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By Toshihiro Uesaka, Keiichi Yano and Motoo Yamasaki


Four somatostatin-related peptides were isolated from eel guts. Two of them were the same as eel SS-25II (eSS-25II) and eel SS-25I (eSS-25I) isolated from European eel pancreas. The remaining two peptides were C-terminal tetradecapeptides (eSS-14II and eSS-14I) of eSS25II and eSS-25I, respectively. These four peptides all enhanced the serosa-negative transepithelial potential difference and short-circuit current across the seawater eel intestine after pretreatment with isobutylmethylxanthine, serotonin (5-HT) and methacholine, an agonist of acetylcholine (ACh). Among these peptides, eSS-25II was the most potent enhancer, followed by eSS-25I and eSS-14II. Since the large peptide (eSS-25II) acts at a lower concentration than the small somatostatin (eSS-14II), the 11 N-terminal amino acid residues seem to potentiate somatostatin action in the eel intestine. In contrast, eSS-14II was more potent than mammalian SS-14, indicating that the three amino acid residues (Tyr 18, Gly 21, Pro 22) in the C-terminal portion also contribute to the potency of somatostatin. Endogenous somatostatin (eSS-25II) activated net Na +, Cl � and water fluxes across the seawater eel intestine. This stimulatory action was not inhibited by tetrodotoxin or yohimbine, an adrenergic antagonist, indicating that eSS-25II does not act through neuronal firing or through catecholamine release. Thus, eel somatostatins may act directly on the enterocytes, but on a distinct receptor from that for adrenaline, to antagonize the inhibition of NaCl and water absorption by 5-HT and ACh in the seawater eel intestine

Topics: Key words, somatostatin, HPLC purification, ion
Year: 1993
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