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At least 19 recordsLinked to original sources
PubMed1976

[Animal experiments on the relationship between urinary excretion of hydroxyproline and serum hydroxyproline fractions].

Hydroxyproline excreted withh the urine and the free and peptide-bound hydroxyproline in the serum originate from collagen catabolism in the connective tissue. The relation of protein-bound hydroxyproline in the serum to the collagen metabolism is still contradictory. In normal and lathyritic rats the time dependent changes of specific hydroxyproline activity in the urine and serum after intraperitoneal application of C-14-proline were determined. In normal rats the main part of hydroxyproline excreted in urine and of the protein-bound hydroxyproline in serum have corresponding half-life periods of 0,6-0,7 days and co-ordinate with the neutral salt soluble collagen. Also in lathyritic rats with their increased amount of neutral salt soluble collagen due to an increase collagen synthesis and a retarded transition from soluble to insoluble collagen these two parameters of collagen metabolisms are in agreement.

Animals↗
PubMed1975

Sequence position of 3-hydroxyproline in basement membrane collagen. Isolation of glycyl-3-hydroxyprolyl-4-hydroxyproline from swine kidney.

The position of 3-hydroxyproline was investigated in the triplet sequences of peptides released by collagenase digestion of a collagen preparation from kidney cortex. Composition of the collagen preparation indicated that it was largely or wholly of basement membrane origin. 3-Hydroxyproline was detected in only one sequence, the tripeptide, glycyl-3-hydroxyprolyl-4-hydroxyproline, which accounted for a major fraction of the total 3-hydroxyproline obtained in the peptides released by collagenase. Preliminary data, based on sequencing the peptide mixture released by collagenase treatment, suggested that, in contrast, 4-hydroxyproline occurs predominantly if not exclusively in the Y position of Gly-X-Y triplet sequences in the collagen preparation studied.

Amino Acid Sequence↗
PubMed1979

Fractionation and structure of several hydroxyproline-containing urinary peptides, with special reference to some 3-hydroxyproline-containing peptides.

After a preliminary separation of the hydroxyproline-containing peptides on Biogel P 2, the largest peptides are fractionated on phosphocellulose and the smallest ones on QAE-Sephadex. The fractions obtained from QAE-Sephadex are subfractionated on a column of Dowex 50-M-82. The total number of hydroxyproline-containing peptides from human urine is not less than 78. Sixteen di, tri and pentapeptides have been purified, their N-terminal amino acids and amino acid compositions determined and a structure is proposed. 3 of these peptides contain 3-hydroxyproline and one of these 3 peptides probably originates from basement membrane collagen.

Chromatography, Ion Exchange↗
PubMed1975

Determination of hydroxyproline polypeptides in urine and blood serum by gel filtration.

Hydroxyproline-containing polypeptides were isolated from urine by filtration on polyacrylamide gel Bio-Gel P-2. This fraction was quantitatively and qualitatively similar to the nondialysable hydroxyproline in urines of normal adult subjects, patients with chronic uremia, and with primary or secondary hyperparathyroidism. Hydroxyproline polypeptides isolated from urines of patients with extensive Paget's disease or from normal growing subjects contained a group of smaller polypeptides slightly retarded on Bio-Gel P-2 which were not retained by the dialysis membrane Spectrapor-TM. In these two groups of subjects the values of hydroxyproline polypeptides were 35-45 percent higher than those of dialysable hydroxyproline. Increased excretion of hydroxyproline polypeptides was found in chronic uremia, primary and secondary hyperparathyroidism, Paget's bone disease and in normal growing subjects. With the notable exception of chronic uremia the excretion of hydroxyproline polypeptides paralleled that of total and oligopeptidic hydroxyproline. In some cases of chronic uremia the polypeptidic hydroxyproline represented the predominant fraction. On long columns of Bio-Gel P-6 hydroxyproline polypeptides separated into several peaks. The chromatographic pattern was rather characteristic for chronic uremia, secondary hyperparathyroidism, Paget's bone disease and physiological growth. Ahydroxyproline fraction of similar chromatographic properties was isolated from blood serum after deproteinisation with heat or ethanol at pH 4.8. High serum levels of this hydroxyproline fraction were observed in pathological conditions with increased urinary excretion of polypeptidic and nondialysable hydroxyproline.

Adenoma↗
PubMed1978

3-Hydroxyproline content of normal urine.

Values for total 3-hydroxyproline and 4-hydroxyproline were obtained from 24-h urine specimens of 18 healthy human subjects of both sexes, whose ages ranged from the first to the sixth decade in age. Urinary 3-hydroxyproline levels, not earlier described to our knowledge, were determined by an isotope-dilution method requiring considerable purification and utilizing the amino acid analyzer for final measurement. 3-Hydroxyproline averaged 3% of the corresponding 4-hydroxyproline in individual urine samples. Like 4-hydroxyproline, 3-hydroxyproline excretion is increased in the second decade, and there is generally good correlation between the two values in individual urines. A hydroxyprolinemic subject excreting greatly elevated 4-hydroxyproline levels did not excrete excessive 3-hydroxyproline, consistent with independent catabolic pathways for the two compounds. 3-Hydroxyproline appears to be selectively excreted relative to 4-hydroxyproline when compared with the probable total body content of each amino acid. Possible explanations are: a more rapid turnover of basement membrane collagen than interstitial collagen or, alternatively, relatively greater resistance to the proteolytic cleavage of peptides containing 3-hydroxyproline.

Adolescent↗
PubMed1976

Bound hydroxyproline excretion following gelatin loading in prolidase deficiency.

The excretion of peptide-bound hydroxyproline before and after gelatin loading was evaluated in two children with prolidase deficiency, two adult heterozygotes, and normal controls. On a low hydroxyproline diet, the patients with prolidase deficiency excreted 6.9 and 2.4 times more bound hydroxyproline than normal children. The bound hydroxyproline excretion for the heterozygotes was comparable to the adult controls. Children ingested 20 g of gelatin and adults 29 g. In the 24 hr following gelatin loading, the homozygotes excreted 14.4 and 17.3 times more of the ingested load of hydroxyproline than did normal children. This constituted 39% and 47% of the hydroxyproline ingested. Of the hydroxyproline excreted in 24 hr, 58%, and 61.4% was excreted in the first 6 hr. Over the 24 hr period, the normal children excreted 2.7% of the hydroxyproline ingested (97.8% in the first 6 hr). The heterozygotes excreted only slightly more than the adult controls. The normal adults excreted 6.0% of the ingested hydroxyproline (82.8% in the first 6 hr). In prolidase deficiency, large amounts of peptide-bound hydroxyproline can cross the intestinal wall unhydrolyzed. Prolidase appears to have an important role in normal hydrolysis of peptide-bound hydroxyproline.

Adult↗
PubMed1979

Serum and synovial fluid hydroxyproline fractions in microcrystalline arthritis and osteoarthritis.

Synovial fluid and serum hydroxyproline fractions were investigated in patients with osteoarthritis and microcrystalline arthritis. Synovial fluid dialysable hydroxyproline levels are higher than serum levels in both conditions. Synovial fluid total and dialysable hydroxyproline are higher in microcrystalline arthritis than in osteoarthritis, while non-dialysable hydroxyproline values are similar in both conditions. In microcrystalline arthritis, synovial fluid dialysable hydroxyproline and polymorphonuclear leukocyte counts closely parallel each other. Irrespective of the type of arthropathy, synovial fluid dialysable hydroxyproline levels correlate with urinary hydroxyproline excretion. While the data suggest overproduction of dialysable hydroxyproline by joints in both conditions, the overproduction appears to be mediated by polymorphonuclear leukocytes in microcrystalline arthritis only. The ratio of serum to synovial total hydroxyproline are further suggestive of a possible differentiation between osteoarthritis and microcrystalline arthritis. In the conditions governing the present study, urinary hydroxyproline may be used as an index of joint tissue collagen resorption. Finally the significance of synovial fluid and serum non-dialysable hydroxyproline is discussed.

Chondrocalcinosis↗
PubMed1977

Total hydroxyproline in urine of 4 to 6 year-old children--an investigation on its relationship to growth and nutrition.

We analysed over a period of 30-32 days the daily total hydroxyproline and creatinine excretine in urine from 9 healthy, normally fed 4 to 6 year-old children (2 girls, 7 boys). The average urinary hydroxyproline excretion was 45.6 mg/24 hr, with a coefficient of variation of 25.6%. Urinary hydroxyproline for individual children showed distinct differences from day to day, which were independent of urine volume. There were significant differences between the mean values for urine hydroxyproline in individual children, which were independent of age. The average creatinine in urine was 346/24 hr with a coefficient of variation of 17.7%. The hydroxyproline-index did not define the nutritional state of these normally developed children on a normal diet. Dietary hydroxyproline contributed 7.4% to the total urinary hydroxyproline in our investigation. There was a close correlation between urine hydroxyproline excretion and growth velocity in each child.

Child↗
PubMed1979

The clinical measurement of urinary total hydroxyproline excretion.

The effect of dietary control on the day-to-day variation in total hydroxyproline excretion has been examined in two studies. In the first, a normal volunteer ate a controlled diet containing varying gelatin supplements for several weeks. In the second, the effect of removing hydroxyproline-containing foods from the diets of 8 volunteers was examined. Both studies confirm that the day-to-day variation in total hydroxyproline excretion falls when the gelatin content of the diet is decreased, whether the results are expressed as total hydroxyproline excretion rate or as the total hydroxyproline: creatinine ratio. This fall in variation takes place within 24 h of dietary control beginning and therefore longer periods of dietary restrictions to achieve optimum precision in the measurement of total hydroxyproline are unnecessary. For some analytical methods, results are better expressed as the ratio total hydroxyproline:creatinine than as the total hydroxyproline excretion rate.

Adult↗
PubMed1979

Hydroxyproline metabolism in type II hyperprolinaemia.

Hydroxyproline metabolism was studied in two patients with type II hyperprolinaemia (HP II) using oral loadings of hydroxyproline or hydroxyproline-ornithine. delta 1-pyrroline-3-hydroxy-5-carboxylic acid (3 OH-PC) and delta 1-pyrroline-5-carboxylic acid (PC) were identified in the urine. The urinary excretion of both 3-OH-PC and PC increased in HP II patients but not in healthy controls during oral loading of hydroxyproline and hydroxyproline-ornithine. The plasma level of proline in patients with HP II is very high but the hydroxyproline concentration is normal or only slightly increased. Therefore one can assume that hydroxyproline is converted to pyrrole-2-carboxylic acid, which is excreted in urine as a glycine conjugate. In this study it was demonstrated that the highly elevated plasma level of proline in one of the patients with HP II decreased greatly after hydroxyproline-ornithine load; this change was followed by a 40-fold rise in urinary excretion of proline.

Adolescent↗
PubMed1977

Effect of mithramycin on hydroxyproline metabolism in Paget's disease.

Hydroxyproline was measured in the plasma and urine of six patients with symptomatic osseous Paget's disease before and after parenteral mithramycin treatment. The plasma profile data included free, peptide, and protein hydroxyproline values. Corresponding urine samples were analyzed for total hydroxyproline content and, in some instances, for free hydroxyproline. Plasma values of free and peptide hydroxyproline fell promptly toward the range of normal within 24 hr after the first intravenous injection of mithramycin. Protein hydroxyproline in the plasma was slightly but significantly lower than in the 15 normal control subjects, and this value did not change appreciably over the 4-day period during which the patients were treated. The urine excretion rate of total hydroxyproline decreased precipitously. Our results support the hypothesis that mithramycin rapidly reduces the accelerated rate of "collagenolytic" activity of osteocytes and osteoclasts in this disorder, presumably by an inhibiting effect on these bone-modeling cells. The major degradative lesion, as reflected in the plasma and urine, is characterized by the production of non-TCA-precipitable peptides containing hydroxyproline, which rapidly fell to normal levels after the administration of mithramycin.

Humans↗
PubMed1977

Hydroxyproline fractions in serum and urine of rats during wound healing.

Total hydroxyproline in urine and free hydroxyproline, free and peptide hydroxyproline and protein bound hydroxyproline in serum are measured during wound healing in rats. The free and free+peptide fractions vary in concert with each other and with urine hydroxyproline. Protein bound hydroxyproline fractions take a very different course and behave as an acute phase reactant. The results suggest that protein bound hydroxyproline does not mirror collagen turnover but may be more relevant to C1q or complement metabolism.

Animals↗
PubMed1978

[Analysis of the hydroxyproline containing serum proteins in connective tissue diseases (author's transl)].

The serum proteins were fractionated on Sephadex G 200, their hydroxyproline content determined. Three protein peaks (I-III) containing different hydroxyproline concentrations could be separated. In connective tissue disorders accompanied by increased collagen synthesis or collagen degradation, an elevation of hydroxyproline was found in peak II. An increase of hydroxyproline always was associated with an increase of the serum proteins in the same fractions. Hydroxyproline serum levels above normal obviously are due to a certain capacity of the serum proteins binding free hydroxyproline and collagen metabolites.

Blood Proteins↗
PubMed1976

Relevance of hydroxyproline excretion to bone metastasis in breast cancer.

In 181 consecutive patients with breast cancer, urinary hydroxyproline excretion has been critically evaluated in conjunction with clinical, biochemical, radiological and scintigraphic parameters. The urinary hydroxyproline/creatinine ratio is a sensitive index of the presence of bone metastases. Urinary hydroxyproline excretion is a reliable method of selecting those patients whose elevated serum alkaline phosphatase is secondary to bone disease rather than liver idsease. The estimation of hydroxyproline excretion furthermore gives information on the activity of bone metastasis, and its response to treatment, which cannot be given by radiological or scintigraphic methods. It is doubtful whether urinary hydroxyproline estimation will help to detect bone metastases before they are apparent on scintigrams. When the bone scan is doubtful, as often occurs in older subjects, hydroxyproline excretion has been found to be helpful in classifying the patient. When scintigraphy is not available, an elevation of hydroxyproline excretion, together with an elevation of Ca/cr ratio or alkaline phosphatase activity, may pre-date by several months the radiological demonstration of osseous metastases.

Adult↗