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Volume 271, Number 43, Issue of October 25, 1996 pp. 26473-26476
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

COMMUNICATION:
Human Immunoglobulins Inhibit Thrombin-induced Ca2+ Movements and Nitric Oxide Production in Endothelial Cells

(Received for publication, July 8, 1996, and in revised form, August 12, 1996)

Olivier Schussler Dagger , Frédérique Lantoine § , Marie-Aude Devynck , Denis Glotz Dagger and Monique David-Dufilho

From the Department of Pharmacology, URA CNRS 1482, Paris V University, Necker University School of Medicine, 156 rue de Vaugirard, 75015, Paris, France, the § Laboratoire d'Electrochimie et de Chimie Analytique, CNRS URA 216, Ecole Nationale Supérieure de Chimie Paris, 11 rue Pierre et Marie Curie, 75231 Paris Cedex 05, France, and Dagger  INSERM U430, Laboratoire d'Immunologie-Pathologie Humaine, Hôpital Broussais, 96 rue Didot, 75674 Paris, France

Binding of natural antibodies to endothelial cell plays an important role in hyperacute xenograft rejection between discordant species. Human intravenous immunoglobulins (IVIg) delay this hyperacute rejection, but their mechanisms of action on endothelial cells have to be defined. Here we demonstrate that IVIg dose-dependently prevent thrombin from eliciting cytosolic Ca2+ movements and nitric oxide (NO) production in aortic endothelial cells from guinea pig. The Ca2+ response to thrombin was similarly affected by IVIg whether they were removed or not from the incubation medium before stimulation. Pretreatment by rat natural antibodies also suppress the thrombin-induced Ca2+ peak corresponding to Ca2+ release from intracellular stores but stimulate the subsequent sustained increase in [Ca2+]i and the release of NO. The action of human intravenous immunoglobulins seems to be selective for the thrombin receptor because they do not affect [Ca2+]i and NO responses to endothelin-1 or thapsigargin. However, these antibodies also suppress the first phase of the cytosolic Ca2+ response to ATP, which does not release NO under our experimental conditions. These observations raise the possibility that IVIg selectively interact with targets localized on plasma membrane of endothelial cells for controlling receptor-activated Ca2+ pathways and NO release.


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