Brief Reports
Copyright ©The Author(s) 2004. Published by Baishideng Publishing Group Inc. All rights reserved.
World J Gastroenterol. Jun 1, 2004; 10(11): 1666-1668
Published online Jun 1, 2004. doi: 10.3748/wjg.v10.i11.1666
Filamentous-actins in human hepatocarcinoma cells with CLSM
Xia Huo, Xi-Jin Xu, Yao-Wen Chen, Hai-Wei Yang, Zhong-Xian Piao
Xia Huo, Xi-Jin Xu, Yao-Wen Chen, Hai-Wei Yang, Zhong-Xian Piao, Central Laboratory, Shantou University Medical College, Shantou 515031, Guangdong Province, China
Author contributions: All authors contributed equally to the work.
Correspondence to: Dr. Xia Huo, Central Laboratory, Shantou University Medical College, 22 Xinlin Road, Shantou 515031, Guangdong Province, China. xhuo@stu.edu.cn
Telephone: +86-754-8900307 Fax: +86-754-8557562
Received: December 30, 2002
Revised: January 4, 2003
Accepted: February 17, 2003
Published online: June 1, 2004
Abstract

AIM: To establish a method for optical sections of HepG2 human hepatoblastoma cells with confocal laser scanning microscope (CLSM) and to study the spatial structure of filamentous actin (F-actin) in HepG2 cells.

METHODS: HepG2 cells were stained with FITC-phalloidin that specifically binds F-actin, with propidium iodide (PI) to the nucleus, and scanned with a CLSM to generate optically sectioned images. A series of optical sections taken successively at different focal levels in steps of 0.7 mm were reconstructed with the CLSM reconstruction program.

RESULTS: CLSM images showed that the FITC-stained F-actin was abundant microfilament bundles parallel or netted through the whole cell and its processes. Most F-actin microfilaments extended through the cell from one part toward the other or run through the process. Some microfilaments were attached to the plasma membrane, or formed a structural bridge connecting to the neighboring cells.

CONCLUSION: A method for double labeling HepG2 human hepatoblastoma cells and CLSM imaging F-actin microfilaments and nuclei by image thin optical sections and spatial structure was developed. It provides a very useful way to study the spatial structure of F-actin.

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