The effect of age on bone collagen turnover as assessed by pyridinium crosslinks and procollagen I C-terminal peptide

1993 ◽  
Vol 3 (S1) ◽  
pp. 100-101 ◽  
Author(s):  
R. Eastell ◽  
N. F. A. Peel ◽  
R. A. Hannon ◽  
A. Blumsohn ◽  
A. Price ◽  
...  
Keyword(s):  
Bone Collagen ◽  
Collagen Turnover ◽  
Pyridinium Crosslinks ◽  
Effect Of Age

10. Effect of age on bone collagen turnover in older women

Bone ◽  
1992 ◽  
Vol 13 (3) ◽  
pp. 275
Author(s):  
R. Eastell ◽  
N.F.A. Peel ◽  
R.A. Hannon ◽  
A. Blumsohn ◽  
A. Price ◽  
...  
Keyword(s):  
Older Women ◽  
Bone Collagen ◽  
Collagen Turnover ◽  
Effect Of Age

Hydroxylysine Glycosides in Human Urine

1971 ◽  
Vol 17 (8) ◽  
pp. 782-788 ◽  
Author(s):  
Marjorie F Lou ◽  
Paul B Hamilton
Keyword(s):  
Amino Acid ◽  
Human Urine ◽  
Bone Collagen ◽  
Molar Ratio ◽  
Collagen Turnover ◽  
Surgical Fusion ◽  
Cation Exchange Column ◽  
Normal Human ◽  
Effluent Stream ◽  
Pass Through

Abstract Hydroxylysyl-galactosyl-glucose (HGG) and hydroxylysyl-galactose (HG) were isolated from normal human urine and shown to be identical with hydroxylysine glycosides (OHLG's) whose structure had been elucidated in other laboratories. We devised a procedure for separating the OHLG's from many other urinary constituents by preliminary fractionation on a column of Sephadex. The OHLG's in the fractions so obtained were then isolated, uncontaminated with other ninhydrin-positive components, in a single pass through an analytical cation-exchange column equipped for splitting the effluent stream. In addition, a procedure was devised for determining as little as 10-9 mol of the OHLG's in 100 µl of filtrate (corresponding to 83.3 µl, of urine) on standard ion-exchange chromatographic amino acid analyzers. In normal adult urine, 1.5, µmol of each glycoside was present per 100 mg of creatinine; the molar ratio of HHG to HG was about 1.1 to 1.2. Each was present in plasma in about 400- to 500-fold smaller concentration than in urine. After surgical fusion of the spine, excretion of OHLG's increased and the ratio of HGG to HG decreased, changes we interpreted as indicating a more rapid bone-collagen turnover consequent to surgical damage.

Sequential extracts of human bone show differing collagen synthetic rates

2002 ◽  
Vol 30 (2) ◽  
pp. 61-65 ◽  
Author(s):  
J. Babraj ◽  
D.J. Cuthbertson ◽  
P. Rickhuss ◽  
W. Meier-Augenstein ◽  
K. Smith ◽  
...  
Keyword(s):  
Acetic Acid ◽  
Collagen Synthesis ◽  
Type I Collagen ◽  
Human Bone ◽  
Bone Collagen ◽  
Type I ◽  
Human Beings ◽  
Collagen Turnover ◽  
Bone Collagen Synthesis

Type I collagen is the major bone protein. Little is known quantitatively about human bone collagen synthesis in vivo, despite its importance for the understanding of bone formation and turnover. Our aim was to develop a method that could be used for the physiological and pathophysiological investigation of human bone collagen synthesis. We have carried out preliminary studies in patients undergoing hip replacement and in pigs to validate the use of the flooding dose method using 13C- or 15N-labelled proline and we have now refined our techniques to allow them to be used in a normal clinical or physiological setting. The results show that the application of a flooding dose causes bone free-proline labelling to equilibrate with that of blood in pigs and human beings, so that only 150 mg of bone will provide enough sample to prepare and measure the labelling of three fractions of bone collagen (dissolved in NaCl, acetic acid and pepsin/acetic acid) which have the same relative labelling (1.0:0.43:0.1) as measured by GC-combustion-isotope ratio MS. The rates of incorporation were substantially faster than in skeletal muscle samples taken at the same time. The results suggest that different fractions of human bone collagen turnover at markedly higher rates than had been previously considered. This approach should allow us to discover how growth and development, food, activity and drugs affect bone collagen turnover and to measure the effects on it of ageing and bone disease.

scholarly journals Redox Potential and Antioxidant Capacity of Bovine Bone Collagen Peptides towards Stable Free Radicals, and Bovine Meat Lipids and Proteins. Effect of Animal Age, Bone Anatomy and Proteases—A Step Forward towards Collagen-Rich Tissue Valorisation

Molecules ◽  
2020 ◽  
Vol 25 (22) ◽  
pp. 5422
Author(s):  
Laurent Aubry ◽  
Claude De-Oliveira-Ferreira ◽  
Véronique Santé-Lhoutellier ◽  
Vincenza Ferraro
Keyword(s):  
Antioxidant Activity ◽  
Free Radicals ◽  
Redox Potential ◽  
Antioxidant Capacity ◽  
Bone Age ◽  
Bone Collagen ◽  
Bovine Bone ◽  
Collagen Peptides ◽  
Stable Free Radicals ◽  
Effect Of Age

Collagen antioxidant peptides are being widely studied. However, no research has paid attention to biological parameters such as the age and anatomy of collagen-rich tissues, which can determine a change in tissue structure and composition, and then in bioactivity. Moreover, only few research works have studied and assessed peptides antioxidant activity on the food matrix. This work aimed to investigate the effect of bovine’s bone age and anatomy, and of six different enzymes, on the antioxidant activity of collagen peptides. Collagen was extracted from young and old bovine femur and tibia; six different enzymes were used for peptides’ release. The redox potential, the quenching of stable free radicals, and the antioxidant capacity on bovine meat lipids and proteins was evaluated, under heating from ambient temperature to 80 °C. Age and anatomy showed a significant effect; the influence of anatomy becomes most important with age. Each enzyme’s effectiveness toward age and anatomy was not the same. The greatest amount of peptides was released from young bones’ collagen hydrolysed with papain. The antioxidant activity was higher at higher temperatures, except for meat proteins. Assessing the effect of age and anatomy of collagen-rich tissues can promote a better application of collagen bioactive peptides.

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