Competitive binding of musclin to natriuretic peptide receptor 3 with atrial natriuretic peptide
Competitive binding of musclin to natriuretic peptide receptor 3 with atrial natriuretic peptide
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DOI：
10.1677/joe-08-0551
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发表时间：
2009-05-01
影响因子：
4
通讯作者：
Shimomura, Iichiro
中科院分区：
文献类型：
--
作者：
Kita, Shunbun;Nishizawa, Hitoshi;Shimomura, Iichiro
Musclin是本课题组分离到的一种新的骨骼肌源性分泌因子。肌蛋白含有与利钠肽（NPs）同源的区域。本研究探讨了肌肉素和NP受体（NPRs）之间的相互作用。Musclin特异性结合NPR 3，但不结合NPR 1或NPR 2。Musclin和心房利钠肽（ANP）竞争结合NPR 3。我们使用各种合成肌肉蛋白肽和突变肌肉蛋白进行结合测定。musclin中的第一NP同源区（（LDRL 91）-L-88）和第二同源区（（MDRI 120）-M-117）协同负责与NPR 3的高亲和力结合。第一个NP同源区比第二个同源区更重要地与NPR 3结合。在体内也证实了musclin与ANP对利钠素清除受体NPR 3的竞争性质。我们的结论是，肌肉蛋白结合NPR 3竞争性与ANP和许多影响ANP浓度在局部或全身的方式。内分泌学杂志（2009）201，287-295
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 ((LDRL91)-L-88) and the second homologous region ((MDRI120)-M-117) 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 ill vivo. We conclude that musclin binds to NPR3 competitively with ANP and many affect ANP concentrations in a local or systemic manner. Journal of Endocrinology (2009) 201, 287-295