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Biotech / Medical : Cadus Pharmaceutical Corp. (KDUS) -- Ignore unavailable to you. Want to Upgrade?

To: BulbaMan who wrote (728)	2/19/2002 1:40:07 AM
From: scaram(o)uche	Read Replies (1) \| Respond to of 1833

L. Silverman was an author on some (several?) publications from Cadus. I presume, but do not know, that this "pheromone-signaling pathway" is the same that we've grown to love (and hate).......... J Biol Chem 2001 Dec 3; [epub ahead of print] Functional expression of heteromeric CGRP and Adrenomedullin receptors in yeast. Miret JJ, Rakhilina L, Silverman L, Oehlen B. OSI Pharmaceuticals, Inc., Tarrytown, NY 10591. The ability of G protein-coupled receptors (GPCRs) to form homo- and heteromeric complexes has important implications for the regulation of cellular events. A notable example of heteromer formation is the interaction of the Calcitonin Receptor Like Receptor (CRLR) with different members of the Receptor Activity Modifying Protein (RAMP) family, which results in the formation of two different receptors: a calcitonin gene related peptide (CGRP) receptor and an adrenomedullin (ADM) receptor. In order to analyze the role of RAMPs in determining ligand specificity, we have co-expressed CRLR and RAMP proteins in the yeast Saccharomyces cerevisiae, which provides a null system to study the function of mammalian receptors. Co-expression of RAMP1 and CRLR reconstituted a CGRP receptor that was able to activate the pheromone-signaling pathway with pharmacological properties similar to those observed previously in mammalian cells. Co-expression of CRLR with RAMP2 or RAMP3 resulted in a response with the pharmacological properties of an ADM receptor. These data indicate that RAMPs are necessary and sufficient to determine ligand specificity of CRLR. Contrary to observations in mammalian cells, the glycosylation of CRLR was not affected by the presence of RAMPs in yeast, indicating that glycosylation of CRLR is not the prime determinant of ligand specificity. The first functional reconstitution of a heteromeric seven transmembrane receptor in yeast suggests this organism as a useful research tool to study the molecular nature of other heteromeric receptors.