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At least 19 recordsLinked to original sources
PubMed1985

Hydroxyproline metabolism by the rat kidney: distribution of renal enzymes of hydroxyproline catabolism and renal conversion of hydroxyproline to glycine and serine.

The metabolism of hydroxyproline by the rat kidney leads to the production of significant quantities of both glycine and serine. This process was observed in both the isolated perfused kidney and in isolated cortical tubule suspensions. The rate of hydroxyproline metabolism was increased in both preparations by the addition of alanine. The distribution of hydroxyproline oxidase, hydroxyoxoglutarate aldolase and alanine-glyoxalate transaminase were determined in detail. All three enzymes were found exclusively in the renal cortex where they were restricted to the mitochondria. Cortical tubule fractionation studies indicated that the enzymes are located in the proximal convoluted and proximal straight segments at the nephron. The results suggest that hydroxyproline degradation could contribute significantly to the renal synthesis of serine.

Alanine Transaminase↗
PubMed1989

Urinary hydroxyproline and hydroxylysine excretions in relation to hepatic hydroxyproline content in chronic liver disease.

In patients with or without various chronic liver diseases, the total urinary excretion of hydroxyproline and hydroxylysine and the hepatic content of hydroxyproline were examined. In 7 patients without liver disease, the urinary excretion of hydroxyproline and hydroxylysine were 10.3 +/- 1.5 and 1.31 +/- 0.21 mmol/mol creatinine, respectively, and the hepatic content of hydroxyproline was 4.9 +/- 0.6 mumol/g of wet liver. In 33 patients with liver disease, the urinary excretion of hydroxyproline and hydroxylysine and the hepatic content of hydroxyproline were increased in proportion to the severity of liver disease. The hepatic content of hydroxyproline showed a significant correlation with the urinary excretion of hydroxyproline and hydroxylysine (r = +0.406 and r = +0.531, respectively). These results suggest that the study of urinary hydroxyproline and hydroxylysine excretion may yield useful information on the metabolism of hepatic collagen in chronic liver disease. Moreover, urinary hydroxylysine excretion seemed to be a better index of hepatic collagen metabolism than urinary hydroxyproline excretion; perhaps urinary hydroxylysine excretion is not much affected by dietary collagen intake.

Adult↗
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↗
PubMed1988

Effects of dietary NaCl supplementation on bone synthesis of hydroxyproline, urinary hydroxyproline excretion and bone 45Ca uptake in the rat.

High sodium chloride intakes are regarded as a risk factor for osteoporosis because they increase the obligatory urinary calcium loss and stimulate parathyroid activity. Sodium chloride loads induce osteopenia in the rat. The effect could be due to a decrease in bone formation or a rise in bone resorption. Two experiments were undertaken to study the effects of dietary NaCl supplementation on 3H-hydroxyproline synthesis and 45Ca uptake in femoral bone. Salt-treated rats excreted 1.7 times more total urinary hydroxyproline (P less than 0.001) and 2.1 times more recently labelled 3H-hydroxyproline than controls (P less than 0.02) but they did not accumulate less 3H-hydroxyproline or less 45Ca in their bones than controls. These results indicate that salt-mediated osteopenia is due to an increase in bone resorption, rather than to a decrease in bone formation.

Animals↗
PubMed1988

Structural and functional changes in lung tissue of mice fed with beta-aminopropionitrile fumarate, L-3-cis-hydroxyproline, and L-4-cis-hydroxyproline.

Structural and functional changes in lung tissue of mice fed with beta-aminopropionitrile fumarate, L-3-cis-hydroxyproline, and L-4-cis-hydroxyproline. We fed 0.1% solutions of 3-cis-hydroxyproline (3cisHP), 4-cis-hydroxyproline (4cisHP) or beta-aminopropionitrile fumarate (beta APN) to 5-week-old mice for 1 month and studied the effect of each of these substances on the lung function and structure. Compared to control animals the compliance of the respiratory system in the mean was increased by 3-15% in the mice fed beta APN or 3cisHP, and decreased by 2-8% in the mice fed 4cisHP. On electron microscopial examination no overt morphological changes were detectable although as proven by biochemical analysis 3cisHP and 4cisHP were incorporated into the collagen of the mice who received these substances. We conclude that the effect of substances interfering with the normal production of collagen molecules depends on the kind of collagen affected and on the rate of collagen turnover.

Aminopropionitrile↗
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↗
PubMed1985

High-performance liquid chromatographic analysis of free hydroxyproline and proline in blood plasma and of free and peptide-bound hydroxyproline in urine.

A rapid, accurate and sensitive method for the determination of free hydroxyproline and proline in plasma and of total hydroxyproline in urine has been developed. Free imino acids and internal standard are extracted from plasma by trichloroacetic acid precipitation of protein and they are selectively derivatized with 4-chloro-7-nitrobenzofurazan, after reaction of the acid extract with o-phthalaldehyde. The highly fluorescent adducts of imino acids are separated on a Spherisorb ODS 2 reversed-phase column using acetonitrile-0.1 M sodium phosphate buffer, pH 7.2 (9:91, v/v) as mobile phase, followed by fluorometric detection. Total hydroxyproline determination in urine hydrolysates is carried out by reaction of the imino acid with 4-chloro-7-nitrobenzofurazan after clean-up on a Sep-Pak C18 cartridge of the o-phthalaldehyde-treated sample, high-performance liquid chromatographic separation and fluorometric quantitation of the derivative.

Chromatography, High Pressure Liquid↗