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Titolo:
Highly heterogeneous nature of delta-aminolevulinate dehydratase (ALAD) deficiencies in ALAD porphyria
Autore:
Maruno, M; Furuyama, K; Akagi, R; Horie, Y; Meguro, K; Garbaczewski, L; Chiorazzi, N; Doss, MO; Hassoun, A; Mercelis, R; Verstraeten, L; Harper, P; Floderus, Y; Thunell, S; Sassa, S;
Indirizzi:
Rockefeller Univ, Lab Biochem Hematol, New York, NY 10021 USA Rockefeller Univ New York NY USA 10021 em Hematol, New York, NY 10021 USA Okayama Prefectural Univ, Okayama, Japan Okayama Prefectural Univ Okayama Japan Prefectural Univ, Okayama, Japan Cornell Univ, Northshore Hosp, Long Isl City, NY USA Cornell Univ Long Isl City NY USA Northshore Hosp, Long Isl City, NY USA Univ Marburg, Marburg, Germany Univ Marburg Marburg GermanyUniv Marburg, Marburg, Germany Univ Catholique Louvain, B-1200 Brussels, Belgium Univ Catholique LouvainBrussels Belgium B-1200 B-1200 Brussels, Belgium Univ Antwerp Hosp, Antwerp, Belgium Univ Antwerp Hosp Antwerp BelgiumUniv Antwerp Hosp, Antwerp, Belgium Huddinge Univ Hosp, S-14186 Huddinge, Sweden Huddinge Univ Hosp HuddingeSweden S-14186 osp, S-14186 Huddinge, Sweden
Titolo Testata:
BLOOD
fascicolo: 10, volume: 97, anno: 2001,
pagine: 2972 - 2978
SICI:
0006-4971(20010515)97:10<2972:HHNODD>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
HEREDITARY HEPATIC PORPHYRIA; ACID DEHYDRATASE; 5-AMINOLEVULINATE DEHYDRATASE; PORPHOBILINOGEN SYNTHASE; ESCHERICHIA-COLI; LEAD; INHIBITION; ENZYME; RATS; TRICHLOROETHYLENE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Clinical Medicine
Life Sciences
Citazioni:
44
Recensione:
Indirizzi per estratti:
Indirizzo: Sassa, S Rockefeller Univ, Lab Biochem Hematol, 1230 York Ave, New York, NY 10021 USA Rockefeller Univ 1230 York Ave New York NY USA 10021 NY 10021 USA
Citazione:
M. Maruno et al., "Highly heterogeneous nature of delta-aminolevulinate dehydratase (ALAD) deficiencies in ALAD porphyria", BLOOD, 97(10), 2001, pp. 2972-2978

Abstract

The properties of 9 delta -aminolevulinate dehydratase (ALAD) mutants frompatients with ALAD porphyria (ADP) were examined by bacterial expression of their complementary DNAs and by enzymologic and immunologic assays. ALADswere expressed as glutathione-S-transferase (GST) fusion proteins in Escherichia coli and purified by glutathione-affinity column chromatography. TheGST-ALAD fusion proteins were recognized by anti-ALAD antibodies and were enzymatically active as ALAD. The enzymatic activities of 3 ALAD mutants, K59N, A274T, and V153M, were 69.9%, 19.3%, and 41.0% of that of the wild-type ALAD, respectively, whereas 6 mutants, G133R, K59N/G133R, F12L, R240W, V275M, and deITC, showed little activity (< 8%). These variations generally reflect the phenotype of ALAD in vivo in patients with ADP and indicate thatGST-ALAD fusion protein is indeed useful for predicting of the phenotype of ALAD mutants. The location of F12L mutation in the enzyme's molecular structure indicates that its disturbance of the quaternary contact of the ALADdimer appears to have a significant influence on the enzymatic activity. Mouse monoclonal antibodies to human ALAD were developed that specifically recognized a carboxy terminal portion of ALAD, or other regions In the enzyme. This study represents the first complete analysis of 9 mutants of ALAD identified In ADP and indicates the highly heterogeneous nature of mutationsin this disorder. (Blood. 2001;97:2972-2978) (C) 2001 by The American Society of Hematology.

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Documento generato il 02/04/20 alle ore 22:17:03