Collagen cross-links in mineralizing tissues: A review of their chemistry, function, and clinical relevance

Knott, Lynda; Bailey, Allen J.

doi:10.1016/s8756-3282(97)00279-2

Cited by 591 publications

(419 citation statements)

References 68 publications

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“…Therefore, the increased PEN level with aging in this study most likely reflects decreased remodeling and turnover rates in bone with increased age. Our findings are consistent with literature that indicates that PEN increases with age in human bone (Knott and Bailey, 1998;Wang et al, 2002). The resistance to tension of the collagen network in decalcified bone significantly decreased between 6 and 18 months of age.…”

Section: Aging In Sedentary Animalssupporting

confidence: 93%

“…The collagen matrix is most likely affected during aging (Bailey and Knott, 1999;Viguet-Carrin et al, 2006). The amounts of intra-and intermolecular enzymatic hydroxylysylpyridinoline (HP), lysylpyridinoline (LP) and non-enzymatic pentosidine (PEN) cross-links are believed to change with age (Bailey and Knott, 1999;Banse et al, 2002;Knott and Bailey, 1998). For example, an increase of PEN due to reduced rate of collagen turnover may be partly responsible for the age-related decrease of mechanical strength of the collagen network (Wang et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

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Long-term voluntary exercise of male mice induces more beneficial effects on cancellous and cortical bone than on the collagenous matrix

Isaksson

Tolvanen

Finnilä

et al. 2009

Experimental Gerontology

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This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. ACCEPTED MANUSCRIPT ABSTRACT:The effects of lifelong physical exercise on the composition, structure and mechanical properties of bone are not well understood. Earlier, we found that voluntary physical exercise improved various properties of bone in maturing male mice up to 6 months of age. In the present study, we extended the previous study to 18 months. Half of the mice (total N=144) had access to running wheels while half were kept sedentary. The collagen network was assessed biochemically and by tensile testing of decalcified bone. The mineralized femur was analyzed with pQCT and 3-point-bending of the diaphysis and neck-strength-test. The proximal tibia was analyzed with microCT. The bone collagen revealed inferior tensional properties with aging and the mineralized femur demonstrated decreased stiffness with age. In the running mice, tensile properties and the BMD were reduced at 18 months of age compared to the sedentary mice. In contrast, the stiffness of both the diaphysis and femoral neck was higher, and trabecular architecture and structure were improved in the running mice. In summary, the results suggest that lifelong exercise training of male mice results in more beneficial effects on intact mineralized bone in both the diaphysis and epiphysis than on bone collagenous matrix.

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Section: Aging In Sedentary Animalssupporting

confidence: 93%

Section: Introductionmentioning

confidence: 99%

Long-term voluntary exercise of male mice induces more beneficial effects on cancellous and cortical bone than on the collagenous matrix

Isaksson

Tolvanen

Finnilä

et al. 2009

Experimental Gerontology

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“…Non-enzymatic collagen cross-links are mediated by oxidation and glycation processes, 185 while enzymatic reactions happen between the telopeptide and adjacent triple helical chains, 186 which is mediated by chemical reactions through lysyl oxidase covalent bonding. 187,188 This results in the formation of inter and intra-molecular and inter-microfibrillar cross-links. 187,188,189,190,191 Such enzymatic reactions are the basis of tissue stability, viscoelasticity and strength of collagen fibrils.…”

Section: Cross-linkersmentioning

confidence: 99%

Bonding efficiency and durability: current possibilities

et al. 2017

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Bonding plays a major role in dentistry nowadays. Dental adhesives are used in association with composites to solve many restorative issues. However, the wide variety of bonding agents currently available makes it difficult for clinicians to choose the best alternative in terms of material and technique, especially when different clinical situations are considered. Moreover, although bonding agents allow for a more conservative restorative approach, achieving a durable adhesive interface remains a matter of concern, and this mainly due to degradation of the bonding complex in the challenging oral environment. This review aims to present strategies that are being used or those still in development which may help to prevent degradation. It is fundamental that professionals are aware of these strategies to counteract degradation as much as possible. None of them are efficient to completely solve this problem, but they certainly represent reasonable alternatives to increase the lifetime of adhesive restorations.

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“…These microfibrils further arrange into fibers that can reach a diameter of several hundreds of nanometers. The structures are stabilized through intermolecular cross-links, formed between telopeptides and adjacent triple helical chains through lysine-lysine covalent bonding [13][14][15]. Telopeptides, present at both N-and C-termini, are non-helical domains that remain after the cleavage of propeptides [16].…”

Section: Introductionmentioning

confidence: 99%

Molecular structure, mechanical behavior and failure mechanism of the C-terminal cross-link domain in type I collagen

Uzel

Buehler

2011

Journal of the Mechanical Behavior of Biomedical Materials

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ABSTRACT:Collagen is a key constituent in structural materials found in biology, including bone, tendon, skin and blood vessels. Here we report a first molecular level model of an entire overlap region of a C-terminal cross-linked type I collagen assembly and carry out a nanomechanical characterization based on large-scale molecular dynamics simulation in explicit water solvent. Our results show that the deformation mechanism and strength of the structure is greatly affected by the presence of the cross-link, and by the specific loading condition of how the stretching is applied. We find that the presence of a cross-link results in greater strength during deformation as complete intermolecular slip is prevented, and thereby particularly affects larger deformation levels. Conversely, the lack of a cross-link results in the onset of intermolecular sliding during deformation and as a result an overall weaker structure. Through a detailed analysis of the distribution of deformation by calculating the molecular strain we show that the location of largest strains does not occur around the covalent bonding region, but is found in regions further away from this location. The insight developed from understanding collagenous materials from a fundamental molecular level upwards could play a role in advancing our understanding of physiological and disease states of connective tissues, and also enable the development of new scaffolding material for applications in regenerative medicine and biologically inspired materials. Keywords

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Collagen cross-links in mineralizing tissues: A review of their chemistry, function, and clinical relevance

Cited by 591 publications

References 68 publications

Long-term voluntary exercise of male mice induces more beneficial effects on cancellous and cortical bone than on the collagenous matrix

Long-term voluntary exercise of male mice induces more beneficial effects on cancellous and cortical bone than on the collagenous matrix

Bonding efficiency and durability: current possibilities

Molecular structure, mechanical behavior and failure mechanism of the C-terminal cross-link domain in type I collagen

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