Study of cartilage and bone layers of the bearing surface of the equine metacarpophalangeal joint relative to different timescales of maturation
M.R. van der HarstChris H.A. van de LestJeroen DeGrootGeesje H. KiersPieter A.J. BramaP. René van Weeren
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Abstract:
A detailed and comprehensive insight into the normal maturation process of the different tissues that make up functional units of the locomotor system such as joints is necessary to understand the influence of early training on musculoskeletal tissues.To study simultaneously the maturation process in the entire composite structure that makes up the bearing surface of a joint (cartilage, subchondral and trabecular bone) in terms of biochemical changes in the tissues of juvenile horses at 2 differently loaded sites of the metacarpophalangeal joint, compared to a group of mature horses.In all the structures described above developmental changes may follow a different timescale.Age-related changes in biochemical characteristics of the collagen part of the extracellular matrix (hydroxylysine, hydroxyproline, hydroxypyridinum crosslinks) of articular cartilage and of the underlying subchondral and trabecular bone were determined in a group of juvenile horses (n = 13) (Group 1, age 6 months-4 years) and compared to a group of mature horses (n = 30) (Group 2, >4 years). In both bony layers, bone mineral density, ash content and levels of individual minerals were determined.In cartilage, subchondral bone and trabecular bone, virtually all collagen parameters in juvenile horses were already at a similar (stable) level as in mature horses. In both bony layers, bone mineral density, ash- and calcium content were also stable in the mature horses, but continued to increase in the juvenile group. For magnesium there was a decrease in the juvenile animals, followed by a steady state in the mature horses.In horses age 6 months-4 years, the collagen network of all 3 layers within the joint has already attained a mature biochemical composition, but the mineral composition of both subchondral and trabecular bone continues to develop until approximately age 4 years.The disparity in maturation of the various extracellular matrix components of a joint can be assumed to have consequences for the capacity to sustain load and should hence be taken into account when training or racing young animals.Keywords:
Metacarpophalangeal joint
Hydroxyproline
Hydroxylysine
High serum levels of total hydroxyproline (Hyp) and hydroxylysine (Hyl) in patients with acute viral hepatitis were found to be due to a marked increase of the peptide-bound form of these aminoacids. The concentrations of free Hyp and Hyl were only slightly changed. The levels of serum Hyp and Hyl were higher in patients with bilirubin concentration, and decreased during recovery.
Hydroxylysine
Hydroxyproline
Viral Hepatitis
Serum bilirubin
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An increase in total (72.67-8.24 mumol/l) and free (14.14-1.97 mumol/l) hydroxyproline and total (7.16-0.72 mumol/l) and free (1.06-0.24 mumol/l) hydroxylysine was found in the serum of 30 patients with decompensated hepatic cirrhosis as compared to the values in 40 healthy subjects (48.70-5.89; 8.41-4.73; 4.34-2.71; 0.77-0.25 mumol/l, respectively). The results were not related to total serum protein concentration. The level of peptide-bound hydroxyproline and peptide-bound hydroxylysine was significantly higher in cirrhotic patients despite the decrease in serum protein content.
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The healing of myocardial infarction is accompanied by an increased accumulation of collagen in the heart muscle. Indexes of collagen metabolism (serum hydroxyproline, hydroxylysine and collagen-like protein concentration) were measured in 60 patients with myocardial infarction and 30 healthy blood donors. Determinations were carried out 1, 2, 3 days after admission and between the 10th-14th and 21st-25th day of the illness. It was found that hydroxyproline and hydroxylysine decreased in the first days of the disease, and subsequently increased in the course of the healing process accompanied by an increased collagen-like protein level. The changes did not depend on the total protein concentration.
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Protein metabolism
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The effect of protein deficiency on the urinary excretion of hydroxyproline (total, nondialysable, dialysable and free fractions) and hydroxylysyl glycosides (glucosyl-galactosyl-hydroxylysine, glc-gal-hyl and galactosyl-hydroxylysine, gal-hyl) was investigated in female albino rats.In comparison to controls, the protein deficient animals were found to excrete significantly decreased amounts of urinary hydroxyproline fractions from the 7th day onwards.The excretion of total hydroxylysyl glycosides in urine parallels the excretion of hydroxyproline.The urinary output of both glc-gal-hyl and gal-hyl was also appreciably lower in deficient animals.The normal ratio of glc-gal-hyl/gal-hyl found in the urine of protein deficient animals suggests that there is a similar decreased turnover of collagen in both bone and skin. Ausscheidung von Kollagen-Metaboliten im Harn bei Protein-MangelernährungZusammenfassung: Die Wirkung eines Proteinmangels auf die Ausscheidung von Hydroxyprolin (gesamtes, nicht dialysierbaies, dialysierbares und freies) und Hydroxylysyl-Glykosiden (Glucosyl-galaktosyl-hydroxylysin, Glc-Gal-Hyl und Galaktosyl-hydroxylysin, Gel-Hyl) im Harn wurde an weiblichen Albinoratten untersucht.Im Vergleich zu den Kontrollen schieden die Tiere mit Proteinmangel vom 7. Tage an signifikant niedrigere Mengen der Hydroxyprolinfraktionen im Harn aus.Die Ausscheidung der Gesamt-Hydroxylysylglykoside im Harn verlief parallel der Ausscheidung an Hydroxyprolin.Die Ausscheidung beider Glykosidfraktionen im Harn war bei den Tieren mit Proteinmangel ebenfalls beträchtlich niedriger.Das normale Verhältnis von Glc-Gal-Hyl zu Gal-Hyl
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1. The urinary peptides and amino acids have been examined in a 28-year-old female with osteomalacia and severe parathyroid bone disease. Forty ninhydrin positive substances were identified. 2. These substances included nine hydroxyproline containing peptides of relatively simple composition. Of these eight contained 4-hydroxyproline, two contained cis-3-hydroxyproline and one had trans-3-hydroxyproline. Two larger peptides which contained a high proportion of 4-hydroxyproline residues were also found. Free 4-hydroxyproline, free hydroxylysine and a hydroxylysine complex were found. 3. Of the remaining twenty-six substances, which may not be derived from collagen, alaninol is reported as an urinary constituent for the first time, six are less common but have been reported previously whilst the remaining nineteen are well-known urinary constituents. 4. The significance of these findings in relation to collagen breakdown is discussed.
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Hydroxyproline
Osteomalacia
Ninhydrin
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Hydroxylysine
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Hydroxyproline, hydroxylysine and proline were determined on skin from 18 patients with localized scleroderma (10 with localized morphoea plaque and 8 with generalized morphoea). Three skin biopsies (4mm punch) were obtained from each patient: One from the center of a sclerotic plaque, one from the perilesional area, and one (control) from unaffected skin of the same region. Clinically, the sclerosis was more pronounced (p less than 0.01) in localized morphoea plaque as compared to generalized morphoea. Patients with localized morphoea plaque had an increased concentration of hydroxylysine (p less than 0.01) and an increased ratio of hydroxylysine to hydroxyproline (p less than 0.01) in the plaques. Hydroxylysine concentration was not changed in patients with generalized morphoea. In the entire material, increased hydroxylysine concentration were related to shorter age of the plaques (p less than 0.05) and to advanced degree of sclerosis (p less than 0.05). The hydroxylysine and hydroxyproline content per mm2 skin surface, and the weight of the dried defatted biopsy cores were increased in sclerotic plaques (p less than 0.01) in localized as well as generalized morphoea. There were no changes in the hydroxyproline and proline concentrations in any of the groups. Specimens from perilesional area showed intermediate changes. The results were compared with selected cases of lichen sclerosis et atrophicus and atrophic skin diseases. The increase in hydroxylysine concentration and ratio to hydroxyproline indicate that patients with localized morphoea plaque contain an increased proportion of newly synthesized collagen in the fibrotic plaque.
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Hydroxyproline
Scleroderma (fungus)
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SUMMARY 1. Urinary levels of glycosaminoglycans (GAG) and hydroxyproline from normal and fluoride treated rabbits were estimated. The hydroxylysine content of serum and urine of rabbits after excessive ingestion of fluoride was also investigated. 2. There was a progressive decrease in GAG content, reduction in hydroxylysine, whereas the hydroxyproline content was increased after fluoride ingestion. 3. Enhanced hydroxyproline in urinary excretion is due to collagen breakdown after fluoride ingestion. 4. The reduction in hydroxylysine content is due to reduced collagen cross‐link formation. 5. The report suggests the possibility of using the urinary levels of GAG or hydroxyproline or hydroxylysine as an index of fluoride intoxication.
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Hydroxylysine
Hydroxyproline
Chronic liver disease
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Connective Tissue. XVI. Species Difference in Amino Acid Composition of Insoluble Collagen of Uterus
Insoluble collagen was prepared from the uteri of rat, guinea pig, rabbit, pig, cow, and human being, after extracting the salt- and acetic acid-soluble collagens. The insoluble collagen of uterus contained a significantly higher content of hydroxyproline and hydroxylysine than the soluble collagen from uterus. The highest content of hydroxyproline, 115 residue/1000 residues, was found in the insoluble collagen of rabbit uterus. The highest content of hydroxylysine, 16 residues/1000 residues, was found in rat uterine insoluble collagen.
Hydroxylysine
Hydroxyproline
Residue (chemistry)
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