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This Article Full Text Full Text (PDF) All Versions of this Article: JOE-08-0551v1 201/2/287    most recent Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Kita, S. Articles by Shimomura, I. Search for Related Content PubMed PubMed Citation Articles by Kita, S. Articles by Shimomura, I.

¹ Pharmaceutical Research Division, Pharmacology Research Laboratories I, Takeda Pharmaceutical Company Ltd, Yodogawa-ku, Osaka 532-8686, Japan² Department of Metabolic Medicine, Graduate School of Medicine³ Department of Medicine and Pathophysiology, Graduate School of Frontier Bioscience, Osaka University, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan

(Correspondence should be addressed to I Shimomura; Email: ichi{at}imed2.med.osaka-u.ac.jp; S Kita; Email: kita_shunbun{at}takeda.co.jp)

Musclin is a novel skeletal muscle-derived secretory factor that was isolated by our group. Musclin contains a region homologous to natriuretic peptides (NPs). This study investigated the interaction between musclin and NP receptors (NPRs). Musclin specifically bound to NPR3, but not to NPR1 or NPR2. Musclin and atrial natriuretic peptide (ANP) competed for binding to NPR3. We conducted binding assays using various synthetic musclin peptides and mutant musclin proteins. The first NP-homologous region in musclin (⁸⁸LDRL⁹¹) and the second homologous region (¹¹⁷MDRI¹²⁰) were responsible cooperatively for high-affinity binding to NPR3. The first NP-homologous region was more importantly associated with binding to NPR3, than the second homologous region. The competitive nature of musclin with ANP for the natriuretic clearance receptor NPR3 was also confirmed in vivo. We conclude that musclin binds to NPR3 competitively with ANP and may affect ANP concentrations in a local or systemic manner.