• Title/Summary/Keyword: Osmoregulatory receptor

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Expression of Prolactin Receptor mRNA and Blood Physiological Responses to Salinity Changes in the Black Porgy Acanthopagrus schlegeli (염분 변화에 따른 감성돔 Acanthopagrus schlegeli의 Prolactin Receptor(PRLR) mRNA 발현 및 생리적 반응)

  • An, Kwang-Wook;Min, Byung-Hwa;Park, In-Seok;Heo, Youn-Seong; Choi, Yong-Ki;Jo, Pil-Gue;Chang, Young-Jin;Choi, Cheol-Young
    • Journal of Aquaculture
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    • v.21 no.2
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    • pp.63-69
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    • 2008
  • We isolated complementary DNA(cDNA) encoding prolactin receptor(PRLR) from gill of black porgy Acanthopagrus schlegeli. Its PRLR cDNA consists of 1,611 base pairs and encodes the protein of 536 amino acids. To investigate the osmoregulatory abilities of black porgy in different salinities(35, 10 and 0 psu), we examined the expression of PRLR mRNA in osmoregulatory organs(gill, kidney and intestine) using reverse transcription(RT)-PCR. In gill and intestine, PRLR mRNA levels were high in 10 psu, and then decreased in 0 psu, but there is no changes in kidney. Also, plasma osmolality, $Na^+\;and\;Cl^-$ levels decreased during the experimental period. These results suggest that PRLR plays an important role in hormonal regulation in osmoregulatory organs during freshwater acclimation, thereby improving the hyper-osmoregulatory ability of black porgy in hypoosmotic environments.

A New Receptor for site Clonidine in the Eel, Anguilla japonica Intestine (뱀장어(Anguilla japonica)장의 상피세포막에 존재하는 새로운 clonidine 결합 수용체에 관한 연구)

  • Kim, Hung-Tae;Seo, Jung-Soo;Park, Nam-Gyu;Lee, Hyung-Ho;Chung, Joon-Ki
    • Journal of fish pathology
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    • v.14 no.1
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    • pp.31-36
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    • 2001
  • A novel clonidine binding sites were characterized in the intestinal membrane isolated from seawater eels, Anguilla japonica. The specific clonidine binding sites consisted of at least two classes, high affinity ($K_d=1.4{\pm}0.3$ nM n = 5) and low affinity ($K_d=175{\pm}34$ nM n = 5) sites. The specific binding of 2 nM [$^3H$]clonidine was most enhanced at $20^{\circ}C$ and pH 7.5, and reversed by unlabelled clonidine. Such binding was hardly inhibited by adrenaline, yohimbine or rauwolscine, indicating that most binding sites are distinct from $\alpha_2$-adrenoceptor. The specific clonidine binding sites was inhibited by various imidazoline/guanidinium drugs, indicating existence of imidazoline/guanidinium receptive sites (IGRS) or imidazoline receptors in the eel intestine. Competition experiments revealed that rank order to displace 2 nM [$^3H$]clonidine from their binding sites was as follows : guanabenz > cirazoline = naphazoline = UK14,304 = ST587 $\geq$ clonidine $\geq$ idazoxan = RX821002 = tolazoline > ST93 = oxymetazoline = amiloride = ST91 > yohimbine = efaroxan = rauwolscine $\geq$ adrenaline = ST567 = histamine = agmatine. Although physiological role of IGRS is not clear yet even in mammalian cell/tissues, eel intestine may be a good model to elucidate how the IGRS act in the cell and to decide what is the endogenous ligand for the IGRS.

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