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Disruption of tubulin polymerization and cell proliferation by 1‐naphthylarsonic acid
Author(s) -
Mahinpour Roya,
Riazi Gholamhossein,
Shokrgozar Mohammad A.,
Sarbolouki Mohammad N.,
Ahmadian Shahin,
Douraghi Masoumeh,
Alijanvand Hamid Hadi,
Azadmanesh Kayhan,
Heidari Maryam,
Gheshlaghi Zahra Naghdi,
MoosaviMovahedi Ali A.
Publication year - 2012
Publication title -
cell biology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.932
H-Index - 77
eISSN - 1095-8355
pISSN - 1065-6995
DOI - 10.1042/cbi20100603
Subject(s) - hela , tubulin , microtubule , chemistry , in vitro , microbiology and biotechnology , cancer cell , biophysics , polymerization , biochemistry , biology , polymer , cancer , genetics , organic chemistry
Arsenical compounds exhibit a differential toxicity to cancer cells. Microtubules are a primary target of a number of anticancer drugs, such as arsenical compounds. The interaction of 1‐NAA (1‐naphthylarsonic acid) has been investigated on microtubule polymerization under in vitro and cellular conditions. Microtubules were extracted from sheep brain. Transmission electron microscopy was used to show microtubule structure in the presence of 1‐NAA. Computational docking method was applied for the discovery of ligand‐binding sites on the microtubular proteins. Proliferation of HeLa cells and HF2 (human foreskin fibroblasts) was measured by the MTT [3‐(4,5‐dimethylthiazol‐2‐yl)‐2,5‐diphenyl‐2 H ‐tetrazolium bromide] assay method following their incubation with 1‐NAA. Fluorescence microscopic labelling was done with the help of α‐tubulin monoclonal antibody and Tunel kit was used to investigate the apoptotic effects of 1‐NAA on the HeLa cells. 1‐NAA inhibits the tubulin polymerization by the formation of abnormal polymers having high affinity to the inner cell wall.