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At least 19 recordsLinked to original sources
PubMed1975

Urinary excretion of free hydroxylysine, peptide-bound hydroxylysine and hydroxylysyl glycosides in physiological conditions.

The amount of urinary hydroxylysine is an index of collagen metabolism. Of the total hydroxylysine measured in normal urine 80 percent is associated with sugars in two glycosidic compounds, glucosyl-galactosyl-hydroxylysine and galactosyl-hydroxylysine, ten percent is free and unglycosylated and the remainder is bound to urinary peptides. The excretion of hydroxylysyl glycosides follow the same physiological variations as urinary hydroxyproline, but it is not influenced by a collagen-free diet. The urinary excretion of hydroxylysyl glycosides, free hydroxylysine and peptide-bound hydroxylysine increases from 6 months of age to puberty. When corrected for urinary creatinine excretion, the largest amounts are found before one year of age. The glucosyl-galactosyl-hydroxylysine/galactosyl-hydroxylysine ratio is lower in the urine of children. After correction of the values to either the body surface area or to the creatinine excretion, no significant differences can be found between the sexes. The different forms of hydroxylysine are discussed.

Adolescent↗
PubMed1978

A method for measuring hydroxylysine and glycosylated hydroxylysines in urine and protein hydrolysates.

A method for measuring hydroxylysine and glycosylated hydroxylysines is described, based on the separation of the 3 compounds by ion-exchange chromatography, followed by spectrophotometric analysis of the hydroxylysine present as glucosylgalactosylhydroxylysine, galactosylhydroxylysine and free hydroxylysine. The method does not require prior preparation of the urine sample nor the use of high-resolution ion-exchange systems. The method is applicable to the determination of the glycosylated hydroxylysine and hydroxylysine content of urine or alkaline hydrolysates of proteins.

Chromatography, Ion Exchange↗
PubMed1979

Urinary excretion of hydroxyproline, hydroxylysine and hydroxylysine glycosides by patients with Paget's disease of bone and carcinoma with metastases in bone.

Patient's with carcinoma metastases in bone and Pagent's disease of bone have different patterns of collagen metabolite excretion. Both forms of bone disease resulted in an increased excretion of total hydroxyproline and the ratio of glucosylgalactosylhydroxylsine to galactosylhydroxylysine was below normal. The excretion of glucosylgalactosylhydroxylysine and galactosylhydroxylysine was increased in all patients with carcinoma metastases in bone while the excretion of glucosylgalactosylhydroxylysine in patients with Paget's disease. The ratio of total hydroxylysine (free hydroxylysine + glycosylated hydroxylysines) to total hydroxyproline was normal in patients with carcinoma metastases in bone and below normal in patients with Paget's disease bosne. The pattern of urinary collagen metabolite excretion is a more specific indicator of the presence of bone disease than is the measurement of the excretion rate of any individual collagen metabolite. Bone diseases of different etiologies may result in different patterns of urinary collagen metabolite excretion.

Bone Neoplasms↗
PubMed1965

Replacement of Lysine by Hydroxylysine and Its Effects on Cell Lysis in Streptococcus faecalis.

Shockman, Gerald D. (Temple University, Philadelphia, Pa.), J. Stuart Thompson, and Margaret J. Conover. Replacement of lysine by hydroxylysine and its effects on cell lysis in Streptococcus faecalis. J. Bacteriol. 90:575-588. 1965.-Hydroxylysine was not significantly incorporated by Streptococcus faecalis ATCC 9790 or 8043 until exponential growth ceased as a result of lysine exhaustion. Uptake was then rapid and virtually complete within 1 hr. Lysine absence, rather than physiological age, seemed to be the governing factor. Hydroxylysine uptake rapidly reached a peak in the acid-soluble fraction, suggesting a precursor role for substances in this fraction. Substitution of hydroxylysine for lysine was much more efficient in mucopeptide synthesis than in protein synthesis. In wall medium, less than 1% of the incorporated hydroxylysine was found in the protein fraction. Addition of lysine to both growth and wall media inhibited both further hydroxylysine uptake and transfer of hydroxylysine from acid-soluble to mucopeptide or protein fractions. Hydroxylysine resulted in decreased penicillin susceptibility only after it was postexponentially incorporated. This effect was physiologically similar to that seen after threonine deprivation or chloramphenicol treatment. Hydroxylysine incorporation increased resistance to autolysis, but failed to decrease lysozyme susceptibility when measured after heat inactivation of autolysis. Electron microscopy of negatively stained cells showed increased thickness of cell walls containing hydroxylysine. Thus, most of the effects of replacement of lysine by hydroxylysine resemble those seen after deprivation of a nonwall amino acid (e.g., threonine or valine) or after chloramphenicol treatment. Each of these conditions results in inhibition of protein synthesis while permitting cell-wall synthesis to continue, resulting in autolysis-resistant, thick-walled cells.

Journal Article↗
PubMed1998

3-Hydroxylysine, a potential marker for studying radical-induced protein oxidation.

gamma-Irradiation of several amino acids (Val, Leu, Ile, Lys, Pro, and Glu) in the presence of O2 generates hydroperoxides. We have previously isolated and characterized valine and leucine hydroperoxides, and hydroxides, and have detected these products in both isolated systems [e.g., bovine serum albumin (BSA) and human low-density lipoprotein (LDL)] and diseased human tissues (atherosclerotic plaques and lens cataractous proteins). This work was aimed at investigating oxidized lysine as a sensitive marker for protein oxidation, as such residues are present on protein surfaces, and are therefore likely to be particularly susceptible to oxidation by radicals in bulk solution. HO* attack on lysine in the presence of oxygen, followed by NaBH4 reduction, is shown to give rise to (2S)-3-hydroxylysine [(2S)-2,6-diamino-3-hydroxyhexanoic acid], (2S)-4-hydroxylysine [(2S)-2,6-diamino-4-hydroxyhexanoic acid], (2S, 5R)-5-hydroxylysine [(2S,5R)-2,6-diamino-5-hydroxyhexanoic acid], and (2S,5S)-5-hydroxylysine [(2S,5S)-2,6-diamino-5-hydroxyhexanoic acid]. 5-Hydroxylysines are natural products formed by lysyl oxidase and are therefore not good markers of radical-mediated oxidation. The other hydroxylysines are however useful markers, with HPLC analysis of 9-fluorenylmethyl chloroformate (FMOC) derivatives providing a sensitive and accurate method for quantitative measurement. Hydroxylysines have been detected in the hydrolysates of peptides (Gly-Lys-Gly and Lys-Val-Ile-Leu-Phe) and proteins (BSA and histone H1) exposed to HO./O2, and subsequently treated with NaBH4. Quantification of the hydroxylysines yields, and comparison with hydroxyvalines and hydroxyleucines, supports the hypothesis that surface residues give higher yields of oxidized products than the hydrophobic leucines and valines, at least with globular proteins such as BSA. Hydroxylysines, and particularly 3-hydroxylysine, may therefore be sensitive and useful markers of radical-mediated protein oxidation in biological systems.

Amino Acids↗
PubMed1981

Comparable content of hydroxylysine-linked glycosides in subcomponents C1q of the first component of human, bovine and mouse complement.

The hydroxylysine-glycosides in bovine and mouse C1q are directly quantified in parallel with those in human C1q after the alkaline hydrolysis of these molecules. Human, bovine and mouse C1q contain 68.3, 66.3 and 64.0 hydroxylysine-galactosylglucose residues in each of these molecules respectively. Only human C1q contains 2.5 residues of hydroxylysine-galactose per molecule, and both of bovine and mouse C1q contain no detectable hydroxylysine-monosaccharides in their molecules. The percentage of hydroxylysine residues glycosylated to total hydroxylysine residues in each of these molecules is calculated to be 86.4, 92.0 and 95.1% for human, bovine and mouse C1q respectively and is comparable with each other. The percentages of hydroxylysine residues resistant to periodate oxidation to total hydroxylysine residues in these molecules were 61.1, 65.3 and 74.3% for human, bovine and mouse C1q respectively and were significantly lower than those estimated by the direct quantification of hydroxylysine-glycosides after the alkaline hydrolysis of these molecules.

Animals↗
PubMed1972

Reducible crosslinks in hydroxylysine-deficient collagens of a heritable disorder of connective tissue.

Reducible compounds that participate in crosslinking were analyzed in hydroxylysine-deficient collagens of patients with a heritable disorder of connective tissue. After treatment with [(3)H]sodium borohydride, new compounds, as well as a totally different pattern of tritiated compounds, were found in hydroxylysine-deficient collagen from skin as compared with age-matched controls. The amount of desmosines detected indicated that more elastin was present in abnormal skin than in control skin.Bone collagen, which was not as deficient in hydroxylysine as skin collagen, had the same compounds as normal bone collagen, but their relative proportions were altered, consistent with a deficiency of hydroxylysine, a precursor of the crosslinks. Although the content of hydroxylysine in collagen of cartilage is essentially normal in these patients, analysis after reduction revealed a different pattern of reduced compounds from that of normal cartilage. It is speculated that Type II collagen, the major collagen component in cartilage, contains a normal amount of hydroxylysine, while Type I collagen, which is the major source of the crosslinks, is hydroxylysine-deficient. This distribution would explain the findings of an abnormal profile of reducible compounds despite an almost normal total hydroxylysine content. The finding that the deficiency of hydroxylysine in the collagen of these patients is accompanied by changes in number, chemical nature, and, probably, distribution of crosslinkages, and the previously reported alterations in the solubility characteristics, suggest that at least some skeletal and connective tissue abnormalities are directly related to underlying molecular pathology.

Amino Acid Metabolism, Inborn Errors↗
PubMed1971

Effect of hydroxylysine on the biosynthesis of lysine in saccharomyces.

Hydroxylysine acts as a growth inhibitor of Saccharomyces for a certain period of time. The inhibition is concentration-dependent and is reversed by a small amount of lysine in the medium. After the growth-inhibitory period, the wild-type cells are able to grow rapidly even in the presence of hydroxylysine. Both lysine auxotrophs and wild-type cells are unable to utilize hydroxylysine in place of lysine. Hydroxylysine, mimicking lysine, controls the biosynthesis of lysine and thereby limits the availability of biosynthetic lysine to the cells. Hydroxylysine affects the biosynthesis of lysine at a number of enzymatic steps. Accumulation of homocitric acid, the first intermediate of lysine biosynthesis, in the mutant strains 19B and A B9 is reduced significantly in the presence of hydroxylysine. Hydroxylysine, like lysine, exerts a significant inhibition in vitro on the homocitric acid-synthesizing activity. Enzymes following the alpha-aminoadipic acid step respond in a noncoordinate fashion to hydroxylysine. Level of the enzyme saccharopine reductase, but not of alpha-aminoadipic acid reductase or saccharopine dehydrogenase, is reduced significantly. These regulatory effects of hydroxylysine are similar to those observed for lysine.

Adipates↗
PubMed1999

Recombinant human type II collagens with low and high levels of hydroxylysine and its glycosylated forms show marked differences in fibrillogenesis in vitro.

Type II collagen is the main structural component of hyaline cartilages where it forms networks of thin fibrils that differ in morphology from the much thicker fibrils of type I collagen. We studied here in vitro the formation of fibrils of pepsin-treated recombinant human type II collagen produced in insect cells. Two kinds of type II collagen preparation were used: low hydroxylysine collagen having 2.0 hydroxylysine residues/1,000 amino acids, including 1.3 glycosylated hydroxylysines; and high hydroxylysine collagen having 19 hydroxylysines/1,000 amino acids, including 8.9 glycosylated hydroxylysines. A marked difference in fibril formation was found between these two kinds of collagen preparation, in that the maximal turbidity of the former was reached within 5 min under the standard assay conditions, whereas the absorbance of the latter increased until about 600 min. The critical concentration with the latter was about 10-fold, and the absorbance/microgram collagen incorporated into the fibrils was about one-sixth. The morphology of the fibrils was also different, in that the high hydroxylysine collagen formed thin fibrils with essentially no interfibril interaction or aggregation, whereas the low hydroxylysine collagen formed thick fibrils on a background of thin ones. The data thus indicate that regulation of the extents of lysine hydroxylation and hydroxylysine glycosylation may play a major role in the regulation of collagen fibril formation and the morphology of the fibrils.

Collagen↗
PubMed1968

Effect of hydroxylysine on the biosynthesis of lysine in Streptococcus faecalis.

We were able to show that two lysine-independent mutants of Streptococcus faecalis ATCC 8043 contained the enzymes for the usual bacterial pathway for lysine biosynthesis. Because of this synthetic capacity, one mutant, the Lys(+)OHLys(s) strain, could not grow in the presence of hydroxylysine without a lysine supplement. Both lysine and hydroxylysine inhibited the first enzyme of the pathway, aspartokinase. Unlike the Escherichia coli enzyme, S. faecalis dihydrodipicolinic acid synthetase was not inhibited by either lysine or hydroxylysine. Both amino acids caused the repression of dihydrodipicolinic acid synthetase and diaminopimelic acid decarboxylase. Failure of Lys(+)OHLys(s) strain to grow in hydroxylysine-supplemented medium was caused by the mimicking of lysine control by hydroxylysine. Because hydroxylysine could not completely substitute for lysine and lysine could not be synthesized, the organism did not grow. We tested three lysine analogues and found that they prevented lysine-depletion lysis in the Lsy(-)OHLys(s) strain, as did hydroxylysine. Each analogue seemed to support cell wall mucopeptide synthesis, although ornithine did not. Preliminary data indicated that these analogues like hydroxylysine, have growth-inhibitory action on the Lys(+)OHLys(s) strain, but not the Lys(+)OHLys(r) strain. The nature of the specificity of the lysine-adding enzyme for cell wall mucopeptide synthesis is discussed.

Aspartic Acid↗