期刊论文详细信息
Cell Structure and Function
Mechanism of the Change in Shape of Human Erythrocytes Induced by Lidocaine
Satoru Ozono1  Eiko Nishiguchi3  Yuichi Takakuwa4  Naotaka Hamasaki2 
[1] Department of Oral Pathology, Kanagawa Dental College;Department of Clinical Chemistry and Laboratory Medicine, Kyushu University;Department of Dental Hygiene, Shonan Junior College;Department of Biochemistry, Tokyo Women's Medical College
关键词: shape change;    human erythrocyte;    lidocaine;    V-ATPase;    carboftie anhydrase;   
DOI  :  10.1247/csf.20.71
学科分类:分子生物学,细胞生物学和基因
来源: Japan Society for Cell Biology
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【 摘 要 】

References(37)Cited-By(6)We studied the mechanism of the lidocaine-induced shape change in human erythrocytes. Immunohistochemical analysis of erythrocytes using spectrin-specific antibodies revealed aggregation of fluorescence in lidocaine-treated cells, while the fluorescence was distributed diffusely in untreated cells. The intracellular pH in lidocaine-treated erythrocytes was examined by flow cytometry of the cells labeled with 3'-aeetyl-2'-carboxyethyl-6', 7'-(dihydropyran-2'-one)-5-carboxyfluorescein diacethoxymethylester (BCECF-AM), and was found to decrease with increasing concentrations of lidocaine. Pre-treatment of erythrocytes with acetazolamide, an inhibitor of carbonic anhydrase, inhibited the lidocaine-induced spectrin aggregation and decrease in intracellular pH. When erythrocytes were incubated in medium containing bafilomycin A1, an inhibitor of V-ATPase, followed by incubation with lidocaine, the cells changed shape slightly and the intracellular pH showed a small decrease in comparison with control. Spectrin dimers extracted from membranesof normal erythrocytes were incubated in buffers of various pHs and analyzed by SDS-PAGE. The amounts of spectrin dimers and tetramers decreased, while that of oligomers increased with decreasing pH. These results suggest that the lidocaine-induced shape change in human erythrocytes may occur by the conformational change of spectrin in a process that may be mediated by carbonic anhydrase and activation of V-ATPase.

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