Mechanical Loading Stimulates Expression of Collagen Cross‐Linking Associated Enzymes in Periodontal Ligament

Kaku, Masaru; Rocabado, Juan Marcelo Rosales; Kitami, Megumi; Ida, Takako; Akiba, Yosuke; Yamauchi, Mitsuo; Uoshima, Katsumi

doi:10.1002/jcp.25184

Cited by 32 publications

(44 citation statements)

References 45 publications

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“…However, cartilage and ligament collagen show normal hydroxylation of telopeptide lysine and normal crosslinking patterns [57,58]. In line with this observation, it has recently been reported that the expression of LH2 increases in response to mechanical loading on the bone-associated, but not the cementum-associated, side of the periodontal ligament [53]. FKBP65, a peptidyl-prolyl cis-trans isomerase, is essential for the dimerization and enzymatic activity of LH2.…”

Section: Post-translational Modifications Of Type I Collagensupporting

confidence: 52%

“…A number of unique collagen-modifying enzymes and molecular chaperones are involved in these processes [46,47]. Various factors affect post-translational modifications of type I collagen, including aging [48], systemic diseases (e.g., osteoporosis, osteopetrosis, OI, and diabetes) [32,49], and mechanical stress [50][51][52][53][54].…”

Section: Post-translational Modifications Of Type I Collagenmentioning

confidence: 99%

“…The importance of enzymatic collagen cross-linking in tissue development and maintenance has been examined using lathyrogens, such as aminoacetonitrile and beta-aminopropionitrile (BAPN), which irreversibly inhibit LOX activity [53,61,63]. In a previous animal study, 4 weeks of daily intraperitoneal injection of BAPN induced a 45% reduction of pyridinium cross-link content, resulting in a 26% reduction in the bending strength of rat femurs [61].…”

Section: Collagen Cross-linkingmentioning

confidence: 99%

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A paradigm shift for bone quality in dentistry: A literature review

Kuroshima

Kaku

Ishimoto

et al. 2017

Journal of Prosthodontic Research

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A B S T R A C TPurpose: The aim of this study was to present the current concept of bone quality based on the proposal by the National Institutes of Health (NIH) and some of the cellular and molecular factors that affect bone quality. Study selection: This is a literature review which focuses on collagen, biological apatite (BAp), and bone cells such as osteoblasts and osteocytes. Results: In dentistry, the term "bone quality" has long been considered to be synonymous with bone mineral density (BMD) based on radiographic and sensible evaluations. In 2000, the NIH proposed the concept of bone quality as "the sum of all characteristics of bone that influence the bone's resistance to fracture," which is completely independent of BMD. The NIH defines bone quality as comprising bone architecture, bone turnover, bone mineralization, and micro-damage accumulation. Moreover, our investigations have demonstrated that BAp, collagen, and bone cells such as osteoblasts and osteocytes play essential roles in controlling the current concept of bone quality in bone around hip and dental implants. Conclusion: The current concept of bone quality is crucial for understanding bone mechanical functions. BAp, collagen and osteocytes are the main factors affecting bone quality. Moreover, mechanical loading dynamically adapts bone quality. Understanding the current concept of bone quality is required in dentistry.

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Section: Post-translational Modifications Of Type I Collagensupporting

confidence: 52%

Section: Post-translational Modifications Of Type I Collagenmentioning

confidence: 99%

Section: Collagen Cross-linkingmentioning

confidence: 99%

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A paradigm shift for bone quality in dentistry: A literature review

Kuroshima

Kaku

Ishimoto

et al. 2017

Journal of Prosthodontic Research

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“…We also visualized collagen fibers by picrosirius red staining (Kaku et al, 2016). No overt changes were found in both E18.5 and P9 samples (Supplementary Fig.…”

Section: Resultsmentioning

confidence: 99%

BmpR1A is a major type 1 BMP receptor for BMP-Smad signaling during skull development

Pan

Zhang

Abraham

et al. 2017

Developmental Biology

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Craniosynostosis is caused by premature fusion of one or more sutures in an infant skull, resulting in abnormal facial features. The molecular and cellular mechanisms by which genetic mutations cause craniosynostosis are incompletely characterized, and many of the causative genes for diverse types of syndromic craniosynostosis have not yet been identified. We previously demonstrated that augmentation of BMP signaling mediated by a constitutively active BMP type IA receptor (ca-BmpR1A) in neural crest cells (ca1A hereafter) causes craniosynostosis and superimposition of heterozygous null mutation of Bmpr1a rescues premature suture fusion (ca1A;1aH hereafter). In this study, we superimposed heterozygous null mutations of the other two BMP type I receptors, Bmpr1b and Acvr1 (ca1A;1bH and ca1A;AcH respectively hereafter) to further dissect involvement of BMP-Smad signaling. Unlike caA1;1aH, ca1A;1bH and ca1A;AcH did not restore the craniosynostosis phenotypes. In our in vivo study, Smad-dependent BMP signaling was decreased to normal levels in mut;1aH mice. However, BMP receptor-regulated Smads (R-Smads; pSmad1/5/9 hereafter) levels were comparable between ca1A, ca1A;1bH and ca1A;AcH mice, and elevated compared to control mice. Bmpr1a, Bmpr1b and Acvr1 null cells were used to examine potential mechanisms underlying the differences in ability of heterozygosity for Bmpr1a vs. Bmpr1b or Acvr1 to rescue the mut phenotype. pSmad1/5/9 level was undetectable in Bmpr1a homozygous null cells while pSmad1/5/9 levels did not decrease in Bmpr1b or Acvr1 homozygous null cells. Taken together, our study indicates that different levels of expression and subsequent activation of Smad signaling differentially contribute each BMP type I receptor to BMP-Smad signaling and craniofacial development. These results also suggest differential involvement of each type 1 receptor in pathogenesis of syndromic craniosynostoses.

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“…Type I collagen production is epigenetically controlled in PDL, with collagen expression decreasing with age . Furthermore, PDL‐derived cells have been shown to up‐ and downregulate various genes under mechanical stress . It is unknown whether the lack of prolyl 3‐hydroxylation in PDL is the result of low P3H2 gene expression or if the rapid turnover of collagen substrate potentially encumbers enzyme activity.…”

Section: Discussionmentioning

confidence: 99%

Distinct post‐translational features of type I collagen are conserved in mouse and human periodontal ligament

Hudson

Garibov

Dixon

et al. 2017

J of Periodontal Research

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Objectives Specifics of the biochemical pathways that modulate collagen cross-links in the periodontal ligament (PDL) are not fully defined. Better knowledge of the collagen post-translational modifications that give PDL its distinct tissue properties is needed to understand the pathogenic mechanisms of human PDL destruction in periodontal disease. In this study the post-translational phenotypes of human and mouse PDL type I collagen were surveyed using mass spectrometry. Background PDL is a highly specialized connective tissue that joins tooth cementum to alveolar bone. The main function of the PDL is to support the tooth within the alveolar bone while under occlusal load after tooth eruption. Almost half of the adult population in the US suffers from periodontal disease resulting from inflammatory destruction of the PDL, leading to tooth loss. Interestingly, PDL is unique from other ligamentous connective tissues as it has a high rate of turnover. Rapid turnover is believed to be an important characteristic in order for this specialized ligament to function within the oral-microbial environment. Like other ligaments, PDL is composed predominantly of type I collagen. Collagen synthesis is a complex process with multiple steps and numerous post-translational modifications including hydroxylation, glycosylation, and cross-linking. The chemistry, placement and quantity of intermolecular cross-links are believed to be important regulators of tissue-specific structural and mechanical properties of collagens. Methods Type I collagen was isolated from several mouse and human tissues, including PDL, and analyzed by mass spectrometry for post-translational variances. Results The collagen telopeptide cross-linking lysines of PDL 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-linking residue varied across species and between ligaments. These data suggest that different types of ligament collagen, notably PDL, appear to have evolved distinctive lysine/hydroxylysine cross-linking variations. Another distinguishing feature of PDL collagen is that, unlike other ligaments, it lacks any of the known P3H2-catalyzed 3-hydroxyproline site modifications that characterize tendon and ligament collagens. This gives PDL a novel modification profile, with hybrid features of both ligament and skin collagens. Conclusion This distinctive post-translational phenotype may be relevant for understanding why some individuals are at risk of rapid PDL destruction in periodontal disease and warrants further investigation. In addition, developing a murine model for studying PDL collagen may be useful for exploring potential clinical strategies for promoting PDL regeneration.

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Mechanical Loading Stimulates Expression of Collagen Cross‐Linking Associated Enzymes in Periodontal Ligament

Cited by 32 publications

References 45 publications

A paradigm shift for bone quality in dentistry: A literature review

A paradigm shift for bone quality in dentistry: A literature review

BmpR1A is a major type 1 BMP receptor for BMP-Smad signaling during skull development

Distinct post‐translational features of type I collagen are conserved in mouse and human periodontal ligament

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