Collagen and Non-Collagenous Proteins in Different Mineralization Stages of Human Femur

Mbuyi-Muamba, J. M.; Dequeker, Jan; Gevers, G

doi:10.1159/000146700

Cited by 18 publications

(6 citation statements)

References 6 publications

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“…19 The function of noncollagenous proteins seems to vary, too. 10,11,[24][25][26][27] The degree of calcification may be a contributing factor in this connection, 28 while calcification may itself be influenced by noncollagenous proteins. 29,30 Proteoglycans may have a regulatory effect, although their role as inhibitors or promoters of the calcification process is still under discussion.…”

Section: Noncollagenous Componentsmentioning

confidence: 99%

“…Because of their different degrees of calcification, osteons and other bone structures can be distinguished on the basis of their different microhardness, 76 and can be separated by means of density gradient fractionation. 28,77,78 The degree of microradiographic density may not be uniform in single osteons. The borders of their vascular canals often appear to be hypermineralized (see Figure 1.8B), a condition that has been thought to be an early sign of bone matrix destruction or "delitescence."…”

Section: Microradiography Of Osteonsmentioning

confidence: 99%

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Basic Composition and Structure of Bone

Bonucci¹

1999

Mechanical Testing of Bone and the Bone-Implant Interface

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Section: Noncollagenous Componentsmentioning

confidence: 99%

Section: Microradiography Of Osteonsmentioning

confidence: 99%

Basic Composition and Structure of Bone

Bonucci¹

1999

Mechanical Testing of Bone and the Bone-Implant Interface

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“…(20) Among NCPs, proteoglycans (PGs) are reported to exist outside of collagen fibrils with strong affinity to extrafibrillar minerals. (21,22) PGs contain abundant glycosaminoglycans (GAGs), which are highly negatively charged and possess a great potential of trapping and retaining water molecules in the matrix. (23,24) In fact, the similar role of GAGs has been well documented for different types of connective tissues, such as articulate cartilage and intervertebral disks.…”

Section: Introductionmentioning

confidence: 99%

Age‐Related Deterioration of Bone Toughness Is Related to Diminishing Amount of Matrix Glycosaminoglycans (GAGs)

et al. 2018

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Hydration status significantly affects the toughness of bone. In addition to the collagen phase, recent evidence shows that glycosaminoglycans (GAGs) of proteoglycans (PGs) in the extracellular matrix also play a pivotal role in regulating the tissue-level hydration status of bone, thereby affecting the tissue-level toughness of bone. In this study, we hypothesized that the amount of GAGs in bone matrix decreased with age and such changes would lead to reduction in bound water and subsequently result in a decrease in the tissue-level toughness of bone. To test the hypothesis, nanoscratch tests were conducted to measure the tissue-level toughness of human cadaveric bone specimens, which were procured only from male donors in three different age groups: young (26 ± 6 years old), mid-aged (52 ± 5 years old) and elderly (73 ± 5 years old), with six donors in each group. Biochemical and histochemical assays were performed to determine the amount and major subtypes of GAGs and proteoglycans in bone matrix. In addition, low-field NMR measurements were implemented to determine bound water content in bone matrix. The results demonstrated that aging resulted in a statistically significant reduction (17%) of GAGs in bone matrix. Concurrently, a significant deterioration (20%) of tissue-level toughness of bone with age was observed. Most importantly, the deteriorated tissue-level toughness of bone was associated significantly with the age-related reduction (40%) of bound water, which was partially induced by the decrease of GAGs in bone matrix. Furthermore, we identified that chondroitin sulfate (CS) was a major subtype of GAGs and the amount of CS decreased with aging in accompany with a decrease of biglycan that is a major subtype of PGs in bone. The findings of this study suggests that reduction of GAGs in bone matrix is likely one of the molecular origins for age-related deterioration of bone quality.

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“…Serving as structural proteins, some NCPs have been found to be directly involved in the deformation and failure of bone . Among the NCPs, proteoglycans (PGs) are present mainly in the extrafibrillar matrix and are unlikely to reside in the mineralized collagen fibrils . These molecules are polar and highly negatively charged, thus possessing a great potential of attracting water into the matrix as observed in articular cartilage .…”

Section: Introductionmentioning

confidence: 99%

“…(9,10) Among the NCPs, proteoglycans (PGs) are present mainly in the extrafibrillar matrix and are unlikely to reside in the mineralized collagen fibrils. (11,12) These molecules are polar and highly negatively charged, thus possessing a great potential of attracting water into the matrix as observed in articular cartilage. (13) Meanwhile, previous evidence has shown that water molecules residing only in very small gaps (<4 Å) in bone matrix play a critical role in the plasticity and toughness of bone.…”

Section: Introductionmentioning

confidence: 99%

Coupling Effect of Water and Proteoglycans on the In Situ Toughness of Bone

Wang

Huang

et al. 2015

Journal of Bone and Mineral Research

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Proteoglycans (PGs) are one type of non-collagenous proteins in the extracellular matrix of bone, which primarily contain a core protein and glycosaminoglycans (GAGs). GAGs are highly polar and negatively charged, thus having a strong tendency in attracting water molecules into the matrix. We hypothesized in this study that PGs in bone play a pivotal role in sustaining the toughness of the tissue only when water is present. To test the hypothesis, we used a novel nanoscratch test to measure the in situ toughness of human cadaveric bone treated with and without PNGase F, an enzyme that specifically removes the N-linked oligosaccharides of GAGs from core proteins. Cortical bone specimens were prepared from the posterior aspect of mid-diaphyseal femurs of six (N=6) male human donors between 51.5±5.17 years old. Biochemical and histochemical assays were used to verify whether N-linked oligosaccharides were removed from bone matrix by PNGase F. By testing wet and dehydrated bone specimens, the coupling effect between water and PGs on the in situ toughness of bone was investigated. The two-way ANOVA analyses showed that removal of GAGs had significant effects on the in situ toughness of wet bone samples. In contrast, the removal of GAGs did not show significant effects on the toughness of dry bone. The results of this study, for the first time, suggest that GAGs play a pivotal role in the in situ toughness of bone only when water is present, and vice versa water functions as a plasticizer in bone only when GAGs are present.

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Collagen and Non-Collagenous Proteins in Different Mineralization Stages of Human Femur

Cited by 18 publications

References 6 publications

Basic Composition and Structure of Bone

Basic Composition and Structure of Bone

Age‐Related Deterioration of Bone Toughness Is Related to Diminishing Amount of Matrix Glycosaminoglycans (GAGs)

Coupling Effect of Water and Proteoglycans on the In Situ Toughness of Bone

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