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一氧化氮合酶活性不影响小鼠胰腺β细胞的电活动。

NO synthase activity does not influence electrical activity of mouse pancreatic B-cells.

作者信息

Drews G, Krippeit-Drews P

机构信息

Department of Physiology, University of Tübingen, FRG.

出版信息

Biochem Biophys Res Commun. 1995 May 25;210(3):914-20. doi: 10.1006/bbrc.1995.1744.

Abstract

The membrane potential of mouse pancreatic B-cells was recorded with intracellular microelectrodes. At a low concentration the NO synthase inhibitor N omega-nitro-L-arginine methyl ester (L-NAME, 100 mumol/l) did not alter electrical activity induced by 15 mmol/l glucose. At 5 mmol/l L-NAME depolarized B-cells similarly to L-arginine. The depolarization of the B-cell membrane induced by 5 mmol/l L-arginine in the presence of 15 mmol/l glucose was not inhibited but further increased by the addition of 15 mmol/l L-NAME. D-arginine which is not used as a substrate by the NO synthase also depolarized the B-cells. However, higher concentrations were necessary than for L-arginine pointing to a preferential transport of the L-enantiomer. It is concluded that the electrical activity of pancreatic B-cells is not influenced by the NO synthase and that the enzyme is not involved in the arginine-induced depolarization of B-cells.

摘要

用细胞内微电极记录小鼠胰腺β细胞的膜电位。在低浓度时,一氧化氮合酶抑制剂Nω-硝基-L-精氨酸甲酯(L-NAME,100μmol/l)不会改变由15mmol/l葡萄糖诱导的电活动。在5mmol/l时,L-NAME使β细胞去极化的情况与L-精氨酸相似。在存在15mmol/l葡萄糖的情况下,5mmol/l L-精氨酸诱导的β细胞膜去极化并未受到抑制,反而因添加15mmol/l L-NAME而进一步增强。一氧化氮合酶不作为底物使用的D-精氨酸也使β细胞去极化。然而,所需的浓度比L-精氨酸更高,这表明L-对映体具有优先转运性。结论是胰腺β细胞的电活动不受一氧化氮合酶的影响,且该酶不参与精氨酸诱导的β细胞去极化。

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