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1.
Res Sports Med ; 24(3): 287-97, 2016.
Article in English | MEDLINE | ID: mdl-27379471

ABSTRACT

We investigated alternatives to commonly used biomarkers of exercise-induced tissue damage. Over 5 days following two bouts of 100 drop-to-vertical jumps (inter-bout rest period of 3 weeks), myosin heavy chain 1, hydroxylysine (HYL), hydroxyproline (HYP), spermine (SPM) and spermine synthase (SMS) were measured in the serum of 10 participants. HYL significantly increased from 5.92 ± 1.49 ng/mL to 6.48 ± 1.47 ng/mL at 24 h. A similar trend was observed for bout 2, but without reaching significance. SPM significantly increased only after bout 1 from 0.96 ± 0.19 ng/mL at pretest to a peak level of 1.12 ± 0.26 ng/mL at 24 h, while B2 increments remained non-significant. Myosin heavy chain 1, HYP and SMS values remained below the detection limit of the applied enzyme-linked immunosorbent assay (ELISA) kit. Though HYL and SM increased after the intervention, both markers showed a large standard deviation (SD) combined with small increments. Therefore, none of the investigated biomarkers provides a meaningful alternative to commonly used damage markers.


Subject(s)
Exercise/physiology , Muscle, Skeletal/pathology , Neutrophils , Adult , Biomarkers/blood , Humans , Hydroxylysine/blood , Hydroxyproline/blood , Leukocyte Count , Male , Myalgia/blood , Myalgia/etiology , Myosin Heavy Chains/blood , Spermine/blood , Spermine Synthase/blood , Young Adult
2.
Ukr Biochem J ; 87(1): 21-32, 2015.
Article in English | MEDLINE | ID: mdl-26036128

ABSTRACT

This review focuses on the analysis of diagnostic value of the major bone remodeling markers, in particular synthesis and degradation markers of collagen type I. These include carboxy- and aminoterminal telopeptide, carboxy- and aminoterminal propeptide of procollagen type I, hydroxyproline, hydroxylysine, pyridinoline and deoxypyridinoline. Their measurement allows evaluating the structural and functional conditions and also the rate of metabolic processes in the bone tissue. The advantages and disadvantages of determination of these markers in the condition of different bone diseases were examined. It is shown that determination of bone collagen type I metabolism markers is the most informative for assessment of bone resorption, formation and turnover.


Subject(s)
Bone Resorption/blood , Bone Resorption/urine , Bone and Bones/metabolism , Collagen Type I/metabolism , Procollagen/metabolism , Acid Phosphatase/metabolism , Alkaline Phosphatase/metabolism , Amino Acids/blood , Amino Acids/urine , Animals , Biomarkers/blood , Biomarkers/urine , Bone Density , Bone Resorption/pathology , Bone and Bones/pathology , Humans , Hydroxylysine/blood , Hydroxylysine/urine , Hydroxyproline/blood , Hydroxyproline/urine , Osteocalcin/metabolism , Peptide Fragments/blood , Peptide Fragments/urine
3.
J Agric Food Chem ; 56(17): 7790-5, 2008 Sep 10.
Article in English | MEDLINE | ID: mdl-18707117

ABSTRACT

Clinical studies have shown that collagen hydrolysate (CH) may be able to protect joints from damage, strengthen joints, and reduce pain from conditions like osteoarthritis. CH is a collection of amino acids and bioactive peptides, which allows for easy absorption into the blood stream and distribution in tissues. However, although various matrices have been studied, the absorption of specific amino acids from CH added to a fresh fermented milk product (FMP) was not studied. The primary objective of the present study was to compare the plasma concentrations of four representative amino acids from the CH (glycine, proline, hydroxyproline, and hydroxylysine) contained in a single administration of a FMP with that of a single administration of an equal amount of neat hydrolyzed collagen. These four amino acids were chosen because they have already been used as markers of CH absorption rate and bioavailability. This was a single-center, randomized open, and crossover study with two periods, which was performed in 15 healthy male subjects. The subjects received randomly and in fasted state a single dose of product 1 (10 g of CH in 100 mL of FMP) and product 2 (10 g of CH dissolved in 100 mL of water) separated by at least 5 days. After administration, the subjects were assessed for plasma concentrations of amino acids and for urine concentrations of hydroxyproline. After FMP administration, mean values of the maximal concentration (Cmax) of the four amino acids were greater than after ingredient administration (p < 0.05). This effect was related to an increased Cmax of proline (p < 0.05). In conclusion, because of their physicochemical characteristics, the fermentation process, and the great homogeneity of the preparation, this milk product improves the plasma concentration of amino acids from CH, that is, proline. The present study suggests an interesting role for FMP containing CH to improve the plasmatic availability of collagen-specific amino acids. Hence, this FMP product could be of potential interest in the management of joint diseases.


Subject(s)
Amino Acids/blood , Collagen/administration & dosage , Collagen/blood , Cultured Milk Products/chemistry , Diet , Collagen/chemistry , Cross-Over Studies , Glycine/blood , Humans , Hydrolysis , Hydroxylysine/blood , Hydroxyproline/blood , Kinetics , Proline/blood
4.
J Strength Cond Res ; 22(2): 490-6, 2008 Mar.
Article in English | MEDLINE | ID: mdl-18550965

ABSTRACT

The aim of the present study was to examine the effect of acute plyometric exercise on indices of muscle damage and collagen breakdown. Nine untrained men performed an intense bout of plyometric jumping exercises (experimental group) and nine men remained at rest (control group). Seven days before and 24, 48, and 72 hours after plyometric exercise or rest, several physiological and biochemical indices of muscle damage and two biochemical indices of collagen damage were determined. No significant changes in concentric and eccentric peak torque of knee extensors and flexors or flexion and extension range of motion were found after the plyometric exercise. Delayed-onset muscle soreness increased 48 hours after exercise. Creatine kinase increased 48 and 72 hours post exercise, whereas lactate dehydrogenase increased 24, 48, and 72 hours post exercise. Serum hydroxyproline increased 24 hours post exercise, peaked at 48 hours, and remained elevated up to 72 hours post exercise. Hydroxylysine (which was measured only before exercise and at 48 hours) was found increased 48 hours post exercise. No differences were found in any physiological or biochemical index in the control group. Intense plyometric exercise increased muscle damage, delayed-onset muscle soreness, and serum indices of collagen breakdown without a concomitant decrease in the functional capacity of muscles. Hydroxyproline and hydroxylysine levels in serum seem promising measures for describing exercise-induced collagen degradation. Coaches need to keep in mind that by using plyometric activities, despite the increased muscle damage and collagen turnover that follow, it is not necessarily accompanied by decreases in skeletal muscle capacity.


Subject(s)
Collagen/metabolism , Exercise/physiology , Muscle, Skeletal/metabolism , Adult , Biomarkers/blood , Creatine Kinase/blood , Humans , Hydroxylysine/blood , Hydroxyproline/blood , L-Lactate Dehydrogenase/blood , Lactic Acid/blood , Male , Physical Exertion/physiology , Time Factors , Torque
5.
Przegl Lek ; 58(6): 495-7, 2001.
Article in Polish | MEDLINE | ID: mdl-11816739

ABSTRACT

The resorption and osteogenesis equilibrium is commonly known basal condition of bone tissue homeostasis. For the purpose of bone turnover analysis in the group of good controlled diabetic patients without any diabetic complications basal biochemical parameters of osteogenesis and resorption were estimated. During low-calcium diet conditions both serum concentration and urine excretion of creatinine, hydroxyproline, hydroxylysine and uric acid were investigated. Serum alkaline phosphatase activity and oxalic acid urine excretion were also measured. As the result of the study the higher serum alkaline phosphatase activity and hydroksyproline urine excretion in type 1 diabetic patients as well as higher hydroxyproline and hydroxylysine urine excretion in type 2 diabetic patients were found.


Subject(s)
Bone Resorption/etiology , Diabetes Mellitus, Type 1/complications , Diabetes Mellitus, Type 1/metabolism , Diabetes Mellitus, Type 2/complications , Diabetes Mellitus, Type 2/metabolism , Alkaline Phosphatase/blood , Bone Resorption/diagnosis , Creatine/blood , Creatine/urine , Humans , Hydroxylysine/blood , Hydroxylysine/urine , Hydroxyproline/blood , Hydroxyproline/urine , Osteogenesis , Time Factors
7.
Clin Chem ; 45(5): 676-81, 1999 May.
Article in English | MEDLINE | ID: mdl-10222355

ABSTRACT

BACKGROUND: Serum-based biochemical markers of bone resorption may provide better clinical information than urinary markers because direct comparison with serum markers of bone formation is possible and because the within-subject variability of serum markers may be lower. We describe a method for the measurement of free beta-1-galactosyl-O-hydroxylysine (Gal-Hyl) in serum. METHODS: The assay used preliminary ultrafiltration of serum, dansylation, and separation by reversed-phase HPLC with fluorescence detection. Healthy subjects were recruited from population-based studies of bone turnover. RESULTS: The within-run (n = 15) and between-run (n = 15) CVs were 7% and 14%, respectively, at a mean value of 48 nmol/L. In women and pubertal girls, serum free Gal-Hyl correlated with urine free Gal-Hyl (r = 0.84; P <0.001). Serum Gal-Hyl was higher during puberty and increased after menopause. The fractional renal clearance of free Gal-Hyl relative to that of creatinine was 0.90 (95% confidence interval, 0.82-0.98). Serum free Gal-Hyl decreased by 36% (SE = 4%) in 14 patients with mild Paget disease treated with an oral bisphosphonate, and this decrease was significantly (P <0. 001) greater than that seen for either serum tartrate-resistant acid phosphatase (9%; SE = 4%) or serum C-terminal telopeptide of collagen I (19%; SE = 8%). CONCLUSION: Serum free Gal-Hyl may be useful as a serum marker of bone resorption.


Subject(s)
Bone Resorption/blood , Hydroxylysine/analogs & derivatives , Adolescent , Adult , Age Factors , Aged , Aged, 80 and over , Biomarkers/blood , Biomarkers/urine , Bone Resorption/urine , Child , Diphosphonates/therapeutic use , Female , Humans , Hydroxylysine/blood , Hydroxylysine/urine , Menopause , Middle Aged , Osteitis Deformans/drug therapy , Osteitis Deformans/urine , Puberty
8.
Pol Arch Med Wewn ; 96(6): 528-35, 1996 Dec.
Article in Polish | MEDLINE | ID: mdl-9139272

ABSTRACT

The aim of the study was determination of the influence of heart infarction on the blood serum level of type I procollagen carboxyterminal peptide (PICP) and its covariability with concentration of hydroxyproline (HP) and hydroxylysine (HL) as well as activity of creatine kinase (CK) and aspartate transferase (AspAT). The investigations were carried out in 30 patients with a heart infarction with Q wave (group I) and in 20 subjects with a heart infarction without Q wave. The control group comprised 30 healthy subjects. The determination of all parameters was performed on the 1st, 2nd, 3rd, 5th and 10th day after the infarct onset. On the 1st day of heart infarction, the concentration of PICP in serum was (x +/- SD): gr. I-235 +/- 33, gr. II-209 +/- 8, gr. C-65 +/- 17 micrograms/l. There was no co-variability of PICP concentration and the values of all other determined parametres. The authors conclude: 1. the increase of serum PICP concentration is connected probably with the magnitude of heart infarction, 2. the reconstruction process of the heart fibrous tissue and scar formation begins already on the first day of infarction onset, 3. during 10 days after infarction onset the serum PICP concentration does not correlate with HP, HL as well as the enzymatic heart infarct indices, namely CK and AspAT.


Subject(s)
Myocardial Infarction/blood , Peptide Fragments/blood , Procollagen/blood , Adult , Aged , Aspartate Aminotransferases/blood , Creatine Kinase/blood , Electrocardiography , Female , Humans , Hydroxylysine/blood , Hydroxyproline/blood , Male , Middle Aged , Myocardial Infarction/classification
9.
Clin Chim Acta ; 234(1-2): 101-8, 1995 Jan 31.
Article in English | MEDLINE | ID: mdl-7758208

ABSTRACT

Urinary galactosyl hydroxylysine/creatinine ratio (GHL) was used to assess rates of bone collagen degradation and the activity of the pagetic lesion as well as for monitoring the rate and degree of suppression of bone resorption over 1 year in patients treated with 30 mg of intravenous pamidronate for 3 consecutive days. The clinical utility of GHL was compared with that of urinary hydroxyproline/creatinine and deoxypyridinoline/creatinine and with bone isoenzyme of serum alkaline phosphatase. The results suggest that GHL is a quantitative marker of the activity of Paget's bone disease. GHL is less sensitive than hydroxyproline, deoxypyridinolone and bone alkaline phosphatase in monitoring treatment of Paget's disease. The assay of GHL is easier, faster and less costly than that of hydroxyproline or deoxypyridinoline and it can be easily standardized.


Subject(s)
Hydroxylysine/analogs & derivatives , Osteitis Deformans/blood , Adult , Aged , Aged, 80 and over , Alkaline Phosphatase/analysis , Alkaline Phosphatase/blood , Biomarkers/blood , Bone Resorption/physiopathology , Bone and Bones/enzymology , Chromatography, High Pressure Liquid , Creatinine/urine , Female , Humans , Hydroxylysine/blood , Hydroxyproline/urine , Isoenzymes/analysis , Isoenzymes/blood , Male , Middle Aged , Osteitis Deformans/enzymology , Spectrometry, Fluorescence
10.
Rom J Intern Med ; 32(4): 271-4, 1994.
Article in English | MEDLINE | ID: mdl-7613499

ABSTRACT

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.


Subject(s)
Hydroxylysine/blood , Hydroxyproline/blood , Liver Cirrhosis, Alcoholic/blood , Adult , Ascites/blood , Chronic Disease , Female , Humans , Male , Middle Aged
11.
Rom J Intern Med ; 31(2): 119-22, 1993.
Article in English | MEDLINE | ID: mdl-8268829

ABSTRACT

The variations of the serum markers of collagen metabolism such as total and free hydroxyproline and hydroxylysine and collagen-like protein were studied in patients with chronic bronchitis, pneumonia and emphysema as compared to healthy controls. The values found in diseased subjects were significantly higher than in controls.


Subject(s)
Collagen/blood , Respiratory Tract Diseases/blood , Aged , Biomarkers/blood , Bronchitis/blood , Chronic Disease , Female , Humans , Hydroxylysine/blood , Hydroxyproline/blood , Male , Middle Aged , Pneumonia/blood , Pulmonary Emphysema/blood
13.
Med Interne ; 22(2): 129-40, 1984.
Article in English | MEDLINE | ID: mdl-6330869

ABSTRACT

Collagen metabolism was studied in patients with viral hepatitis, chronic hepatic disorders as well as under experimental conditions, in rats with carbon tetrachloride-induced hepatic fibrosis. Changes in serum hydroxyproline, hydroxylysine and collagen-like protein levels, and collagen peptidase activity were observed in clinical investigations. An increase of collagen content and collagen-glycosaminoglycan interactions were found in the liver samples of rats with the hepatic fibrosis. An increase of collagenase activity in the course of fibrosis is due to an elevated biosynthesis of the enzyme de novo as well as to a decreased content of inhibitors. The activity of collagen peptidase and collagenolytic cathepsin were increased, and it was suggested that an increase of collagen degradation in the liver was a self-defensive mechanism against fibrosis but insufficient to protect the organ against it. This was caused probably by changes in susceptibility of collagen to degradating enzymes in the course of chronic hepatic disorders.


Subject(s)
Collagen/metabolism , Liver Diseases/metabolism , Adult , Aged , Animals , Carbon Tetrachloride Poisoning/metabolism , Carcinoma, Hepatocellular/metabolism , Female , Hepatitis, Viral, Human/metabolism , Humans , Hydroxylysine/blood , Hydroxyproline/blood , Liver Cirrhosis/metabolism , Liver Neoplasms , Male , Microbial Collagenase/biosynthesis , Middle Aged , Rats
14.
Acta Physiol Pol ; 34(5-6): 507-9, 1983.
Article in English | MEDLINE | ID: mdl-6679986

ABSTRACT

In 38 male and 42 female healthy subjects serum concentrations of free and peptide-bound hydroxylysine were determined. There were no statistically significant differences between men and women.


Subject(s)
Hydroxylysine/blood , Adult , Blood Proteins/metabolism , Female , Humans , Male , Protein Binding , Reference Values , Sex Factors
16.
Cor Vasa ; 24(5): 339-44, 1982.
Article in English | MEDLINE | ID: mdl-7172687

ABSTRACT

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.


Subject(s)
Carrier Proteins , Collagen/metabolism , Myocardial Infarction/metabolism , Proteins , Adult , Aged , Blood Proteins , Humans , Hydroxylysine/blood , Hydroxyproline/blood , Middle Aged , Time Factors
17.
Acta Biol Med Ger ; 39(2-3): 287-93, 1980.
Article in English | MEDLINE | ID: mdl-7424348

ABSTRACT

Adult rats were given water with sodium fluoride (10 mg/l) during 7 weeks before pregnancy, during pregnancy and after the delivery. The born rats were treated in the same manner and were investigated 1, 2, 4 and 6 months after birth. It was found that exposure to sodium fluoride stimulated an increase of hydroxyproline and hydroxylysine concentration in serum and the urinary excretion of these catabolites. A decrease of soluble and insoluble collagen was shown in skin and lungs of exposed animals as compared with controls. The decrease of collagen in tissues was not age-dependent.


Subject(s)
Collagen/metabolism , Fluorides/pharmacology , Lung/metabolism , Skin/metabolism , Sodium Fluoride/pharmacology , Aging , Animals , Hydroxylysine/blood , Hydroxylysine/urine , Hydroxyproline/blood , Hydroxyproline/urine , Rats , Water Supply
19.
Med Interne ; 16(1): 79-82, 1978.
Article in English | MEDLINE | ID: mdl-635409

ABSTRACT

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.


Subject(s)
Hepatitis, Viral, Human/blood , Hydroxylysine/blood , Hydroxyproline/blood , Acute Disease , Adult , Bilirubin/blood , Female , Humans , Male , Middle Aged
20.
Clin Chim Acta ; 76(1): 41-53, 1977 Apr 01.
Article in English | MEDLINE | ID: mdl-856503

ABSTRACT

Free hydroxylysine and hydroxylysing glycosides were separated from urine and serum extracts on cation exchange resin and assayed spectrophotometrically. The method in conjunction with gel filtration in Bio-Gel P2 allowed to separate from urine also polypeptide hydroxylysine and hydroxylysine bound in small molecules of neutral or acidic character. Glycosylgalactosylhydroxylysineand galactosylhydroxylysine were separated by partition and/or ion exchange chromatography. Patients with chronic renal insufficiency had elevated serum levels and urinary excretion of hydroxylysine glycosides with increased excretion of hydroxylysine bound in polypeptides and in small molecules of neutral or acidic character. The excretion of free hydroxylysine was often within normal limits. When compared to values found in normal growing subjects and in adult patients with increased bone turnover and normal renin function the urinary excretion of hydroxylysine glycosides in chronic uremia was more markedly increased than excretion of hydroxyproline polypeptides and total hydroxyproline.


Subject(s)
Hydroxylysine/metabolism , Uremia/metabolism , Bone Diseases/metabolism , Chemical Fractionation , Chronic Disease , Collagen/metabolism , Glycosides , Humans , Hydroxylysine/blood , Hydroxylysine/urine
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