Inhibitory effects of meta-iodo-benzylguanidine (MIBG) on endothelial histamine receptor binding.
Cast your vote
You can rate an item by clicking the amount of stars they wish to award to this item.
When enough users have cast their vote on this item, the average rating will also be shown.
Your vote was cast
Thank you for your feedback
Thank you for your feedback
MetadataShow full item record
CitationBiochim. Biophys. Acta. 1998, 1379(1):143-50
AbstractMeta-iodo-benzylguanidine (MIBG), a selective inhibitor of mono-ADP-ribosylation, has been shown to inhibit histamine induced inositol-trisphosphate and prostacyclin production. The purpose of this study was to evaluate the effect of MIBG on the binding of histamine to the H1-receptor and to study its effects on phospholipid metabolism in human endothelial cells. The effects of MIBG and MIBA (meta-iodo-benzylamine), which does not affect cellular ADP-ribosylation, on agonist induced cGMP production in cultured HUVEC's were measured by RIA and a binding study carried out to evaluate their effects on the binding of [3H]mepyramine to membrane fractions. MIBG (0.3 mM) reduced histamine induced cGMP production by 90.8% but did not inhibit the cGMP production induced by other agonists. MIBA had no effect. MIBG also reduced the binding of [3H]mepyramine (1.0 nM) to membrane fractions with IC50 at 0.094 mM and maximal inhibition (83%) at 0.22mM MIBG. The calculated Ki was 0.076mM. MIBG and MIBA altered phospholipid metabolism in a similar way as the cationic amphiphilic drug propranolol. MIBA caused up to 42% reduction in [3H]mepyramine binding, probably due to its inhibition of nonspecific binding. These results indicate that MIBG reduces histamine induced cGMP production by inhibiting its binding to H1-receptors and alters phospholipid metabolism in cultured endothelial cells in a similar way as known cationic amphiphilic drugs.
DescriptionTo access publisher full text version of this article. Please click on the hyperlink in Additional Links field
- Characteristics of the binding of [3H]-mepyramine to intact human U373 MG astrocytoma cells: evidence for histamine-induced H1-receptor internalisation.
- Authors: Hishinuma S, Young JM
- Issue date: 1995 Nov
- Pharmacology of [3H]-pyrilamine binding and of the histamine-induced inositol phosphates generation, intracellular Ca2+ -mobilization and cytokine release from human corneal epithelial cells.
- Authors: Sharif NA, Wiernas TK, Griffin BW, Davis TL
- Issue date: 1998 Nov
- Histamine stimulates inositol phosphate accumulation via the H1-receptor in cultured human endothelial cells.
- Authors: Lo WW, Fan TP
- Issue date: 1987 Oct 14
- High affinity, saturable [3H]mepyramine binding sites on rat liver plasma membrane do not represent histamine H1-receptors. A warning.
- Authors: Leurs R, Bast A, Timmerman H
- Issue date: 1989 Jul 1
- Role of ADP-ribosylation in endothelial signal transduction and prostacyclin production.
- Authors: Halldórsson H, Bödvarsdóttir T, Kjeld M, Thorgeirsson G
- Issue date: 1992 Dec 21