Intermolecular crosslinking and stereospecific molecular packing in type I collagen fibrils of the periodontal ligament

Yamauchi, Mitsuo; Katz, Elton P.; Mechanic, Gerald L.

doi:10.1021/bi00365a027

Cited by 133 publications

(124 citation statements)

References 46 publications

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“…6). However, biochemical studies have shown that the periodontal ligament exhibits no significant changes in the quantities of the major reducible collagen cross-links during development and maturation (Pearson et al, 1975), and shows only small amounts of mature, nonreducible cross-links (Yamauchi et al, 1986) in the bovine incisor. Further studies are needed to clarify the discrepancy between polarized light microscopic and biochemical studies.…”

Section: Discussionmentioning

confidence: 99%

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Polarized light microscopic analyses of collagen fibers in the rat incisor periodontal ligament in relation to areas, regions, and ages

Komatsu¹,

Mosekilde²,

Viidik³

et al. 2002

Anat. Rec.

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We prepared decalcified sagittal sections (20 m thick) from the incisal, middle, and basal regions of the mandibular incisor of male Wistar rats aged 2, 6, 12, and 24 months, and examined the sections using polarized light microscopy. Most of the birefringent fibers appeared to run obliquely across the periodontal ligament. Birefringent fibers running parallel to the long axis of the incisor were also found in the intermediate area of the ligament. Similar fiber architecture was observed in all four age groups. Quantitative analysis showed that the retardation values of collagen were higher in the bone-and tooth-related areas and lower in the intermediate area of the ligament. The values for the bone-and tooth-related areas increased from the basal toward the incisal regions in all four age groups. Age-related changes in the retardation values were found only in the incisal region of the incisor. In the incisal region, the values for the bone-and tooth-related areas increased markedly from 2-24 months of age, whereas those for the intermediate area increased slightly but significantly with age. Our findings indicate that the degrees of molecular organization and alignment of collagen fibers in the bone-and tooth-related areas of the ligament are higher than those in the intermediate area and increase near the incisal region and with age. It is also suggested that the collagen fibers in the intermediate area remain immature along the long axis of the incisor throughout the life span of the animal. Anat Rec 268: 381-387, 2002.

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Section: Discussionmentioning

confidence: 99%

“…Its key structural components are load-bearing collagen fibers consisting mainly of type I and III collagens (Yamauchi et al, 1986;Sodek and Ferrier, 1988).…”

mentioning

confidence: 99%

Polarized light microscopic analyses of collagen fibers in the rat incisor periodontal ligament in relation to areas, regions, and ages

Komatsu¹,

Mosekilde²,

Viidik³

et al. 2002

Anat. Rec.

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“…The specific activity of the NaB 3 H 4 was determined by the method described previously (34,35). The reduced samples were washed with cold distilled water several times by repeated centrifugation at 4,000 ϫ g and lyophilized.…”

Section: Methodsmentioning

confidence: 99%

“…The glycosylated immature reducible cross-links were analyzed employing base hydrolysis of the reduced samples as described above (34). By applying the hydrolysates to the HPLC system, the glycosylated (GG-and G-) and non-glycosylated cross-links were separated.…”

Section: Methodsmentioning

confidence: 99%

Cyclophilin-B Modulates Collagen Cross-linking by Differentially Affecting Lysine Hydroxylation in the Helical and Telopeptidyl Domains of Tendon Type I Collagen

Terajima

Taga

Chen

et al. 2016

Journal of Biological Chemistry

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Covalent intermolecular cross-linking provides collagen fibrils with stability. The cross-linking chemistry is tissue-specific and determined primarily by the state of lysine hydroxylation at specific sites. A recent study on cyclophilin B (CypB) null mice, a model of recessive osteogenesis imperfecta, demonstrated that lysine hydroxylation at the helical cross-linking site of bone type I collagen was diminished in these animals (Cabral, W. A., Perdivara, I., Weis, M., Terajima, M., Blissett, A. R., Chang, W., Perosky, J. E., Makareeva, E. N., Mertz, E. L., Leikin, S., Tomer, K. B., Kozloff, K. M., Eyre, D. R., Yamauchi, M., and Marini, J. C. (2014) PLoS Genet. 10, e1004465). However, the extent of decrease appears to be tissue-and molecular site-specific, the mechanism of which is unknown. Here we report that although CypB deficiency resulted in lower lysine hydroxylation in the helical cross-linking sites, it was increased in the telopeptide cross-linking sites in tendon type I collagen. This resulted in a decrease in the lysine aldehyde-derived cross-links but generation of hydroxylysine aldehyde-derived cross-links. The latter were absent from the wild type and heterozygous mice. Glycosylation of hydroxylysine residues was moderately increased in the CypB null tendon. We found that CypB interacted with all lysyl hydroxylase isoforms (isoforms 1-3) and a putative lysyl hydroxylase-2 chaperone, 65-kDa FK506-binding protein. Tendon collagen in CypB null mice showed severe size and organizational abnormalities. The data indicate that CypB modulates collagen cross-linking by differentially affecting lysine hydroxylation in a site-specific manner, possibly via its interaction with lysyl hydroxylases and associated molecules. This study underscores the critical importance of collagen post-translational modifications in connective tissue formation.Collagens comprise a large family of structurally related extracellular matrix proteins (1). Among all of the genetic types of collagen identified, fibrillar type I collagen is the most abundant, providing tissues and organs with form and stability. It is a heterotrimeric molecule composed of two ␣1 chains and one ␣2 chain forming a long uninterrupted triple helix with short non-helical domains (telopeptide) at both N and C termini. One of the functionally important characteristics of collagen is its unique, sequential post-translational modifications of Lys residues. The modifications include hydroxylation and monoand diglycosylation of hydroxylysine (Hyl), 3 and oxidative deamination of Lys and Hyl in the N-and C-telopeptides followed by extensive covalent intermolecular cross-linking (2). It is now clear that defective Lys modifications of collagen cause and/or are associated with a broad range of connective tissue disorders, including Ehlers-Danlos syndrome type VIA (3), bronchopulmonary dysplasia (4), Kuskokwim syndrome (5), Bruck syndrome (6, 7), fibrosis (8), disuse osteoporosis (9), and cancer progression (10, 11). Our recent finding showed that a switch of collage...

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“…Collagen cross-linking sites reportedly correlate with the molecular packing of collagen fibrils and subsequent nucleation of BAp [67]. Although the bio-mineralization process has been thought to be directed by acidic non-collagenous proteins, such as small integrin-binding ligand N-linked glycoprotein [68], it has been reported that type I collagen can initiate bio-mineralization in the absence of any other extracellular matrix molecules in vitro [69].…”

Section: Collagen Cross-linkingmentioning

confidence: 99%

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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Intermolecular crosslinking and stereospecific molecular packing in type I collagen fibrils of the periodontal ligament

Cited by 133 publications

References 46 publications

Polarized light microscopic analyses of collagen fibers in the rat incisor periodontal ligament in relation to areas, regions, and ages

Polarized light microscopic analyses of collagen fibers in the rat incisor periodontal ligament in relation to areas, regions, and ages

Cyclophilin-B Modulates Collagen Cross-linking by Differentially Affecting Lysine Hydroxylation in the Helical and Telopeptidyl Domains of Tendon Type I Collagen

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

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