Alteration in the Extent of Collagen I Hydroxylation, Isolated from Femoral Heads of Women with a Femoral Neck Fracture Caused by Osteoporosis

Köwitz, Jutta; Knippel, Monika; Schuhr, T.; Mach, J

doi:10.1007/s002239900271

Cited by 48 publications

(21 citation statements)

References 21 publications

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“…These two features (low collagen and high Lys hydroxylation) are similar those found in femurs of SAMP6 [17] indicating the similarity between mandibles and femurs. Higher Lys hydroxylation was reported in human osteoporotic bone [33,34]. The extent of Lys hydroxylation and subsequent glycosylation affect lateral packing of collagen molecules [24] and collagen fibrillogenesis [25,26].…”

Section: Discussionmentioning

confidence: 97%

Characterization of Mandibular Bones in Senile Osteoporotic Mice

Tokutomi

Mizutani

Atsawasuwan

et al. 2008

Connective Tissue Research

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At present, little is known about the age-related changes in jaw bones. The aim of this study was to characterize the mandibles of 6 month-old senile osteoporotic mice, SAMP6, and compare with those of age-matched controls, SAMR1. In comparison to SAMR1, SAMP6 showed thinner cortical bone, lower bone volume, and poorly organized collagen matrix. The collagen fibril diameter in SAMP6 was significantly smaller than that of SAMR1. In SAMP6 both collagen content and cross-links were lower than those of SAMR1, but the ratio of the major mature cross-link (pyridinoline) to its precursor reducible cross-link (dehydrodihydroxylysinonorleucine/its ketoamine) was higher in comparison to SAMR1. In addition, the extent of lysine hydroxylation of collagen was higher in SAMP6 than that of SAMR1. These results indicate that not only the quantity of collagen but also its quality are altered in SAMP6 and may result in the age-associated osteoporotic defects of mandibles.

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Section: Discussionmentioning

confidence: 97%

Characterization of Mandibular Bones in Senile Osteoporotic Mice

Tokutomi

Mizutani

Atsawasuwan

et al. 2008

Connective Tissue Research

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“…In human, osteoporotic bones, which exhibit decreased quantity and impaired mineralization of bone, have shown lower content of collagen 18,19) and higher extent of Lys hydroxylation [19][20][21][22] be partly damaged compared to those from fresh bone. However, the contents of collagen (average of 125~128 ìg/mg of dried bone)…”

Section: Discussionmentioning

confidence: 99%

Higher Contents of Mineral and Collagen but Lower of Hydroxylysine of Collagen in Mandibular Bone Compared with Those of Humeral and Femoral Bones in Human

Sasaki

Mizutani

Katafuchi

et al. 2010

J. Hard Tissue Biology.

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Minerals and collagen are major components of bone. At present, little is known about the material property of the jaw bone compared to other bones of the body. The purpose of this study was to characterize the material property of mandibular bone expressed by the amount of mineral, collagen, and hydroxylysine (Hyl) in comparison with humeral and femoral bones using human cadavers. Mineral and collagen contents were significantly higher in the mandible than in humerus and femur but Hyl was significantly lower in the mandible. Among the three indices, a weak but significantly positive correlation between collagen and mineral contents was observed. On the contrary, Hyl showed a weak but significantly negative correlation with mineral. The three indices were almost not affected by aging, gender, and dental status which were thought to influence bone quantity. These results suggest that human mandibular bone differs in material property from humeral and femoral bones, and may possess a higher mechanical property explained by the hypothesis that adequate and no excessive extent of lysine hydroxylation of collagen leads to optimal collagen fibrillogenesis and matrix mineralization. The assessment of bone property as shown in this study could disclose unknown characteristics which cannot be expressed by bone quantity.

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“…Various changes in the compositional properties of the collagen have been reported at the onset of post-menopausal osteoporosis; a recent study suggests that type I collagen synthesis increases during osteoporosis, whereas earlier studies reported a reduction in the amount of type VI collagen and type III collagen (Bailey et al 1993). Increased hydroxylation of lysine residues occurs (Batge et al 1992;Kowitz et al 1997) and this modulates the nature of the collagen cross-links that are formed extracellularly. Indeed, decreases in the quantity of ketoimine, pyridinium (Mansell & Bailey 2003), aldimine (Bailey et al 1993;Oxlund et al 1996) and pyrrole cross-links have been reported for osteoporotic bone (Knott et al 1995).…”

Section: Bone Tissue Properties and Composition During Osteoporosismentioning

confidence: 99%

Perspective on post-menopausal osteoporosis: establishing an interdisciplinary understanding of the sequence of events from the molecular level to whole bone fractures

McNamara

2009

J. R. Soc. Interface.

102

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Current drug treatments for post-menopausal osteoporosis cannot eliminate bone fractures, possibly because the mechanisms responsible for bone loss are not fully understood. Although research within various disciplines has significantly advanced the state of knowledge, fundamental findings are not widely understood between different disciplines. For that reason, this paper presents noteworthy experimental findings from discrete disciplines focusing on post-menopausal osteoporosis. These studies have established that, in addition to bone loss, significant changes in bone micro-architecture, tissue composition and micro-damage occur. Cellular processes and molecular signalling pathways governing pathological bone resorption have been identified to a certain extent. Ongoing studies endeavour to determine how such changes are initiated at the onset of oestrogen deficiency. It emerges that, because of the discrete nature of previous research studies, the sequence of events that lead to bone fracture is not fully understood. In this paper, two sequences of multi-scale changes are proposed and the experimental challenges that need to be overcome to fully define this sequence are outlined. Future studies must comprehensively characterize the time sequence of molecular-, cellular-and tissue-level changes to attain a coherent understanding of the events that ultimately lead to bone fracture and inform the future development of treatments for post-menopausal osteoporosis.

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Alteration in the Extent of Collagen I Hydroxylation, Isolated from Femoral Heads of Women with a Femoral Neck Fracture Caused by Osteoporosis

Cited by 48 publications

References 21 publications

Characterization of Mandibular Bones in Senile Osteoporotic Mice

Characterization of Mandibular Bones in Senile Osteoporotic Mice

Higher Contents of Mineral and Collagen but Lower of Hydroxylysine of Collagen in Mandibular Bone Compared with Those of Humeral and Femoral Bones in Human

Perspective on post-menopausal osteoporosis: establishing an interdisciplinary understanding of the sequence of events from the molecular level to whole bone fractures

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