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PubMed1988

Calcium oxalate in sarcoid granulomas. With particular reference to the small ovoid body and a note on the finding of dolomite.

The nature, prevalence, and specificity of birefringent calcific particles in granulomas of sarcoidosis have been examined, including histochemical reactions, single particle, and microchemical analyses. Particular attention was paid to small ovoid forms of which most were calcium oxalate monohydrate. Larger crystals, those within giant cells, and the birefringent component of a Schaumann complex were also calcium oxalate. Small ovoids appeared to originate in macrophages and to be precursors of other forms; they were found in 86% of lymph nodes and 73% of surgical lung specimens. They were not specific for sarcoidosis. Organisms could not be certainly identified in them. Their origin is discussed in relation to activated macrophages, calcium, and oxalate metabolism, and the role of calcium oxalate in granulomas is considered. Four particles from two cases were dolomite and two were a calcium-sulphur compound. The biologic origin of dolomite is reviewed.

Birefringence↗
PubMed1987

The composition of four-hour urine samples from patients with calcium oxalate stone disease.

Urine collected during a 24-h period between 06.00 and 10.00 h from 25 patients with recurrent CaOx stone disease was analysed with respect to calcium, oxalate, magnesium, citrate and creatinine. Urinary excretion of oxalate in relation to creatinine was slightly higher in 24-h urine but the correlation between 24-h and 4-h values was good. Good correlations were also recorded for calcium and citrate, whereas a more variable result was obtained for magnesium. In terms of the risk of forming a supersaturated urine (CaOx risk index), a good correlation was observed between 24-h and 4-h urine samples, although the highest values were found in 24-h urine. As a result of a low mean urine flow between 06.00 and 10.00 h, the highest supersaturation in terms of the AP (CaOx) index was observed in these samples. When the risk of calcium oxalate crystallisation (CaOx-CR) was determined by means of the increment in oxalate concentration required for precipitation of CaOx, 7 of 11 samples had the highest values in the 4-h urine. Samples collected during a 4-h period might thus be useful in the evaluation and follow-up of CaOx stone formers and further studies will show to what extent they can replace 24-h urine collections.

Calcium↗
PubMed1991

[Studies on calcium oxalate crystal formation in urolithiasis. Multi-regressive analysis of urinary CaOx crystalline volumes and the effects of urinary various substances on CaOx crystal formation].

Because human urine contains various substances which can affect each other, it is quite difficult to clarify the mechanism of formation of calcium oxalate (CaOx) crystal in urine. The authors recently determined CaOx crystalline content and the concentrations of other substances in urine specimens from patients with urolithiasis and healthy volunteers, and subjected the data to multi-regressive analysis for the purpose of assessing the effect of these urinary substances on CaOx crystal formation. 1. In analysis of urine from patients with urolithiasis, the partial correlation coefficients of CaOx crystal formation with oxalic acid, sodium, calcium, uric acid magnesium were 0.67, 0.28, 0.18, and -0.10, respectively. The formula of regression was as follows: Amount of CaOx crystal (X 10(6) microns3/ml) = 3.59 X 10(-2) Ox (mM/L) + 4.72 X 10(-3) Ca (mM/L) + 4.52 X 10(-3) Na (mM/L) + 2.51 X 10(-4) UA (mM/L) -2.39 X 10(-2) Mg (mM/L) -1.65. The multiple correlation coefficient was 0.759. Thus, in patients with urolithiasis, urinary crystal formation was most dependent on the oxalic acid level, sodium, calcium, and uric acid were found to promote crystal formation, while magnesium to suppress it. 2. In analysis of urine from healthy volunteers, the partial correlation coefficients of CaOx crystal formation with oxalic acid and inorganic phosphorus were 0.51 and -0.24, respectively. The formula of regression was as follows: Amount of CaOx crystal (X 10(6) microns3/ml) = 1.91 X 10(-2) Ox (mM/L) -3.43 X 10(-4) P (mM/L) +0.29 The multiple correlation coefficient was 0.525.(ABSTRACT TRUNCATED AT 250 WORDS)

Calcium↗
PubMed1985

Identification of calcium oxalate crystals using alizarin red S stain.

Calcium oxalate crystals stain with alizarin red S at a pH of 7.0 but not at a pH of 4.2. In contrast, calcium phosphate and calcium carbonate stain at a pH of both 7.0 and 4.2. This difference allows presumptive identification of calcium oxalate deposits. The identity of calcium oxalate can then be confirmed by its insolubility in 2M acetic acid, since both calcium carbonate and calcium phosphate are soluble. We have applied this procedure for several years and have found it to be a rapid, reliable, and technically simple procedure for distinguishing calcium oxalate from other calcium deposits.

Animals↗
PubMed1993

Evidence of a link between erythrocyte band 3 phosphorylation and anion transport in patients with 'idiopathic' calcium oxalate nephrolithiasis.

This study was carried out to verify the hypothesis of a link between faster endogenous phosphorylation of band 3 protein, the anion carrier, and anomalous oxalate transmembrane self-exchange found in erythrocyte from calcium oxalate renal stone formers. Agents able to modify 32P-labelling of band 3 protein induced a concurrent modification in oxalate transmembrane flux. Cyclic AMP- and phospholipid-sensitive Ca(2+)-independent protein kinases seem to be critical modulators of band 3 function. These observations demonstrate a close link between the band 3 phosphorylation state and its anion transport function, and provide new insights into the pathogenetic mechanisms of the cellular anomalies observed in calcium-oxalate renal stone disease.

Anion Exchange Protein 1, Erythrocyte↗
PubMed2005

New types of blue, red or near IR luminescent phosphonate-decorated lanthanide oxalates.

Hydrothermal reactions of the lanthanide chlorides with MeN(CH2CO2H)(CH2PO3H2), (H3L1) (or Me2NCH2PO3H2, H2L2) and sodium oxalate lead to seven new lanthanide oxalate phosphonate hybrids with three types of 3D network structures, namely, [Ln(C2O4){MeNH(CH2CO2)(CH2PO3H)}]0.5 H2O (Ln=Nd: 1; Eu: 2; Gd: 3), [Ln4(C2O4)5(Me2NHCH2PO3)2(H2O)4]2 H2O (Ln=La: 4, Nd: 5), [Ln3(C2O4)4(Me2NHCH2PO3)(H2O)6]6 H2O (Gd: 6, Er: 7). Their structures have been established by X-ray single-crystal diffraction. Complexes 1-3 are isostructural and feature a 3D network formed by the interconnection of 3D network of {Ln(H2L1)}2+ with 1D chains of {Ln(C2O4)}+. Complexes 4 and 5 are isostructural and feature a complex 3D network built from 3D network of lanthanide oxalate and {Ln4(HL2)2} units. The isostructural 6 and 7 form another type of 3D network composed of porous lanthanide-oxalate network inserted by 1D chains of lanthanide-oxalate phosphonate. Compounds 1, 5 and 7 are luminescent materials in the near IR region. Compounds 3 and 6 exhibit a broad blue fluorescent emission band at 451 and 467 nm, respectively. Compound 2 displays very strong and sharp emission bands at 592, 616 and 699 nm with a long luminescent lifetime of 1.13 ms.

Journal Article↗
PubMed2007

Inorganic-organic hybrid structures: open-framework iron phosphite-oxalates of varying dimensionality.

Inorganic-organic hybrid structures belonging to the family of iron phosphite-oxalates have been prepared by employing hydrothermal methods. Their structures, determined by single-crystal X-ray diffraction, show a hierarchy within the family. While compounds I and II are low dimensional, III-VI have three-dimensional structures. Compound I has edge-shared ladders of iron phosphite with oxalate units hanging from the iron centers. Compound II has a layer structure with a honeycomb-like arrangement. The three-dimensional hybrid structures have the oxalate units connected in both in-plane and out-of-plane modes. A newly identified secondary building unit (SBU-7) and the oxalate units satisfying the valence and coordination requirements in the structure of V are novel and noteworthy structural features. Magnetic studies show that the dominant interactions between the iron centers are antiferromagnetic. Similar to other known hybrid structures, the phosphite-oxalate structures appear to show wide compositional and structural diversity.

Journal Article↗
PubMed2004

Isolation and characterization of mesophilic, oxalate-degrading Streptomyces from plant rhizosphere and forest soils.

The present work was aimed at the isolation of additional new pure cultures of oxalate-degrading Streptomyces and its preliminary characterization for further work in the field of oxalate metabolism and taxonomic studies. Mesophilic, oxalate-degrading Streptomyces were enriched and isolated from plant rhizosphere and forest soil samples. Strains were examined for cultural, morphological (spore chain morphology, spore mass colour, diffusible and melanin pigment production), physiological (antibiosis, growth in the presence of inhibitory compounds, assimilation of organic acids and enzyme substrates) and chemotaxonomic characters (cellular lipid components and diagnostic cell-wall diamino acid). The taxonomic data obtained were analysed by using the simple matching (SSM) and Jaccard (Sj) coefficients, clustering was achieved using the UPGMA algorithm. All strains were able to utilize sodium-, potassium-, calcium- and ammonium-oxalate salts. Based on the results of numerical taxonomy, isolates were grouped into five cluster groups with a > or =70% S(SM) similarity level. Streptomyces rochei was the most common of the cluster groups, with a Willcox probability of P > 0.8. Streptomyces antibioticus, S. anulatus, S. fulvissimus, S. halstedii and S. violaceusniger are newly reported as oxalate-utilizing Streptomyces.

Ecosystem↗
PubMed2006

In-situ infrared study of the adsorption and oxidation of oxalic acid at single-crystal and thin-film gold electrodes: a combined external reflection infrared and ATR-SEIRAS approach.

The adsorption and oxidation of oxalic acid at gold electrodes were studied by in-situ infrared spectroscopy. External reflection experiments carried out with gold single-crystal electrodes were combined with internal reflection (ATR-SEIRAS) experiments with gold thin-film electrodes. These gold thin films, with a typical thickness of ca. 35 nm, were deposited on silicon substrates by argon sputtering. As previously reported for evaporated gold films, the voltammetric curves obtained in sulfuric acid solutions after electrochemical annealing show typical features related to the presence of wide bidimensional (111) domains with long-range order. The in-situ infrared data collected for solutions of pH 1 confirmed the potential-dependent adsorption of either oxalate (Au(100)) or a mixture of bioxalate and oxalate (Au(111), Au(110), and gold thin films) anions in a bidentate configuration. The better signal-to-noise ratio associated with the SEIRA effect in the case of the gold thin-film electrodes allows the observation of the carbonyl band for adsorbed bioxalate that was not detected in the external reflection experiments. Besides, additional bands are observed between 2000 and 3000 cm(-)(1) that can be tentatively related to the formation of hydrogen bonds between neighboring bioxalate anions. The intensities of these bands decrease with increasing solution pH values, disappearing for pH 3 solutions in which adsorbed oxalate anions are the predominant species. The analysis of the intensities of the nu(s)(O-C-O) and nu(C-OH) + delta(C-O-H) bands for adsorbed oxalate and bioxalate, respectively, suggests that the pK(a) for the surface equilibrium between these species is significantly lower than that for the solution equilibrium.

Journal Article↗
PubMed1998

An epidermis/papilla-specific oxalate oxidase-like protein in the defence response of barley attacked by the powdery mildew fungus.

A cDNA clone of a defence response transcript was isolated from a library prepared from barley leaves expressing papilla resistance towards the powdery mildew fungus, Blumeria (syn. Erysiphe) graminis f.sp. hordei (Bgh). The 904 bp sequence encodes a 229 amino acid polypeptide with a putative signal peptide of 23 amino acids. After cleavage, the protein has a mass of 22.3 kDa and exhibits up to 60% amino acid identity to certain dicot proteins, and 46% amino acid identity to barley oxalate oxidase; therefore we designated it HvOxOLP (for Hordeum vulgare oxalate oxidase-like protein). Single-base substitutions among several cDNA and RACE clones demonstrate a gene of many copies. Both the transcript and protein accumulate from 3 h after inoculation with Bgh. The transcript level peaks at 18-24 h and subsequently decreases, whereas the protein level is stable from 24 h after inoculation. The accumulation patterns are independent of the outcome of the barley/powdery mildew interaction, unlike that of PR proteins, for example. The transcript accumulates specifically in the inoculated epidermal tissue. This temporal and spatial expression pattern suggests a very close relationship to papilla formation. Immunoblot analyses have facilitated a demonstration that HvOxOLP, like oxalate oxidase, is a water-soluble 100 kDa oligomeric protein. The oligomer is heat-stable and SDS-tolerant, and it can be denatured into a 25 kDa monomer. Attempts to demonstrate oxalate oxidase activity for this protein have failed. However, the relationships to oxalate oxidase suggests that HvOxOLP may be involved in H2O2 generation necessary for, for example, cross-linking of cell wall components during formation of papillae.

Amino Acid Sequence↗
PubMed2007

Burst kinetics and redox transformations of the active site manganese ion in oxalate oxidase: implications for the catalytic mechanism.

Oxalate oxidase (EC 1.2.3.4) catalyzes the oxidative cleavage of oxalate to carbon dioxide and hydrogen peroxide. In this study, unusual nonstoichiometric burst kinetics of the steady state reaction were observed and analyzed in detail, revealing that a reversible inactivation process occurs during turnover, associated with a slow isomerization of the substrate complex. We have investigated the underlying molecular mechanism of this kinetic behavior by preparing recombinant barley oxalate oxidase in three distinct oxidation states (Mn(II), Mn(III), and Mn(IV)) and producing a nonglycosylated variant for detailed biochemical and spectroscopic characterization. Surprisingly, the fully reduced Mn(II) form, which represents the majority of the as-isolated native enzyme, lacks oxalate oxidase activity, but the activity is restored by oxidation of the metal center to either Mn(III) or Mn(IV) forms. All three oxidation states appear to interconvert under turnover conditions, and the steady state activity of the enzyme is determined by a balance between activation and inactivation processes. In O(2)-saturated buffer, a turnover-based redox modification of the enzyme forms a novel superoxidized mononuclear Mn(IV) biological complex. An oxalate activation role for the catalytic metal ion is proposed based on these results.

Binding Sites↗
PubMed1995

Excessive urinary oxalate excretion occurs in long-term TPN patients both with and without ileostomies.

OBJECTIVE: To determine if excessive oxalate and deficient citrate excretion were associated with TPN-associated nephropathy. DESIGN: Crossectional cohort. SETTING: Outpatient clinic. SUBJECTS: Twenty-five patients (15 males, 10 females) aged 51 +/- 17 (mean +/- SD) years who had received home total parenteral nutrition (TPN) for 10 +/- 4 years. Fifteen subjects had ileostomies (Group A) and 10 had functional colons (Group B). OUTCOME MEASURES: Glomerular filtration rate (GFR), tubular reabsorption of phosphate (TRP), urinary oxalate and citrate excretion. RESULTS: The mean GFR was 68.1 +/- 34.5 ml/minute/1.73 m2 and did not differ between Groups A and B. The mean TRP was 65.0 +/- 32.2% for Group A and 80.5 +/- 16.0% for Group B. The difference was not statistically significant. Urinary oxalate and citrate excretion were 40.2 +/- 30.2 and 324.4 +/- 239.0 mg/day respectively for Group A, and 63.2 +/- 34.2 and 474.8 +/- 936.3 respectively for Group B. The differences were not statistically significant. Thirty-eight percent (38%) of patients with ileostomies and 78% of patients without ileostomies had excessive urinary oxalate excretion (> 40 mg/day). Fifteen percent (15%) of patients with ileostomies and 50% of patients without ileostomies had decreased urinary citrate excretion (< 140 mg/day). CONCLUSIONS: Increased endogenous oxalate production may occur in patients receiving long-term TPN.

Absorption↗
PubMed1998

High aluminum resistance in buckwheat. Ii. Oxalic acid detoxifies aluminum internally

Buckwheat (Fagopyrum esculentum Moench. cv Jianxi), which shows high Al resistance, accumulates Al in the leaves. The internal detoxification mechanism was studied by purifying and identifying Al complexes in the leaves and roots. About 90% of Al accumulated in the leaves was found in the cell sap, in which the dominant organic acid was oxalic acid. Purification of the Al complex in the cell sap of leaves by molecular-sieve chromatography resulted in a complex with a ratio of Al to oxalic acid of 1:3. A 13C-nuclear magnetic resonance study of the purified cell sap revealed only one signal at a chemical shift 164.4 ppm, which was assigned to the Al-chelated carboxylic group of oxalic acid. A 27Al-nuclear magnetic resonance analysis revealed one major signal at the chemical shift of 16.0 to 17.0 ppm, with a minor signal at the chemical shift of 11.0 to 12 ppm in both the intact roots and their cell sap, which is consistent with the Al-oxalate complexes at 1:3 and 1:2 ratios, respectively. The purified cell sap was not phytotoxic to root elongation in corn (Zea mays). All of these results indicate that Al tolerance in the roots and leaves of buckwheat is achieved by the formation of a nonphytotoxic Al-oxalate (1:3) complex.

Journal Article↗
PubMed1968

Biogenesis of oxalate in plant tissues.

Red beet root discs aerated in potassium phosphate for 2 to 3 days and young spinach leaves actively produce oxalate. A series of labeled compounds was supplied to each of these tissues to determine the extent of conversion to oxalate. Similar results were obtained with the 2 tissues except that in the leaf tissue glyoxylate and glycolate were outstandingly good precursors. Carbon from glucose, acetate, and particularly from some acids of the tricarboxylic acid cycle was recovered in oxalate. Extracts from both tissues were found to contain an enzyme which converts oxaloacetate to oxalate and acetate. The enzyme was partially purified and some of its properties are described. A pathway of oxalate synthesis which does not include glycolate or its oxidase is therefore proposed.

Journal Article↗
PubMed1981

Metabolism of Glycolate in Isolated Spinach Leaf Peroxisomes : KINETICS OF GLYOXYLATE, OXALATE, CARBON DIOXIDE, AND GLYCINE FORMATION.

The flow of glyoxylate derived from glycolate into various metabolic routes in the peroxisomes during photorespiration was assessed. Isolated spinach leaf peroxisomes were fed [(14)C] glycolate in the absence or presence of exogenous glutamate, and the formation of radioactive glyoxylate, CO(2), glycine, oxalate, and formate was monitored at time intervals. In the absence of glutamate, 80% of the glycolate was consumed within 2 hours and concomitantly glyoxylate accumulated; CO(2), oxalate, and formate each accounted for less than 5% of the consumed glycolate. In the presence of equal concentration of glutamate, glycolate was metabolized at a similar rate, and glycine together with some glyoxylate accumulated; CO(2), oxalate, and formate each accounted for an even lesser percentage of the consumed glycolate. CO(2) and oxalate were not produced in significant amounts even in the absence of glutamate, unless glycolate had been consumed completely and glyoxylate had accumulated for a prolonged period. These in vitro findings are discussed in relation to the extent of CO(2) and oxalate generated in leaf peroxisomes during photorespiration.

Journal Article↗
PubMed1983

Synthesis of oxalic Acid by enzymes from lettuce leaves.

A rapid purification of lactate dehydrogenase and glycolate oxidase from lettuce (Lactuca sativa) leaves is described. The kinetics of both enzymes are reported in relation to their possible roles in the production of oxalate. Lettuce lactate dehydrogenase behaves like mammalian dehydrogenase, catalyzing the dismutation of glyoxylate to glycolate and oxalate. A model is proposed in which glycolate oxidase in the peroxisomes and lactate dehydrogenase in the cytosol are involved in the production of oxalate. The effect of pH on the balance between oxalate and glycolate produced from glyoxylate suggests that in leaves lactate dehydrogenase may function as part of an oxalate-based biochemical, pH-stat.

Journal Article↗
PubMed1984

Oxalate metabolism by tobacco leaf discs.

The turnover rate of oxalate in leaf discs of Nicotiana tabacum, var Havana Seed, during photosynthesis was estimated to be 1 to 2 micromoles per gram fresh weight per hour. Radioactivity from the enzymic oxidation of [(14)C]oxalate rapidly appeared in neutral sugars (mainly sucrose), organic acids (mainly malate), and amino acids. Only 5% of the radioactivity was released to the atmosphere as (14)CO(2), and no formate or formaldehyde could be detected. The metabolism of oxalate was not increased by raising the O(2) concentration from 1% to 21% to 60%, nor was the formation of [(14)C]oxalate from [2-(14)C]glyoxylate changed under the same conditions as was previously observed in vitro (Havir 1983 Plant Physiol 71: 874-878). While oxalate is not an inert end product of the glycolate pathway, it contributes little to the formation of photorespiratory CO(2).

Journal Article↗
PubMed1993

Identification of barley oxalate oxidase as a germin-like protein.

A barley oxalate oxidase was purified to homogeneity and the N-terminal sequences of the protein and of two peptides generated by CNBr cleavage of this protein were determined. Searches for similarities in data bank revealed that the sequences are highly homologous to the amino-acid sequence of a wheat protein, germin, which is synthesized de novo during germination. The similarity of the two proteins was confirmed by showing that anti-oxalate oxidase antibodies strongly recognize germin produced in Escherichia coli. We show that like germin, oxalate oxidase is glycosylated, resistant to SDS denaturation, heat stable, and protease resistant. Moreover, oxalate oxidase activity is strongly induced during germination of barley embryos resulting from an accumulation of the protein. Thus, we conclude that barley oxalate oxidase is a germin-like protein.

Glycoproteins↗