Differential signal transduction by five splice variants of the PACAP receptor
Identifieur interne : 004584 ( Main/Exploration ); précédent : 004583; suivant : 004585Differential signal transduction by five splice variants of the PACAP receptor
Auteurs : Dietmar Spongier ; Christian Waeber ; Colette Pantaloni ; Florian Holsboer ; Jol Bockaert ; Peter H. Seeburgt ; Laurent JournotSource :
- Nature [ 0028-0836 ] ; 1993-09-09.
Abstract
THE two forms of pituitary adenylyl cyclase-activating polypeptide (PACAP-27 and -38) are neuropeptides of the secretin/glucagon/ vasoactive intestinal polypeptide/growth-hormone-releasing hor-mone family and regulate hormone release from the pituitary and adrenal gland13. They may also be involved in spermatogenesis4, and PACAP-38 potently stimulates neuritogenesis and survival of cultured rat sympathetic neuroblast5,6 and promotes neurite out-growth of PC-12 cells7. The PACAP type-I receptor (found in hypothalamus, brain stem, pituitary, adrenal gland and testes), specific for PACAP, is positively coupled to adenylyl cyclase and phospholipase C. The recently cloned type II receptor does not discriminate between PACAP and vasoactive intestinal polypeptide and is coupled to only adenylyl cyclase8. Here we have used a new expression cloning strategy, based on the induction of a reporter gene by cyclic AMP, to isolate a complementary DNA encoding the type-I PACAP receptor. On transfection of this cDNA, both PACAP-27 and -38 stimulate adenylyl cyclase with similar EC50 values (50% effective concentration, 0.10.4 nM), whereas only PACAP-38 stimulates phospholipase C with high potency (EC50 = 15 nM). Four other splice variants were isolated with insertions at the C-terminal end of the third intracellular loop. Expression of these cDNAs revealed altered patterns of adenylyl cyclase and phospholipase C stimulation, suggesting a novel mechanism for fine tuning of signal transduction.
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DOI: 10.1038/365170a0
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Seeburgt</name></author><author><name sortKey="Journot, Laurent" sort="Journot, Laurent" uniqKey="Journot L" first="Laurent" last="Journot">Laurent Journot</name></author></analytic><monogr></monogr><series><title level="j" type="main">Nature</title><imprint><publisher>Nature Publishing Group</publisher><date when="1993-09-09">1993-09-09</date><biblScope unit="vol">365</biblScope><biblScope unit="issue">6442</biblScope><biblScope unit="page" from="170">170</biblScope><biblScope unit="page" to="175">175</biblScope><date type="Copyright" when="1993">1993</date></imprint><idno type="ISSN">0028-0836</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0028-0836</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract">THE two forms of pituitary adenylyl cyclase-activating polypeptide (PACAP-27 and -38) are neuropeptides of the secretin/glucagon/ vasoactive intestinal polypeptide/growth-hormone-releasing hor-mone family and regulate hormone release from the pituitary and adrenal gland13. They may also be involved in spermatogenesis4, and PACAP-38 potently stimulates neuritogenesis and survival of cultured rat sympathetic neuroblast5,6 and promotes neurite out-growth of PC-12 cells7. The PACAP type-I receptor (found in hypothalamus, brain stem, pituitary, adrenal gland and testes), specific for PACAP, is positively coupled to adenylyl cyclase and phospholipase C. The recently cloned type II receptor does not discriminate between PACAP and vasoactive intestinal polypeptide and is coupled to only adenylyl cyclase8. Here we have used a new expression cloning strategy, based on the induction of a reporter gene by cyclic AMP, to isolate a complementary DNA encoding the type-I PACAP receptor. On transfection of this cDNA, both PACAP-27 and -38 stimulate adenylyl cyclase with similar EC50 values (50% effective concentration, 0.10.4 nM), whereas only PACAP-38 stimulates phospholipase C with high potency (EC50 = 15 nM). Four other splice variants were isolated with insertions at the C-terminal end of the third intracellular loop. Expression of these cDNAs revealed altered patterns of adenylyl cyclase and phospholipase C stimulation, suggesting a novel mechanism for fine tuning of signal transduction.</div></front></TEI><affiliations><list></list><tree><noCountry><name sortKey="Bockaert, Jol" sort="Bockaert, Jol" uniqKey="Bockaert J" first="Jol" last="Bockaert">Jol Bockaert</name><name sortKey="Holsboer, Florian" sort="Holsboer, Florian" uniqKey="Holsboer F" first="Florian" last="Holsboer">Florian Holsboer</name><name sortKey="Journot, Laurent" sort="Journot, Laurent" uniqKey="Journot L" first="Laurent" last="Journot">Laurent Journot</name><name sortKey="Pantaloni, Colette" sort="Pantaloni, Colette" uniqKey="Pantaloni C" first="Colette" last="Pantaloni">Colette Pantaloni</name><name sortKey="Seeburgt, Peter H" sort="Seeburgt, Peter H" uniqKey="Seeburgt P" first="Peter H." last="Seeburgt">Peter H. Seeburgt</name><name sortKey="Spongier, Dietmar" sort="Spongier, Dietmar" uniqKey="Spongier D" first="Dietmar" last="Spongier">Dietmar Spongier</name><name sortKey="Waeber, Christian" sort="Waeber, Christian" uniqKey="Waeber C" first="Christian" last="Waeber">Christian Waeber</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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