Glycation of collagen: the basis of its central role in the late complications of ageing and diabetes

Paul, R G; Bailey, Allen J.

doi:10.1016/s1357-2725(96)00079-9

Cited by 324 publications

(237 citation statements)

References 77 publications

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“…Non-enzymatic glycation is a post-translational modification of proteins that occurs through the Maillard reaction, where extracellular sugars spontaneously react with amino groups on proteins to form molecular entities, known as advanced glycation end products (AGEs) (for a review, see Paul and Bailey 15 ). AGEs formed in bone are divided into two types, those making crosslinks between collagen molecules and those that are non-crosslinks.…”

Section: Reviewmentioning

confidence: 99%

The contribution of collagen crosslinks to bone strength

Garnero¹

2012

BoneKEy Reports

102

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Collagen crosslinking is a major post-translational modification of collagen which has important roles in determining the biomechanical competence of bone. Crosslinks can be divided into enzymatic lysil oxidase-mediated and nonenzymatic glycation-induced (advanced glycation end products, AGE) molecules. In addition, collagen in bone can also undergo spontaneous isomerization and racemization of the aspartic acid residues with the C-telopeptide (CTX), leading to the formation of two isomers namely ␣ (newly formed collagen) and ␤ (matured isomerized collagen) CTX. Several in vitro and ex vivo studies, relating the bone content of these crosslinks with bone strength, have shown that they contributed to the mechanical competence of trabecular and cortical bone -mainly on the post-yield properties -in part independent of the bone mineral content. In addition, AGEs such as pentosidine have been reported to alter the formation and propagation of microdamage by making the bone more brittle. The bone content of AGEs and isomerization can also be modified by antiresorptive and anabolic therapies. They may thus explain part of the antifracture efficacy of these treatments. The main challenge consists in the transposition of these in vitro / ex vivo studies to clinical applications for the development of a non-invasive biomarker, as none of currently identified collagen crosslinks (both enzymatic and nonenzymatic) is bone specific. Nevertheless, serum or urine levels of pentosidine and the ratio of ␣ / ␤ CTX have been reported to predict fracture risk in postmenopausal women, in men and in patients with type 2 diabetes.

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Section: Reviewmentioning

confidence: 99%

The contribution of collagen crosslinks to bone strength

Garnero¹

2012

BoneKEy Reports

102

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“…These non-enzymatic cross-links undergo sequential modifications, culminating in the formation of advanced glycation end products (AGE) (Paul and Bailey 1996) which increase tissue stiffness (Sims et al 1996), inhibit collagen assembly (Tsilibary et al 1988) and impair collagen/cell binding (Haitoglou et al 1992). The abundance of these pathological cross-links is positively correlated with both age and with the incidence of chronic hyperglycaemia as found in conditions such as diabetes mellitus (Bruel and Oxlund 1996;Mikulikova et al 2008;Paul and Bailey 1996). Although the structural and functional consequences of AGE formation within ageing collagen-rich tissues have been well characterised in recent years (DeGroot 2004) less attention has been paid to the impact of AGE formation on elastic fibre function (Bailey 2001).…”

Section: Degradationmentioning

confidence: 99%

Tissue elasticity and the ageing elastic fibre

Sherratt

2009

AGE

269

189

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The ability of elastic tissues to deform under physiological forces and to subsequently release stored energy to drive passive recoil is vital to the function of many dynamic tissues. Within vertebrates, elastic fibres allow arteries and lungs to expand and contract, thus controlling variations in blood pressure and returning the pulmonary system to a resting state. Elastic fibres are composite structures composed of a cross-linked elastin core and an outer layer of fibrillin microfibrils. These two components perform distinct roles; elastin stores energy and drives passive recoil, whilst fibrillin microfibrils direct elastogenesis, mediate cell signalling, maintain tissue homeostasis via TGFβ sequestration and potentially act to reinforce the elastic fibre. In many tissues reduced elasticity, as a result of compromised elastic fibre function, becomes increasingly prevalent with age and contributes significantly to the burden of human morbidity and mortality. This review considers how the unique molecular structure, tissue distribution and longevity of elastic fibres pre-disposes these abundant extracellular matrix structures to the accumulation of damage in ageing dermal, pulmonary and vascular tissues. As compromised elasticity is a common feature of ageing dynamic tissues, the development of strategies to prevent, limit or reverse this loss of function will play a key role in reducing age-related morbidity and mortality.

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“…Non-enzymatic reactions between collagen and sugars result in various advanced glycation end products (AGEs) that form additional intermolecular crosslinks or protein adducts [5]. AGEs accumulate with age and impair both mechanical and biological functions of tissues [4,6,7].…”

Section: Introductionmentioning

confidence: 99%

Thermal stability of collagen in naturally ageing and in vitro glycated rabbit tissues

Trębacz

Szczęsna

Arczewska

2018

J Therm Anal Calorim

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The aim of the work was to compare glycation-related changes in thermal denaturation of collagen in naturally ageing and in vitro ribosylated tissues. Samples of cornea, meniscus and Achilles tendon from young adult and from ageing rabbits were compared. Moreover, in vitro glycated samples (ribose, 100 mg mL -1 , 14 days) were prepared for both age groups. Collagen in tissues was characterized in terms of thermal denaturation parameters obtained from differential scanning calorimetry. The level of pentosidine and other fluorescent advanced glycation end products (AGEs) in the papain-digested tissue samples was evaluated using spectrofluorimetry (k ex/em : 335/385 and 370/440 nm). In naturally ageing tissues, changes in properties of extracellular matrix collagen expressed in terms of parameters of thermal denaturation and fluorescent AGEs levels were tissue dependent and were related to differences in organization of matrix components. No signs of increased level of AGEs were found in the naturally ageing cornea, unlike in the tendon and meniscus. In vitro ribation proved by gains of fluorescent AGEs affected thermal stability of collagen in all tissues, both in young adult and in the ageing ones. The effects of ribation were considerably greater than the effects of natural ageing. The increase in denaturation temperature was similarly strong in all tissues and did not correlate with the increase in fluorescent AGEs. As a conclusion, parameters of collagen thermal denaturation are tissue and age dependent and an amount of fluorescent AGEs is not the only determinant of increasing thermal stability of glycated collagen.

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Glycation of collagen: the basis of its central role in the late complications of ageing and diabetes

Cited by 324 publications

References 77 publications

The contribution of collagen crosslinks to bone strength

The contribution of collagen crosslinks to bone strength

Tissue elasticity and the ageing elastic fibre

Thermal stability of collagen in naturally ageing and in vitro glycated rabbit tissues

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