Molecular analysis of dihydropteridine reductase deficiency and restoration of the enzyme activity by gene transfer

1990 ◽  
Vol 13 (5) ◽  
pp. 787-791 ◽  
Author(s):  
H. Mikami ◽  
Y. Matsubara ◽  
K. Hayasaka ◽  
K. Narisawa ◽  
M. Obinata ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Gene Transfer ◽  
Molecular Analysis ◽  
Dihydropteridine Reductase ◽  
Reductase Deficiency

scholarly journals Identification of dihydropteridine reductase in human platelets

Blood ◽  
1979 ◽  
Vol 53 (1) ◽  
pp. 116-121
Author(s):  
HT Abelson ◽  
C Gorka ◽  
GP Beardsley
Keyword(s):  
Enzyme Activity ◽  
Biogenic Amine ◽  
De Novo ◽  
Human Platelets ◽  
Partial Purification ◽  
Dihydropteridine Reductase ◽  
Transport Function ◽  
Reductase Deficiency ◽  
Physical Data ◽  
Normal Human

Normal human platelets were shown to contain the enzyme dihydropteridine reductase. The enzyme was not found in a variety of other cells of hematogenous origin. Partial purification and kinetic and physical data indicated that the platelet enzyme is similar to that previously characterized from liver. Dihydropteridine reductase is important for the regeneration of tetrahydrobiopterin, a required cofactor in hydroxylation reactions involved in biogenic amine formation. The presence of the enzyme may indicate that some synthesis de novo of serotonin and/or catecholamines occurs in platelets, as opposed to a purely storage and transport function. In addition, screening for hyperphenylalaninemia due to dihydropteridine reductase deficiency may become feasible by assaying platelets for enzyme activity.

scholarly journals Identification of dihydropteridine reductase in human platelets

Blood ◽  
1979 ◽  
Vol 53 (1) ◽  
pp. 116-121 ◽  
Author(s):  
HT Abelson ◽  
C Gorka ◽  
GP Beardsley
Keyword(s):  
Enzyme Activity ◽  
Biogenic Amine ◽  
De Novo ◽  
Human Platelets ◽  
Partial Purification ◽  
Dihydropteridine Reductase ◽  
Transport Function ◽  
Reductase Deficiency ◽  
Physical Data ◽  
Normal Human

Abstract Normal human platelets were shown to contain the enzyme dihydropteridine reductase. The enzyme was not found in a variety of other cells of hematogenous origin. Partial purification and kinetic and physical data indicated that the platelet enzyme is similar to that previously characterized from liver. Dihydropteridine reductase is important for the regeneration of tetrahydrobiopterin, a required cofactor in hydroxylation reactions involved in biogenic amine formation. The presence of the enzyme may indicate that some synthesis de novo of serotonin and/or catecholamines occurs in platelets, as opposed to a purely storage and transport function. In addition, screening for hyperphenylalaninemia due to dihydropteridine reductase deficiency may become feasible by assaying platelets for enzyme activity.

Molecular analysis of dihydropteridine reductase deficiency: identification of two novel mutations in Japanese patients

1997 ◽  
Vol 100 (5-6) ◽  
pp. 637-642 ◽  
Author(s):  
Hiroyuki Ikeda ◽  
Y. Matsubara ◽  
Hitoshi Mikami ◽  
Shigeo Kure ◽  
Misao Owada ◽  
...  
Keyword(s):  
Molecular Analysis ◽  
Japanese Patients ◽  
Dihydropteridine Reductase ◽  
Novel Mutations ◽  
Reductase Deficiency

Neuroblastoma in a patient with dihydropteridine reductase deficiency

1990 ◽  
Vol 149 (10) ◽  
pp. 713-715 ◽  
Author(s):  
L. G. Greeves ◽  
R. J. Leeming ◽  
K. Hyland ◽  
S. I. Dempsey ◽  
D. J. Carson
Keyword(s):  
Dihydropteridine Reductase ◽  
Reductase Deficiency

scholarly journals Molecular analysis of chromosome-mediated gene transfer.

1979 ◽  
Vol 76 (8) ◽  
pp. 3987-3990 ◽  
Author(s):  
G. A. Scangos ◽  
K. M. Huttner ◽  
S. Silverstein ◽  
F. H. Ruddle
Keyword(s):  
Gene Transfer ◽  
Molecular Analysis

scholarly journals High prolactin levels in dihydropteridine reductase deficiency: A sign of therapy failure or additional pathology?

JIMD Reports ◽  
2021 ◽  
Author(s):  
Nicola Vitturi ◽  
Livia Lenzini ◽  
Concetta Luisi ◽  
Miryam Carecchio ◽  
Giorgia Gugelmo ◽  
...  
Keyword(s):  
Dihydropteridine Reductase ◽  
Therapy Failure ◽  
Reductase Deficiency

Hyperphenylalaninemia Due to Dihydropteridine Reductase Deficiency: Diagnosis by Measurement of Oxidized and Reduced Pterins in Urine

PEDIATRICS ◽  
1980 ◽  
Vol 65 (4) ◽  
pp. 806-810
Author(s):  
Sheldon Milstien ◽  
Seymour Kaufman ◽  
George K. Summer
Keyword(s):  
High Performance ◽  
Active Form ◽  
High Performance Liquid Chromatographic ◽  
Dihydropteridine Reductase ◽  
Normal Children ◽  
Reductase Deficiency ◽  
Cultured Skin ◽  
Aromatic Amino Acid Hydroxylase ◽  
Liver Biopsies ◽  
Liquid Chromatographic

Hyperphenylalaninemia due to dihydropteridine reductase deficiency results from the inability to maintain the aromatic amino acid hydroxylase cofactor, tetrahydrobiopterin, in its reduced or active form. Diagnosis of the disease is usually made by direct enzymatic assay on liver biopsies or in cultured skin fibroblasts. Evidence is presented that normal children and classic phenylketonuric children excrete mainly tetrahy-drobiopterin in their urmnes, whereas children with dihydropteridine reductase deficiency excrete only oxidized forms of biopterin. Details of a rapid high performance liquid chromatographic assay for the measurement of the various forms of biopterin in urine are presented. This assay can be used to screen for suspected dihydropteridine reductase mutants.

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