Disease relevance of homoarginine

• When phenylalanine and homoarginine were used to define ALP isoenzymes in stored amniotic fluids, 9 of 10 cases of cystic fibrosis were identified, while only 9 of 831 control fluids were scored as false positives [1].
• Inhibitory effect of L-homoarginine on murine osteosarcoma cell proliferation [2].
• Transformation of Lys4 into homoarginine did not affect toxicity [3].
• Enzymohistochemically as well as biochemically, ALP in germinoma cells was little sensitive to L-phenylalanine, moderately sensitive to L-homoarginine and somewhat resistant to heat in its inhibition tests [4].
• Phaseolotoxin [N delta(N'-sulfo-diaminophosphinyl)-ornithyl-alanyl- homoarginine] produced by Pseudomonas syringae pv. phaseolicola, the bean halo blight pathogen, is a potent inhibitor of ornithine carbamoyltransferase (OCT) [5].

Psychiatry related information on homoarginine

• A methylisourea solution of 0.5 M and a 6-d reaction time are recommended for converting lysine to homoarginine in barley and canola meal [6].

High impact information on homoarginine

• Second-trimester amniotic fluid contains two major alkaline phosphatase (ALP) isoenzymes, one susceptible to inhibition by phenylalanine and the other to inhibition by homoarginine [1].
• Percent trans-stimulation of homoarginine efflux was 1.0 +/- 0.5% in homozygous LPI cells, 10 +/- 0.5% in heterozygous cells, and 22 +/- 0.5% in control cells indicating a gene-dosage effect [7].
• Expression of the arginase (CAR1) gene in Saccharomyces cerevisiae is induced by arginine or its analog homoarginine [8].
• A comparison of fast homoarginine-sensitive alkaline phosphatase and carcinoembryonic antigen as markers in colon carcinoma [9].
• Thus, L-homoarginine inhibits proliferation and alkaline phosphatase activity of mouse OS cells and appears to increase acid phosphatase activity in synthesis of lysosomal granules [2].

Chemical compound and disease context of homoarginine

• We found that, unlike the BLK-ALP of the Saos-2 osteosarcoma cell line, the activity of U-2 OS ALP was thermostable, unaffected by L-homoarginine and levamisole, but inhibited by L-phenylalanine; these properties are characteristic of the placental and/or placental-like (PL-/PL-like ALP) isoenzymes which are 98% homologous at the amino acid level [10].
• The phototrophic bacterium Rhodobacter capsulatus E1F1 grew with L-arginine or L-homoarginine as nitrogen source under light/anaerobiosis [11].
• The other ALP isozyme of FL cells had properties common to hepatoma ALP with regard to L-phenylalanine sensitivity, inhibition by ethylenediaminetetraacetate, inactivation by urea, and antigen site, but differed from it in electrophoretic mobility, sensitivity to L-leucine and L-homoarginine, and the presence of another antigen site [12].

Biological context of homoarginine

• Although the present phenotype was stable during long-term culture in regard to the isozyme properties, the original cancer cells from which the cell line had been derived were L-phenylalanine sensitive and moderately L-homoarginine sensitive [13].
• In water at pH 5.25, 5 degrees C, homoarginine shows an isotope effect k12/k13 = 1.601, indicating that the decarboxylation step is entirely rate determining [14].
• The addition of 10(-4) or 10(-3) M cationic amino acids (l-ornithine, l-lysine, or l-homoarginine) or neutral amino acids (l-glutamine, l-leucine, or l-serine) to the perfusate decreased NO and increased renal vascular resistance [15].
• The application of guanidination chemistry, the conversion of lysine into homoarginine residues, is used to illustrate several important general considerations relating to the use of differential isotope labelling for relative quantification in proteomics [16].
• However, PTA-noraginine was much less susceptible to tryptic hydrolysis that PTA-homoarginine, while the linear esters of norarginine are known to be more susceptible than those of homoarginine [17].

Anatomical context of homoarginine

• Arginine and homoarginine accumulate in human fibroblasts reaching distribution ratios of more than 20 at external amino acid concentrations in the physiological range [18].
• Egg white lysozyme, treated with O-methylisourea to convert lysine to homoarginine residues, was used as a substrate for the ATP-dependent proteolytic pathway in rabbit reticulocyte lysates [19].
• Investigation of pH dependence and susceptibility to inhibition by L-phenylalanine and L-homoarginine indicated similarity of the alkaline phosphatase from B cell lines to the enzyme recoverable from normal mouse kidney, placenta, bone marrow, and lymphoid organs [20].
• L-Lysine, like-L-arginine, L-ornithine, or L-homoarginine, accumulated in rat pancreatic islets and stimulated 86Rb efflux, 45Ca uptake and efflux, and insulin release in islets exposed to D-glucose (7.0 mM) [21].
• L-Lysine or L-homoarginine, which does not activate acetylglutamate synthetase, had no effect on acetylglutamate synthesis, in the isolated mitochondria [22].

Associations of homoarginine with other chemical compounds

• The increase in alkaline phosphatase sensitivity to the inhibitors levamisole and homoarginine, together with changes in the apparent molecular size and in the sialization of the enzyme, indicated a change in the isoform expressed [23].
• 6. Inhibition of alkaline phosphatase activity by increasing or decreasing the pH of the incubation medium or by the presence of vanadate (1 mM) or homoarginine (500 microM) led to a significant increase in the accumulation of [3H]-MPP+ in isolated hepatocytes [24].
• A simple capillary zone electrophoresis (CZE) method has been developed for the simultaneous quantitative determination of beta-N-oxalyl-L-alpha,beta-diaminopropionic acid (beta-ODAP) and homoarginine in Lathyrus sativus (LS; grass pea) [25].
• Alkaline phosphatase isoenzymes from small intestine, cecum, large colon, small colon, liver, kidney, leukocytes, and serum from ten clinically normal horses were defined by their sensitivities to L-phenylalanine, L-homoarginine, levamisole and heat, and by polyacrylamide gel disc electrophoresis [26].
• Serum levels of guanidinoacetic acid (GAA) and homoarginine are significantly decreased [27].

Gene context of homoarginine

• Partial purification and properties of a transamidinase from Lathyrus sativus seedlings. Involvement in homoarginine metabolism and amine interconversions [28].
• L-Homoarginine was not a substrate for liver arginase [29].
• Serum of cancer patients often contains high activities of a homoarginine-sensitive isoenzyme of alkaline phosphatase with high electrophoretic mobility, which is present in relatively low activities in sera from most normal persons and persons with benign disease [30].
• 3. L-phenylalanine and L-homoarginine give a major degree of discrimination between liver/bone/kidney ALP on the one hand, and placental and intestinal ALPs on the other [31].
• Differential inhibition by homoarginine and phenylalanine indicates that butyrate is inducing the liver-bone kidney isozyme that is found in endometrial glands in vivo [32].

Analytical, diagnostic and therapeutic context of homoarginine

• The postsource decay (PSD) MALDI tandem mass spectra of a model peptide (VGGYGYGAK), the homoarginine analog and the sulfonated homoarginine analog are compared [33].
• In free-flow micropuncture experiments, the concentrations of endogenous L-arginine+, [Arg], and of intravenously infused L-homoarginine+, [HoArg], were determined by HPLC [34].
• An intraperitoneal injection of L-homoarginine (10 mg/rats) produced immediate and transient reduction in pancreatic secretion in BPJ-diverted rats, but not in normal rats [35].
• L-Homoarginine benzylester was coupled with Sepharose 4B and used for affinity chromatography of human plasma kallikrein [EC 3.4.21.8] and urokinase [EC 3.4.99.26] [36].
• The effect of homoarginine on the EEG of rats [37].

References