Gastric Cancer
Copyright ©The Author(s) 2002. Published by Baishideng Publishing Group Inc. All rights reserved.
World J Gastroenterol. Jun 15, 2002; 8(3): 441-445
Published online Jun 15, 2002. doi: 10.3748/wjg.v8.i3.441
Expression and function of classical protein kinase C isoenzymes in gastric cancer cell line and its drug-resistant sublines
Ying Han, Zhe-Yi Han, Xin-Min Zhou, Ru Shi, Yue Zheng, Yong-Quan Shi, Ji-Yan Miao, Bo-Rong Pan, Dai-Ming Fan
Ying Han, Zhe-Yi Han, Xin-Min Zhou, Yong-Quan Shi, Ji-Yan Miao, Dai-Ming Fan, Institute of Digestive Disease, Xijing Hospital, Fourth Military Medical University, Xi’an 710032, Shaanxi Province, China
Ru Shi, Department of Pharmacology and Reagents, Xijing Hospital, Fourth Military Medical University, Xi’an 710032, Shaanxi Province, China
Yue Zheng, the 6th Undergraduate Section, Fourth Military Medical University, Xi’an 710032, Shaanxi Province, China
Bo-Rong Pan, Oncology Center of Xijing Hospital, Fourth Military Medical University, Xi’an 710032, Shaanxi Province, China
Author contributions: All authors contributed equally to the work.
Supported by the National Nature Science Fundation of China, No. 30030140 and No. 30000066.
Correspondence to: Dai-Ming Fan, Institute of Digestive Disease, Xijing Hospital, Fourth Military Medical University, Xi’an 710032, Shaanxi Province, China. fandaim@fmmu.edu.cn
Telephone: +86-29-3375221 Fax:+86-29-2539041
Received: November 2, 2001
Revised: November 15, 2001
Accepted: December 6, 2001
Published online: June 15, 2002
Abstract

AIM: To investigate the expression and function of classical protein kinase C (PKC) isoenzymes in inducing MDR phenotype in gastric cancer cells.

METHODS: Two cell lines were used in the study: gastric cancer cell SGC7901 and its drug-resistant cell SGC7901/VCR stepwise-selected by vincristine 0.3, 0.7 and 1.0 mg·L-1, respectively. The expression of classical PKC (cPKC) isoenzymes in SGC7901 cells and SGC7901/VCR cells were detected using immunofluorescent cytochemistry, laser confocal scanning microscope and Western blot. The effects of anti-PKC isoenzymes antibody on adriamycin accumulation in SGC7901/VCR cells were determined using flow cytometric analysis.

RESULTS: (1) SGC7901 cells exhibited positive staining of PKC-α. SGC7901/VCR cells exhibited stronger staining of PKC-α than SGC7901 cells. The higher dosage vincristine selected, the much stronger staining of PKC-α was observed on SGC7901/VCR cells. (2) Both SGC7901 and SGC7901/VCR cells exhibited positive staining of PKC-β I and PKC-β II with no significant difference. (3) Compared with SGC7901, SGC7901/VCR cells had decreased adriamycin accumulation and retention. Accumulation of adriamycin in SGC7901 was 5.21 ± 2.56 mg·L-1, in SGC7901/VCR 0.3 was 0.85 ± 0.29 mg·L-1, in SGC7901/VCR 0.7 was 0.81 ± 0.32 mg·L-1, and in SGC7901/VCR 1.0 was 0.80 ± 0.33 mg·L-1; Retention of adriamycin in SGC7901 was 2.51 ± 1.23 mg·L-1, in SGC7901/VCR 0.3 was 0.47 ± 0.14 mg·L-1, in SGC7901/VCR 0.7 was 0.44 ± 0.15 mg·L-1, and in SGC7901/VCR 1.0 was 0.41 ± 0.11 mg·L-1. (4) Fluorescence intensity presented adriamycin accumulation in SGC7901/VCR cells was increased from 1.14 ± 0.36 to 2.71 ± 0.94 when cells were co-incubated with anti-PKC-α but not with anti-PKC-β I, PKC-α II and PKCγ antibodies.

CONCLUSION: PKC-α, but not PKC-β I, PKC-β II or PKCγ, may play a role in multidrug resistance of gastric cancer cells SGC7901/VCR.

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