Regulation of the expression of ferrochelatase in a murine model of diabetes mellitus type I

Background: Diabetes produces changes on cellular hemeprotein metabolism. The last enzyme of heme biosynthetic pathway is ferrochelatase (FECH), an enzyme that catalyzes the insertion of ferrous ion into protoporphyrin IX to produce heme. The aim of this work was to investigate whether FECH expressi...

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Main Authors: Leda María Oliveri, Ana Maria Buzaleh, Esther Noemí Gerez
Format: Article
Language:English
Published: Elsevier 2025-06-01
Series:Biochemistry and Biophysics Reports
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Online Access:http://www.sciencedirect.com/science/article/pii/S2405580825000767
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author Leda María Oliveri
Ana Maria Buzaleh
Esther Noemí Gerez
author_facet Leda María Oliveri
Ana Maria Buzaleh
Esther Noemí Gerez
author_sort Leda María Oliveri
collection DOAJ
description Background: Diabetes produces changes on cellular hemeprotein metabolism. The last enzyme of heme biosynthetic pathway is ferrochelatase (FECH), an enzyme that catalyzes the insertion of ferrous ion into protoporphyrin IX to produce heme. The aim of this work was to investigate whether FECH expression can be other key point in the regulation of heme biosynthesis in diabetic animals. Methods: Mice were rendered diabetic with streptozotocin (STZ, 170 mg/kg body weight i.p. for 15 days). Liver FECH protein and mRNA levels were evaluated by Western blot and Northern blot respectively. Vanadate was used as a hypoglycemic agent. The levels of the transcription factor Sp1 bound to the FECH promoter were assessed by chromatin immunoprecipitation (ChIP). Results: Hyperglycemia caused an increase in FECH mRNA levels but no changes in FECH protein expression. ChIP analysis revealed that the increase in FECH mRNA levels was due to enhanced Sp1 binding to the FECH promoter in diabetic animals, which was reduced by vanadate administration. Conclusions: In diabetic animals, enhanced binding of Sp1 to the FECH promoter may be responsible for the increase in FECH mRNA levels. However, this increase was not reflected in the amount of FECH protein, which would confirm that FECH could be another control point in heme synthesis.
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spelling doaj-art-22e59aa9f4cf44f0a6442e67b51ea1432025-08-20T03:22:35ZengElsevierBiochemistry and Biophysics Reports2405-58082025-06-014210198910.1016/j.bbrep.2025.101989Regulation of the expression of ferrochelatase in a murine model of diabetes mellitus type ILeda María Oliveri0Ana Maria Buzaleh1Esther Noemí Gerez2Centro de Investigaciones sobre Porfirinas y Porfirias (CIPYP), UBA-CONICET, Hospital de Clínicas José de San Martín, ArgentinaCentro de Investigaciones sobre Porfirinas y Porfirias (CIPYP), UBA-CONICET, Hospital de Clínicas José de San Martín, Argentina; Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, ArgentinaCentro de Investigaciones sobre Porfirinas y Porfirias (CIPYP), UBA-CONICET, Hospital de Clínicas José de San Martín, Argentina; Cátedra Bioquímica General Celular y Molecular, Facultad de Ciencias Médicas. Universidad Católica Argentina (UCA), Buenos Aires, Argentina; Corresponding author. Av. Córdoba 2351, 1120, BUENOS AIRES, Argentina.Background: Diabetes produces changes on cellular hemeprotein metabolism. The last enzyme of heme biosynthetic pathway is ferrochelatase (FECH), an enzyme that catalyzes the insertion of ferrous ion into protoporphyrin IX to produce heme. The aim of this work was to investigate whether FECH expression can be other key point in the regulation of heme biosynthesis in diabetic animals. Methods: Mice were rendered diabetic with streptozotocin (STZ, 170 mg/kg body weight i.p. for 15 days). Liver FECH protein and mRNA levels were evaluated by Western blot and Northern blot respectively. Vanadate was used as a hypoglycemic agent. The levels of the transcription factor Sp1 bound to the FECH promoter were assessed by chromatin immunoprecipitation (ChIP). Results: Hyperglycemia caused an increase in FECH mRNA levels but no changes in FECH protein expression. ChIP analysis revealed that the increase in FECH mRNA levels was due to enhanced Sp1 binding to the FECH promoter in diabetic animals, which was reduced by vanadate administration. Conclusions: In diabetic animals, enhanced binding of Sp1 to the FECH promoter may be responsible for the increase in FECH mRNA levels. However, this increase was not reflected in the amount of FECH protein, which would confirm that FECH could be another control point in heme synthesis.http://www.sciencedirect.com/science/article/pii/S2405580825000767DiabetesFerrochelataseVanadateSp1O-GlcNAcylation
spellingShingle Leda María Oliveri
Ana Maria Buzaleh
Esther Noemí Gerez
Regulation of the expression of ferrochelatase in a murine model of diabetes mellitus type I
Biochemistry and Biophysics Reports
Diabetes
Ferrochelatase
Vanadate
Sp1
O-GlcNAcylation
title Regulation of the expression of ferrochelatase in a murine model of diabetes mellitus type I
title_full Regulation of the expression of ferrochelatase in a murine model of diabetes mellitus type I
title_fullStr Regulation of the expression of ferrochelatase in a murine model of diabetes mellitus type I
title_full_unstemmed Regulation of the expression of ferrochelatase in a murine model of diabetes mellitus type I
title_short Regulation of the expression of ferrochelatase in a murine model of diabetes mellitus type I
title_sort regulation of the expression of ferrochelatase in a murine model of diabetes mellitus type i
topic Diabetes
Ferrochelatase
Vanadate
Sp1
O-GlcNAcylation
url http://www.sciencedirect.com/science/article/pii/S2405580825000767
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AT esthernoemigerez regulationoftheexpressionofferrochelataseinamurinemodelofdiabetesmellitustypei