Search Results

You are looking at 1 - 1 of 1 items for

  • Author: V Pannunzio x
  • Refine by access: All content x
Clear All Modify Search
Y Pomeraniec
Search for other papers by Y Pomeraniec in
Google Scholar
PubMed
Close
,
N Grion
Search for other papers by N Grion in
Google Scholar
PubMed
Close
,
L Gadda
Search for other papers by L Gadda in
Google Scholar
PubMed
Close
,
V Pannunzio
Search for other papers by V Pannunzio in
Google Scholar
PubMed
Close
,
EJ Podesta
Search for other papers by EJ Podesta in
Google Scholar
PubMed
Close
, and
CB Cymeryng
Search for other papers by CB Cymeryng in
Google Scholar
PubMed
Close

Heme oxygenase (HO) catalyzes the first and rate-controlling step of heme catabolism into biliverdin, iron and carbon monoxide. Three isoforms of HO have been identified so far: the inducible HO-1 and the constitutive HO-2 and HO-3. Both HO-1 and HO-2 were expressed in zona fasciculata (ZF) adrenal cells and in a mouse adrenocortical cell line (Y1). HO-1 but not HO-2 expression was upregulated by adrenocorticotropic hormone (ACTH) and accumulation of HO-1 protein correlated with an increase in HO activity in Y1 cells. ACTH induced HO-1 expression in a time- and dose-dependent manner with a maximum after 5 h of treatment and a threshold concentration of 0.1 mIU/ml. Actinomycin D and cycloheximide completely blocked the effect of ACTH on HO-1 mRNA expression whereas mRNA stability was not affected by ACTH. Permeable analogs of cAMP mimicked the effect of ACTH on HO-1 expression and ACTH induction was prevented by the protein kinase A (PKA) inhibitor H89. Steroid production was significantly increased when both HO-1 and HO-2 activities were inhibited by Sn-protoporphyrin IX (SnPPIX). The lipid peroxidation and increase in carbonyl content triggered by hydrogen peroxide was prevented by treatment of Y1 cells with bilirubin and ACTH.

Free access