen post\u2010translational modifications that give PDL<\/jats:styled-content> its distinct tissue properties is needed to understand the pathogenic mechanisms of human PDL<\/jats:styled-content> destruction in periodontal disease. In this study, the post\u2010translational phenotypes of human and mouse PDL<\/jats:styled-content> type I collagen were surveyed using mass spectrometry.<\/jats:p>PDL<\/jats:styled-content> is a highly specialized connective tissue that joins tooth cementum to alveolar bone. The main function of the PDL<\/jats:styled-content> is to support the tooth within the alveolar bone while under occlusal load after tooth eruption. Almost half of the adult population in the USA<\/jats:styled-content> has periodontal disease resulting from inflammatory destruction of the PDL<\/jats:styled-content>, leading to tooth loss. Interestingly, PDL<\/jats:styled-content> is unique from other ligamentous connective tissues as it has a high rate of turnover. Rapid turnover is believed to be an important characteristic for this specialized ligament to function within the oral\u2010microbial environment. Like other ligaments, PDL<\/jats:styled-content> is composed predominantly of type I collagen. Collagen synthesis is a complex process with multiple steps and numerous post\u2010translational modifications including hydroxylation, glycosylation and cross\u2010linking. The chemistry, placement and quantity of intermolecular cross\u2010links are believed to be important regulators of tissue\u2010specific structural and mechanical properties of collagens.<\/jats:p><\/jats:sec>Material and Methods<\/jats:title>Type I collagen was isolated from several mouse and human tissues, including PDL<\/jats:styled-content>, and analyzed by mass spectrometry for post\u2010translational variances.<\/jats:p><\/jats:sec>Results<\/jats:title>The collagen telopeptide cross\u2010linking lysines of PDL<\/jats:styled-content> were found to be partially hydroxylated in human and mouse, as well as in other types of ligament. However, the degree of hydroxylation and glycosylation at the helical Lys87 cross\u2010linking residue varied across species and between ligaments. These data suggest that different types of ligament collagen, notably PDL<\/jats:styled-content>, appear to have evolved distinctive lysine\/hydroxylysine cross\u2010linking variations. Another distinguishing feature of PDL<\/jats:styled-content> collagen is that, unlike other ligaments, it lacks any of the known prolyl 3\u2010hydroxylase 2\u2010catalyzed 3\u2010hydroxyproline site modifications that characterize tendon and ligament collagens. This gives PDL<\/jats:styled-content> a novel modification profile, with hybrid features of both ligament and skin collagens.<\/jats:p><\/jats:sec>Conclusion<\/jats:title>This distinctive post\u2010translational phenotype may be relevant for understanding why some individuals are at risk of rapid PDL<\/jats:styled-content> destruction in periodontal disease and warrants further investigation. In addition, developing a murine model for studying PDL<\/jats:styled-content> collagen may be useful for exploring potential clinical strategies for promoting PDL<\/jats:styled-content> regeneration.<\/jats:p><\/jats:sec>","DOI":"10.1111\/jre.12475","type":"journal-article","created":{"date-parts":[[2017,6,20]],"date-time":"2017-06-20T07:43:35Z","timestamp":1497944615000},"page":"1042-1049","source":"Crossref","is-referenced-by-count":35,"title":["Distinct post\u2010translational features of type I collagen are conserved in mouse and human periodontal ligament"],"prefix":"10.1111","volume":"52","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-3253-9890","authenticated-orcid":false,"given":"D. 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