Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. A family is reported with an unusual type of cystinuria. 2. The propositus presented with a cystine renal stone; the renal tubular reabsorption of cystine was grossly abnormal but the tubular reabsorption of ornithine, lysine and arginine was only slightly less than normal. 3. One of the children of the propositus escreted cystine and lysine in increased amounts typical of type II heterozygotes for cystinuria. 4. The renal transport defect in this family may represent one end of the spectrum of cystinuria or it may be a form akin to isolated hypercystinuria.
Clin Sci Mol Med 1976 Jul
PMID:Cystinuria: a new genetic variant. 93 63

1. Two women with severe hypokalaemic alkalosis were investigated by means of muscle biopsy before and at the end of 2 and 3 weeks respectively of intense therapy with potassium chloride. 2. The muscle biopsy material was analysed for water, electrolytes, adenine nucleotides, phosphocreatine, free creatine, pyruvate, lactate, glycogen and free amino acids. The extra- and intra-cellular distribution of water, electrolytes and amino acids was calculated by the chloride method. 3. Both patients showed a marked loss of intracellular potassium and an increase in intracellular sodium concentration. The muscle magnesium content was also slightly decreased. After repletion with potassium chloride, muscle sodium and potassium became normal. 4. The contents of creatine phosphate, ATP, ADP, AMP, lactate and pyruvate were within normal limits, but the phosphocreatine/total creatine ratio was reduced. After repletion, a small change in the apparent creatine-phosphokinase equilibrium had occurred, suggesting a minor increase in intracellular pH. 5. The concentrations of the basic amino acids, lysine, arginine and ornithine were increased far above normal. The intracellular accumulation of arginine was much higher than the increase in lysine concentration and histidine concentration was normal. This differs from findings in potassium-depleted rats, where the intracellular lysine concentration is much higher than arginine concentration and histidine is high as well. After potassium repletion the intracellular concentration of ornithine, lysine and arginine became normal in one case and decreased considerable in the other. An increased intracellular concentration of glutamate and glutamine was also observed after potassium repletion.
Clin Sci Mol Med 1976 Dec
PMID:Influence of severe potassium depletion and subsequent repletion with potassium on muscle electrolytes, metabolites and amino acids in man. 107 Apr 23

1. A technique has been developed for the measurement of kallikrein 'production' in rat renal cortical cells in suspension. 2. After preparative steps, column chromatography on DEAE-cellulose yielded a peak of alpha-N-tosyl-L-arginine methyl ester (Tos-Arg-OMe) esterase activity identical with kallikrein isolated from rat urine in respect of pH optimum, effects of inhibitors, biological activity and immunological properties. 3. The nutrient medium surrounding incubated cells contained measurable kallikrein activity, which was increased by aldosterone and decreased by spironolactone. 4. The results raised the possibility that kallikrein could be an aldosterone-induced protein.
Clin Sci Mol Med Suppl 1976 Dec
PMID:The effects of aldosterone and spironolactone on renal kallikrein in the rat. 107 27

Mutants with a feedback resistant N-acetylglutamate synthase have been isolated from a proA/B, argD, argR strain by screening for proline excretion on minimal medium with arginine. The feedback resistant character of three mutants was transduced into an argA (N-acetylglutamate synthase negative) strain. It was cotransducible with argA at a frequency of greater than 99%. N-acetylglutamate synthase extracted from the three mutants was approximately one hundred times less sensitive to L-arginine than the enzyme from the feedback sensitive parent strain.
Mol Gen Genet 1975 Jun 19
PMID:Isolation and characterization of mutants with a feedback resistant N-acetylglutamate synthase in Escherichia coli K 12. 110 31

The regulatory gene (argR) for the arginine biosynthetic pathway has been located at 106 min on the chromosome of S. typhimurium. In addition, the location of the gene specifying cytosine deaminase (cod) has been more precisely determined.
Mol Gen Genet 1975 Sep 08
PMID:Location of the argR gene on the chromosome of Salmonella typhimurium. 110 41

Relationship of citrate synthase (EC 4.1.3.7) to the biosynthesis of glutamic acid was investigated by characterizing a new glutamic acid auxotroph FL100-D1 (glu 3) of Saccharomyces cerevisiae. Nutritional requirement of the mutant was satisfied by L-glutamic acid, L-glutamic acid peptide as well as several analogs of glutamic acid, but not by proline, ornithine, arginine, lysine or aspartic acid. The mutant was unable to utilize nonfermentable carbon sources, glycerol, acetate or lactate. Mutant glu3 unlike aconitaseless glutamic acid auxotroph glu 1, failed to accumulate 14C-citric acid in vivo from 1-14C-sodium acetate or U-14C-glutamic acid. Both spectrophotometric and radioactive assay procedures demonstrated a lack of significant citrate synthase activity in the dialysed extract of the mutant compared to the wild type strain. Mutant glu 3 complemented with glu 1 and glu 2 individually in vivo and exhibited a significant aconitase (EC 4.2.1.3) activity in vitro.
Mol Gen Genet 1975 Sep 08
PMID:Citrate synthaseless glutamic acid auxotroph of Saccharomyces cerevisiae. 110 43

Hydroxyproline-2-epimerase was treated with 14C-iodoacetate under conditions that produced almost complete inactivation of the enzyme and concomitant incorporation of almost one molar equivalent of iodoacetate. Both processes were prevented by saturating concentrations of substrate. From reaction mixtures in which both incorporation and inactivation were 85 to 90% complete, two radioactive tryptic peptides were isolated by paper chromatography-electrophoresis. The incorporated radioactivity was divided between the peptides in an approximately 2:1 ratio. Analysis of the isolated peptides suggested that they both contained 9 amino acids and had similar composition; one appeared to be a lysine, the second an arginine peptide. Attempts to sequence each peptide failed, apparently because of the conversion of the S-carboxymethylcysteine to S-carboxymethylcysteine sulfone, indicating that the cysteine residue was N-terminal in each peptide.
Mol Cell Biochem 1975 Aug 30
PMID:Hydroxyproline-2-epimerase of Pseudomonas: active-site peptides. 116 63

Cationic amino acids, arginine and lysine partition differentially from water into aqueous micellar sodium dodecanoate. Conversely, partitioning of serine, glycine, aspartic acid, glutamic acid, threonine, alanine, proline, valine, leucine, phenylalanine and isoleucine do not vary appreciably. Partitioning from neat hexane into dodecylammonium propionate trapped water in hexane is, however, dependent upon both electrostatic and hydrophobic interactions. These results imply that the interior of dedecylammonium propionate aggregates is negatively charged and is capable of hydrogen bonding in addition to providing a hydrophobic enviroment. The solubilities of amino acids in neat hexane substantiate the previously derived amino acid hydrophobicity scale. Relevance of partitioning in these systems to the postulated selective amino acid compartmentalization is discussed.
J Mol Evol 1975 Nov 04
PMID:Compartmentalization of amino acids in surfactant aggregates. Partitioning between water and aqueous micellar sodium deodecanoate and between hexane and dodecylammonium propionate trapped water in hexane. 120 27

The spatial structure of methylamide N-acetyl-L-argine was studied taking into account the non-valent and electrostati interactions, the torsion energy, and the distorsion of valency angles. Calculation of the favourable conformations of the molecule was carried out with the use of all the combinations of angles phi, psi, chi1 divided by chi4 as an intital approximation. These correspond to the low energy forms of the main chain and to the minima of the torsion potentials of the side chain. Conformational possibilities of arginine and lysine were compared. The calculated stable conformation of N-acetyl-L-arginine-methylamide are compared with the geometry of arginine residues in the proteins with known structure.
Mol Biol (Mosk)
PMID:[Theoretical conformational analysis of methylamide N-acetyl-L-arginine]. 121 9

We have recently shown that transforming growth factor-beta (TGF beta) acts in an autocrine manner to maintain the beating rate of neonatal rat cardiac myocytes cultured in serum-free medium on cardiac fibroblast matrix. Interleukin-1 beta (IL-1 beta) suppresses the myocyte-beating rate, and TGF beta antagonizes this effect. We now show that TGF beta and IL-1 beta also have antagonistic effects on the secretion of nitric oxide (NO) by these myocytes, and that NO secretion, the activity of NO synthase (NOS), and expression of the inducible form of NOS correlate inversely with the effects of these two agents on the beating rate. Western blot analysis shows that treatment of myocytes with TGF beta antagonizes the induction of NOS after treatment with IL-1 beta. Release of NO, induced by IL-1 beta, is dependent upon the availability of the substrate, L-arginine, and is suppressed by a competitive inhibitor, NG-monomethyl-L-arginine. L-Arginine (> 0.25 mM) also suppresses, and NG-monomethyl-L-arginine (> 0.5 mM) enhances the myocyte-beating rate. Treatment with IL-1 beta, but not TGF beta, increases cellular cGMP, presumably by activation of guanylate cyclase by NO. Methylene blue, an inhibitor of guanylate cyclase, reverses the suppression of beating caused by IL-1 beta. Bacterial lipopolysaccharide, present in the serum-free medium, is a coinducer of NO secretion. The suppressive effects of NO on the beating rate can be overcome by altering either the set of cytokines employed to induce NO or the matrix on which the myocytes are cultured, demonstrating that additional parameters are also involved in regulation of the beating rate.
Mol Endocrinol 1992 Nov
PMID:Role of nitric oxide in antagonistic effects of transforming growth factor-beta and interleukin-1 beta on the beating rate of cultured cardiac myocytes. 128 74


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