دورية أكاديمية
Synergistic induction of delta-aminolevulinate synthase by glutethimide and iron: relationship to the synergistic induction of heme oxygenase.
العنوان: | Synergistic induction of delta-aminolevulinate synthase by glutethimide and iron: relationship to the synergistic induction of heme oxygenase. |
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المؤلفون: | Cable EE; Department of Biochemistry, Emory University School of Medicine, Atlanta, GA., Healey JF, Greene Y, Evans CO, Bonkovsky HL |
المصدر: | Biochimica et biophysica acta [Biochim Biophys Acta] 1991 Nov 15; Vol. 1080 (3), pp. 245-51. |
نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S. |
اللغة: | English |
بيانات الدورية: | Publisher: Elsevier Pub. Co Country of Publication: Netherlands NLM ID: 0217513 Publication Model: Print Cited Medium: Print ISSN: 0006-3002 (Print) Linking ISSN: 00063002 NLM ISO Abbreviation: Biochim Biophys Acta Subsets: MEDLINE |
أسماء مطبوعة: | Original Publication: Amsterdam : Elsevier Pub. Co. |
مواضيع طبية MeSH: | 5-Aminolevulinate Synthetase/*drug effects , Glutethimide/*pharmacology , Heme Oxygenase (Decyclizing)/*drug effects , Iron/*pharmacology, 5-Aminolevulinate Synthetase/biosynthesis ; Animals ; Cells, Cultured ; Chick Embryo ; Drug Synergism ; Enzyme Induction/drug effects ; Ferric Compounds/pharmacology ; Heme/pharmacology ; Heme Oxygenase (Decyclizing)/biosynthesis ; Liver/embryology ; Liver/enzymology ; Metalloporphyrins/pharmacology ; Nitrilotriacetic Acid/analogs & derivatives ; Nitrilotriacetic Acid/pharmacology |
مستخلص: | Relationships between activities of delta-aminolevulinate synthase and heme oxygenase, respectively the rate-limiting enzymes of heme biosynthesis and degradation, have been studied in chick embryo liver cell cultures following exposure of the cultures to glutethimide and iron, a combination known to produce a synergistic induction of both enzymes. In time-course experiments, synergistic induction of heme oxygenase activity by glutethimide and iron preceded that of delta-aminolevulinate synthase by 4 h. Effects of selective inhibitors of both heme synthesis and degradation have also been studied with respect to effects on delta-aminolevulinate synthase and heme oxygenase activities. The synergistic induction of heme oxygenase by glutethimide and iron appears to be dependent upon cellular heme synthesis because addition of inhibitors of heme biosynthesis, 4,6-dioxoheptanoic acid or N-methyl-mesoporphyrin abolishes this synergistic induction. Exposure of cultures to tin-mesoporphyrin, a potent inhibitor of heme oxygenase, prevented the synergistic induction of delta-aminolevulinate synthase produced by glutethimide and iron, or, when added after induction was already established, promptly halted any further induction. These results suggest that the level of activity of heme oxygenase can reciprocally modulate intracellular heme levels and thus activity of delta-aminolevulinate synthase. |
معلومات مُعتمدة: | DK 38825 United States DK NIDDK NIH HHS |
المشرفين على المادة: | 0 (Ferric Compounds) 0 (Metalloporphyrins) 0KAE1U0G7Q (tin mesoporphyrin) 42VZT0U6YR (Heme) C8I4BVN78E (Glutethimide) E1UOL152H7 (Iron) EC 1.14.14.18 (Heme Oxygenase (Decyclizing)) EC 2.3.1.37 (5-Aminolevulinate Synthetase) KA90006V9D (Nitrilotriacetic Acid) Z3U5ED15B9 (ferric nitrilotriacetate) |
تواريخ الأحداث: | Date Created: 19911115 Date Completed: 19911230 Latest Revision: 20190609 |
رمز التحديث: | 20221213 |
DOI: | 10.1016/0167-4838(91)90009-o |
PMID: | 1954232 |
قاعدة البيانات: | MEDLINE |
تدمد: | 0006-3002 |
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DOI: | 10.1016/0167-4838(91)90009-o |