<?xml version="1.0" encoding="utf-8"?><rss version="2.0"><channel><title>RSS for Dendroaspis natriuretic peptide binds to the natriuretic peptide clearance receptor</title><link>http://academic.research.microsoft.com/Rss.aspx?cata=9&amp;id=36262003</link><description>Search RSS feed for Microsoft Academic Search</description><generator>MSRA Libra RSS Burner</generator><copyright>(c)2008 Microsoft Corpration, All right reserved.</copyright><pubDate>Mon, 20 May 2013 13:37:26 GMT</pubDate><lastBuildDate>Mon, 20 May 2013 13:37:26 GMT</lastBuildDate><category /><item><title>Dendroaspis natriuretic peptide binds to the natriuretic peptide clearance receptor</title><link>http://academic.research.microsoft.com/Publication/36262003</link><pubDate>Mon, 20 May 2013 06:37:26 GMT</pubDate><guid isPermaLink="false">3626200312</guid><description><![CDATA[<div><a href="http://academic.research.microsoft.com/Author/55420702">Douglas G.. Johns</a>, <a href="http://academic.research.microsoft.com/Author/24558353">Zhaohui Ao</a>, <a href="http://academic.research.microsoft.com/Author/53903108">Bradley J. Heidrich</a>, <a href="http://academic.research.microsoft.com/Author/55093056">Gerald E. Hunsberger</a>, <a href="http://academic.research.microsoft.com/Author/28437573">Taylor Graham</a>, <a href="http://academic.research.microsoft.com/Author/55251259">Lisa Payne</a>, <a href="http://academic.research.microsoft.com/Author/23390975">Nabil Elshourbagy</a>, <a href="http://academic.research.microsoft.com/Author/52350528">Quinn Lu</a>, <a href="http://academic.research.microsoft.com/Author/23386969">Nambi Aiyar</a>, <a href="http://academic.research.microsoft.com/Author/21298794">Stephen A. Douglas</a>:
            
            <span style="margin-left:20px">(Citations:12)</span><span style="margin-left:20px"><a href="http://www.sciencedirect.com/science/article/pii/S0006291X07008145">view publication</a></span></div><div>Dendroaspis <a href='http://academic.research.microsoft.com/Keyword/27096/natriuretic-peptide'>natriuretic peptide</a>  (DNP) is a newly-described <a href='http://academic.research.microsoft.com/Keyword/27096/natriuretic-peptide'>natriuretic peptide</a>  which lowers <a href='http://academic.research.microsoft.com/Keyword/3698/blood-pressure'>blood pressure</a>  via vasodilation. The <a href='http://academic.research.microsoft.com/Keyword/27096/natriuretic-peptide'>natriuretic peptide</a>  clearance receptor (NPR-C) removes natriuretic peptides from the circulation, but whether DNP interacts with human NPR-C directly is unknown. The purpose of this study was to test the hypothesis that DNP binds to NPR-C. ANP, BNP, CNP, and the NPR-C ligands AP-811 and cANP(4–23) displaced [125I]-ANP from NPR-C with pM-to-nM Ki values. DNP displaced [125I]-ANP from NPR-C with nM potency, which represents the first direct demonstration of binding of DNP to human NPR-C. DNP showed high pM affinity for the GC-A receptor and no affinity for GC-B (Ki&gt;1000nM). DNP was nearly 10-fold more potent than ANP at stimulating cGMP production in GC-A expressing cells. Blockade of NPR-C might represent a novel therapeutic approach in augmenting the known beneficial actions of DNP in cardiovascular diseases such as hypertension and heart failure.</div><div></div><div>Journal: <a href="http://academic.research.microsoft.com/Journal/1452">Biochemical and Biophysical Research Communications - BIOCHEM BIOPHYS RES COMMUN</a>, vol. 358, no. 1, pp. 145-149, 2007</div><div />]]></description></item></channel></rss>