Role of ADP-ribosylation in endothelial signal transduction and prostacyclin production

H Halldorsson; T Bodvarsdottir; M Kjeld; G Thorgeirsson

doi:10.1016/0014-5793(92)81497-A

Role of ADP-ribosylation in endothelial signal transduction and prostacyclin production

H Halldorsson, T Bodvarsdottir, M Kjeld, G Thorgeirsson

Landspitali - The National University Hospital of Iceland

Research output: Contribution to journal › Article › peer-review

Abstract

ADP-ribosylation of proteins by the enzymatic transfer of ADP-ribose from NAD has been implicated in a number of biological processes. We report that inhibitors of ADP-ribosylation, most notably the novel inhibitor of arginine specific cellular mono(ADP-ribosyl) transferase, meta-iodobenzylguanidine (MIBG) as well as nicotinamide, L-arginine methyl ester (LAME) and guanyltyramine, inhibit histamine-induced endothelial production of inositol phosphates, release of arachidonic acid and production of prostacyclin (PGI2). Those same responses were unaffected by MIBG when triggered by thrombin or leukotriene C4. These findings suggest that ADP-ribosylation serves a role in histamine-induced production of prostacyclin and imply differences in transduction pathways employed by the different agonists.

Original language	English
Journal	FEBS Letters
DOIs	https://doi.org/10.1016/0014-5793(92)81497-A
Publication status	Published - 21 Dec 1992

Other keywords

3-Iodobenzylguanidine
Adenosine Diphosphate Ribose
Cells, Cultured
Endothelium, Vascular
Epoprostenol
Humans
Inositol Phosphates
Iodobenzenes
Signal Transduction

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10.1016/0014-5793(92)81497-A

http://dx.doi.org/10.1016/0014-5793(92)81497-A

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title = "Role of ADP-ribosylation in endothelial signal transduction and prostacyclin production",

abstract = "ADP-ribosylation of proteins by the enzymatic transfer of ADP-ribose from NAD has been implicated in a number of biological processes. We report that inhibitors of ADP-ribosylation, most notably the novel inhibitor of arginine specific cellular mono(ADP-ribosyl) transferase, meta-iodobenzylguanidine (MIBG) as well as nicotinamide, L-arginine methyl ester (LAME) and guanyltyramine, inhibit histamine-induced endothelial production of inositol phosphates, release of arachidonic acid and production of prostacyclin (PGI2). Those same responses were unaffected by MIBG when triggered by thrombin or leukotriene C4. These findings suggest that ADP-ribosylation serves a role in histamine-induced production of prostacyclin and imply differences in transduction pathways employed by the different agonists.",

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author = "H Halldorsson and T Bodvarsdottir and M Kjeld and G Thorgeirsson",

year = "1992",

month = dec,

day = "21",

doi = "10.1016/0014-5793(92)81497-A",

language = "English",

journal = "FEBS Letters",

issn = "0014-5793",

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T1 - Role of ADP-ribosylation in endothelial signal transduction and prostacyclin production

AU - Halldorsson, H

AU - Bodvarsdottir, T

AU - Kjeld, M

AU - Thorgeirsson, G

PY - 1992/12/21

Y1 - 1992/12/21

N2 - ADP-ribosylation of proteins by the enzymatic transfer of ADP-ribose from NAD has been implicated in a number of biological processes. We report that inhibitors of ADP-ribosylation, most notably the novel inhibitor of arginine specific cellular mono(ADP-ribosyl) transferase, meta-iodobenzylguanidine (MIBG) as well as nicotinamide, L-arginine methyl ester (LAME) and guanyltyramine, inhibit histamine-induced endothelial production of inositol phosphates, release of arachidonic acid and production of prostacyclin (PGI2). Those same responses were unaffected by MIBG when triggered by thrombin or leukotriene C4. These findings suggest that ADP-ribosylation serves a role in histamine-induced production of prostacyclin and imply differences in transduction pathways employed by the different agonists.

AB - ADP-ribosylation of proteins by the enzymatic transfer of ADP-ribose from NAD has been implicated in a number of biological processes. We report that inhibitors of ADP-ribosylation, most notably the novel inhibitor of arginine specific cellular mono(ADP-ribosyl) transferase, meta-iodobenzylguanidine (MIBG) as well as nicotinamide, L-arginine methyl ester (LAME) and guanyltyramine, inhibit histamine-induced endothelial production of inositol phosphates, release of arachidonic acid and production of prostacyclin (PGI2). Those same responses were unaffected by MIBG when triggered by thrombin or leukotriene C4. These findings suggest that ADP-ribosylation serves a role in histamine-induced production of prostacyclin and imply differences in transduction pathways employed by the different agonists.

KW - 3-Iodobenzylguanidine

KW - Adenosine Diphosphate Ribose

KW - Cells, Cultured

KW - Endothelium, Vascular

KW - Epoprostenol

KW - Humans

KW - Inositol Phosphates

KW - Iodobenzenes

KW - Signal Transduction

KW - 3-Iodobenzylguanidine

KW - Adenosine Diphosphate Ribose

KW - Cells, Cultured

KW - Endothelium, Vascular

KW - Epoprostenol

KW - Humans

KW - Inositol Phosphates

KW - Iodobenzenes

KW - Signal Transduction

U2 - 10.1016/0014-5793(92)81497-A

DO - 10.1016/0014-5793(92)81497-A

M3 - Article

C2 - 1468563

SN - 0014-5793

JO - FEBS Letters

JF - FEBS Letters

ER -

Role of ADP-ribosylation in endothelial signal transduction and prostacyclin production

Abstract

Other keywords

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