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KMID : 0811720040080000190
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Korean Journal of Physiology & Pharmacology
2004 Volume.8 No. 0 p.190 ~ p.0
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Distribution and Characterization of Natriuretic Peptide Receptors in the Gills of the Boleophthalmus Pectinirostris
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Kim So-Young
Park Sung-Hun
Kim Sun-Young
Cho Kyung-Woo
Kim Sun-Hee
Kim Sung-Zoo
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Abstract
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The gill is a major respiratory organ in fishes which allows them to survive in the water, and natriuretic peptides have been implicated in regulation of fluid homeostasis. In this study, specific binding of iodinated rat atrial natriuretic peptide (125I-APⅢ) and iodinated porcine C-type natriuretic peptide (125I-CNP) was examined in the gills of the goby Boleophthalmus pectinirostris (Class Actinopterygii family Gobiidae) using in vitro receptor autoradiography, membrane binding assay, affinity cross-linking. Autoradiographs showed specific and saturable binding on the lamellar folds and cavernous tissue of B. pectinirostris gills. In vitro analysis of the binding sites demonstrated that 125I-APⅢ and 125I-CNP were bound to natriuretic peptide receptor (NPR) sites with a similar affinity. Affinity cross-linking of 125I-APⅢ and 125I-CNP to gill membranes followed by SDS-PAGE revealed a single binding site of approximately 110kDa, with no appreciable observation of a mammalian type NPR-C at a lower estimated molecular mass. But Western blotting of cross-linking of 125I-APⅢ to gill memebranes followed by SDS-PAGE revealed two binding site of approximately 80kDa and 110kDa. Natriuretic peptides increased cGMP production in gill membranes with a rank order of potency of chANP＞chCNP＞rCNP＞rANP＞fCNP＞fANP＞eANP, and C-ANP did not stimulate cGMP production. These data suggest the existence of NPRs of gill membrane similar to the mammalian NPR-A/B or NPR-C. But their molecular mass may are not homologous with mammalian NPRs.
Source: Korean Journal of Physiology & Pharmacology.2004 Oct;8(Suppl I):S140-S140
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KEYWORD
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Natriuretic peptide receptor, cGMP Stimulation, Fish, Natriuretic peptide
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