By a News Reporter-Staff News Editor at Health & Medicine Week -- Data detailed on Bone Research have been presented. According to news reporting out of New Haven, Connecticut, by NewsRx editors, research stated, "Mechanical resilience of bone tissue decreases with age. The ability to comprehensively probe and understand bone properties could help alleviate this problem."
Our news journalists obtained a quote from the research from Yale University, "One important aspect of bone quality that has recently been made evident is the presence of dilatational bands formed by osteocalcin (OC) and osteopontin (OPN), which contribute to fracture toughness. However, experimental evidence of the structural role of these two proteins at the organic-mineral interface in bone is still needed. Solid state nuclear magnetic resonance (SSNMR) is emerging as a useful technique in probing molecular level aspects of bone. Here, we present the first SSNMR study of bone tissue from genetically modified mice lacking OC and/or OPN. Probing the mineral phase, the organic matrix and their interface revealed that, despite the absence of OC and OPN, the organic matrix and mineral were well preserved, and the overall exposure of collagen to hydroxyapatite (HA) nanoparticles was hardly affected. However, the proximity to the HA surface was slightly increased for a number of bone components including less abundant amino acids like lysine, suggesting that this is how the tissue compensates for the lack of OC and OPN. Taken together, the NMR data supports the recently proposed model, in which the contribution of OC-OPN to fracture toughness is related to their presence at the extrafibrillar organic-mineral interfaces, where they reinforce the network of mineralized fibrils and form dilatational bands. In an effort toward further understanding the structural role of individual amino acids of low abundance in bone, we then explored the possibility of specific C-13 enrichment of mouse bone, and report the first SSNMR spectra of 97% C-13 lysine-enriched tissue."
According to the news editors, the research concluded: "Results show that such isotopic enrichment allows valuable molecular-level structural information to be extracted, and sheds light on post-translational modifications undergone by specific amino acids in vivo."
For more information on this research see: NMR Investigation of the Role of Osteocalcin and Osteopontin at the Organic-Inorganic Interface in Bone. Langmuir, 2013;29(45):13873-13882. Langmuir can be contacted at: Amer Chemical Soc, 1155 16TH St, NW, Washington, DC 20036, USA. (American Chemical Society - www.acs.org; Langmuir - www.pubs.acs.org/journal/langd5)
Our news journalists report that additional information may be obtained by contacting O. Nikel, Yale University, Sch Med, New Haven, CT 06520, United States. Additional authors for this research include D. Laurencin, S.A. McCallum, C.M. Gundberg and D. Vashishth (see also Bone Research).
Keywords for this news article include: Peptides, New Haven, Cytokines, Connecticut, Amino Acids, Osteopontin, United States, Bone Research, North and Central America, Extracellular Matrix Proteins
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