Expression of chloride channel, CIC-5, and its role in receptor-mediated endocytosis of albumin in OK cells

被引：23

作者：

Sasaki, Y ^{[1
]}

Nagai, J ^{[1
]}

Kitahara, Y ^{[1
]}

Takai, N ^{[1
]}

Murakami, T ^{[1
]}

Takano, M ^{[1
]}

机构：

[1] Hiroshima Univ, Fac Med, Inst Pharmaceut Sci, Minami Ku, Hiroshima 7348551, Japan

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2001年 / 282卷 / 01期

关键词：

receptor-mediated endocytosis; albumin; chloride channel; culture cell; vacuolar H+-ATPase; Dent's disease;

D O I：

10.1006/bbrc.2001.4557

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

By using Western blot and RT-PCR analyses, the expression of ClC-5, a member of the CIC family of voltage-gated chloride channels, and its mRNA was detected in OK cells. The effect of chloride channel inhibitors on receptor-mediated endocytosis of albumin was examined in OK cells and compared to that of vacuolar H+-ATPase inhibitors. Accumulation of fluorescein-isothiocyanate (FITC)-albumin, a receptor-mediated endocytosis marker, was inhibited by 5-nitro-2-(3-phenylpropylamino)-benzoic acid (NPPB), a chloride channel inhibitor, in a concentration-dependent fashion. In contrast, uptake of FITC-inulin, a fluid-phase endocytosis marker, was not affected by NPPB. Other chloride channel inhibitors, 4,4'-diisothiocyanatostilbene-2-2'-disulfonic acid and diphenylamine-2-carboxylic acid, also inhibited FITC-albumin uptake. NPPB, as well as a vacuolar H+-ATPase inhibitor bafilomycin A(1), caused a decrease in the affinity and in the maximal velocity of FITC-albumin uptake. These results suggest that chloride channel, most likely ClC-5, plays an important role in the receptor-mediated endocytosis of albumin in OK cells. (C) 2001 Academic Press.

引用

页码：212 / 218

页数：7

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