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Titolo:
Influence of nonenzymatic glycation on biomechanical properties of cortical bone
Autore:
Vashishth, D; Gibson, GJ; Khoury, JI; Schaffler, MB; Kimura, J; Fyhrie, DP;
Indirizzi:
Rensselaer Polytech Inst, Dept Biomed Engn, JEC 7046, Troy, NY 12180 USA Rensselaer Polytech Inst Troy NY USA 12180 , JEC 7046, Troy, NY 12180 USA Henry Ford Hosp, Ctr Bone & Joint, Detroit, MI 48202 USA Henry Ford Hosp Detroit MI USA 48202 Bone & Joint, Detroit, MI 48202 USA Mt Sinai Sch Med, Dept Orthopaed, New York, NY USA Mt Sinai Sch Med New York NY USA h Med, Dept Orthopaed, New York, NY USA
Titolo Testata:
BONE
fascicolo: 2, volume: 28, anno: 2001,
pagine: 195 - 201
SICI:
8756-3282(200102)28:2<195:IONGOB>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
COLLAGEN CROSS-LINKS; MECHANICAL-PROPERTIES; ELASTIC-ANISOTROPY; DIABETIC-PATIENTS; AGE; ORIENTATION; CHEMISTRY; FRACTURES; RELEVANCE; TOUGHNESS;
Keywords:
nonenzymatic glycation; cortical bone; mechanical properties; collagen; cross-link;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Clinical Medicine
Life Sciences
Citazioni:
41
Recensione:
Indirizzi per estratti:
Indirizzo: Vashishth, D Rensselaer Polytech Inst, Dept Biomed Engn, JEC 7046, 110 8thSt, Troy, NY12180 USA Rensselaer Polytech Inst 110 8th St Troy NY USA 12180 180 USA
Citazione:
D. Vashishth et al., "Influence of nonenzymatic glycation on biomechanical properties of cortical bone", BONE, 28(2), 2001, pp. 195-201

Abstract

In this study, the influence of nonenzymatic glycation (NEG) on the mechanical properties of bone and bone collagen were investigated. Bovine cortical bone specimens were incubated in ribose to cause collagen cross-links in vitro, and nondestructive mechanical testing was used to determine tensile and compressive elastic modulus as a function of incubation time. Mechanical properties associated with yield, postyield, and final fracture of bone were determined at the end of the incubation period. The stiffness of the collagen network was measured using stress relaxation tests of demineralized bone cylinders extracted periodically throughout the incubation period, It was found that accumulation of nonenzymatic glycation end-products in cortical bone caused stiffening of the type I collagen network in bone (r(2) = 0.92; p < 0.001) but did not significantly affect the overall stiffness of the mineralized bone (p = 0.98). The ribosylated group had significantly more NEG products and higher yield stress and strain than the control group (p< 0.05). Postyield properties including postyield strain and strain energywere lower in the ribosylated group but were not significantly different from the control group (p = 0.24). Compared with the control group, the ribosylated group was characterized by significantly higher secant modulus and lower damage fraction (p < 0.05). Taken together, the results of this studysuggest that collagen in bone is susceptible to the same NEG-mediated changes as collagen in other connective tissues and that an increased stiffnessof the collagen network in bone due to NEG may explain some of the age-related increase in skeletal fragility and fracture risk. (Bone 28:195-201; 2001) (C) 2001 by Elsevier Science Inc. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 11/07/20 alle ore 13:53:36