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(Received for publication, April 16, 1996)
From CNRS-UPR 9023, Centre CNRS-INSERM de
Pharmacologie-Endocrinologie, rue de la Cardonille, F-34094 Montpellier
Cedex 05, France and § Molecular Neuroendocrinology, Max
Planck Institute of Psychiatry, Kraepelinstrasse,
2, D-80804 Munich, Federal Republic of Germany
Pituitary adenylate cyclase-activating
polypeptide (PACAP)-27 and PACAP-38 are neuropeptides of the vasoactive
intestinal peptide/secretin/glucagon family. We previously described
alternative splicing of the region encoding the third intracellular
loop of the PACAP receptor generating six isoforms with differential
signal transduction properties (Spengler, D., Waeber, C., Pantaloni,
C., Holsboer, F., Bockaert, J., Seeburg, P. H., and Journot, L. (1993)
Nature 365, 170-175). In addition, we demonstrated that
the potencies of the two forms of PACAP are similar for adenylate
cyclase stimulation, whereas PACAP-38 is more potent than PACAP-27 in
phospholipase C activation. In the present work, we document the
existence of a new splice variant of the PACAP receptor that was
characterized by a 21-amino-acid deletion in the N-terminal
extracellular domain. We demonstrate that this domain modulates
receptor selectivity with respect to PACAP-27 and -38 binding and
controls the relative potencies of the two agonists in phospholipase C
stimulation.
Volume 271, Number 36,
Issue of September 6, 1996
pp. 22146-22151
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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