Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P00492 (hypoxanthine-guanine phosphoribosyltransferase)
 2,385 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We have confirmed the assignment of the structural locus of the complement factor properdin (Pfc) to the mouse X chromosome and mapped it between monoamine oxidase-A (Mao-a) and hypoxanthine phosphoribosyltransferase (Hprt) using a Mus spretus x Mus musculus interspecific backcross of 108 animals. The structural locus for murine tissue inhibitor of metallothionine proteases (Timp) could not be separated from properdin in a panel of 18 recombinant animals. By minimizing the number of double recombinants the following gene order was obtained: Otc-Mao-a-(Pfc, Timp)-Hprt-Cf-9. The implications for comparative mapping of human and mouse X chromosomes are discussed.
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PMID:The properdin structural locus (Pfc) lies close to the locus for tissue inhibitor of metallothionine proteases (Timp) on the mouse X chromosome. 191 8

Lesch-Nyhan syndrome results from a deficiency of hypoxanthine-guanine phosphoribosyltransferase (HPRT). It is manifest by behavioral abnormalities, including self-mutilation, and evidence of abnormal 3,4-dihydroxyphenylethylamine (dopamine) metabolism. To assess whether an HPRT deficiency in a dopaminergic cell can adversely affect dopamine metabolism in that cell, dopamine metabolism was examined in HPRT-deficient variants of PC12 pheochromocytoma cells and in cells that had regained HPRT activity by virtue of transformation with a recombinant retrovirus containing the human gene for HPRT. There was no correlation between HPRT activity and endogenous dopamine levels, dopamine uptake, dopamine release, or monoamine oxidase activity. Transformation with the HPRT retrovirus did not adversely affect dopamine metabolism.
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PMID:Dopamine metabolism in hypoxanthine-guanine phosphoribosyltransferase-deficient variants of PC12 cells. 351 67

Inherited variations in monoamine oxidase (MAO) activity are thought to affect human behavior and expression of disease. The present study has established the chromosomal location of one of the structural genes coding for this enzyme. Mapping was carried out by somatic cell hybridization between normal human skin fibroblasts and mouse neuroblastoma cells. Selective media for growth of cells with or without hypoxanthine phosphoribosyltransferase (HPRT) activity were used to obtain hybrid lines which had retained or lost the human X chromosome, respectively. Cytogenetic techniques, isozyme analysis, and limited proteolysis and peptide mapping of [3H]pargyline-labeled MAO were used to characterize hybrid lines. With one exception, only lines containing the human X chromosome and human forms of two X-linked enzymes (phosphoglycerate kinase and glucose-6-phosphate dehydrogenase) expressed the human form of the flavin polypeptide of type A MAO. The exceptional hybrid line contained a putative translocation of part of the human X chromosome, since it expressed human forms of both MAO and phosphoglycerate kinase but neither the human form of glucose-6-phosphate dehydrogenase nor HPRT activity. This evidence indicates that the structural gene for the flavin polypeptide of MAO-A is on the human X chromosome. This represents the first chromosomal assignment of a human gene coding for an enzyme of neurotransmitter metabolism. This information will help to elucidate the structure of MAO and modes of its inheritance in the human population.
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PMID:Gene for monoamine oxidase type A assigned to the human X chromosome. 719 39

Monoamine oxidase activity of the A type was measured in homogenates of cultured human skin fibroblasts. Twenty-four control lines had activities ranging over fifty-fold with an apparent bimodal distribution. Activity in fibroblasts from 20 patients with the Lesch-Nyhan syndrome fell in the low portion of the normal distribution with a mean activity about 50% that of the control mean (p < 0.05). In a subgroup of control and Lesch-Nyhan lines with levels of enzyme activity from 0.9 to 179 pmol/min/mg protein, monoamine oxidase was similar with respect to apparent Km for tryptamine, thermal stability at 56 C, and sensitivity to clorgyline. Thus the lower mean levels of activity observed in the Lesch-Nyhan as compared to control fibroblasts were not associated with other altered properties of the enzyme. The bimodal distribution of enzyme activity suggests that a genetic polymorphism for monoamine oxidase may control levels of activity expressed in fibroblasts.
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PMID:Properties of monoamine oxidase in control and Lesch-Nyhan fibroblasts. 743 13