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Mol. Cells 2004; 18(1): 46-52

Published online January 1, 1970

© The Korean Society for Molecular and Cellular Biology

Aurintricarboxylic Acid Translocates across the Plasma Membrane, Inhibits Protein Tyrosine Phosphatase and Prevents Apoptosis in PC12 Cells

Hyeongjin Cho, Dong Yoon Lee, Suja Shrestha, Yi Sup Shim, Ki Chul Kim, Mee-Kyung Kim, Keun-Hyeung Lee, Jonghwa Won, Jae-Seung Kang

Abstract

Aurintricarboxylic acid (ATA) prevents apoptosis in a diverse range of cell types including PC12 cells. It is known to stimulate tyrosine phosphorylation of signaling proteins including Shc proteins, phosphatidylinositol 3-kinase, phospholipase C-g and mitogen-activated protein kinases (MAPKs). However, it has been unclear how ATA increases the phosphorylation of these proteins as it was believed to be membrane impermeable. We found that ATA translocates across the plasma membrane of PC12 cells and have confirmed that it is a potent inhibitor of protein tyrosine phosphatases (PTP ases). Other PTPase inhibitors also prevented apoptosis independent of ATA. These observations indicate that ATA exerts its anti-apoptotic effect on PC12 cells at least in part by inhibiting certain PTPase(s).

Keywords Apoptosis; Aurintricarboxylic Acid; Inhibitor; PC12 Cells; Permeability; Protein Tyrosine Phosphatase

Article

Research Article

Mol. Cells 2004; 18(1): 46-52

Published online August 31, 2004

Copyright © The Korean Society for Molecular and Cellular Biology.

Aurintricarboxylic Acid Translocates across the Plasma Membrane, Inhibits Protein Tyrosine Phosphatase and Prevents Apoptosis in PC12 Cells

Hyeongjin Cho, Dong Yoon Lee, Suja Shrestha, Yi Sup Shim, Ki Chul Kim, Mee-Kyung Kim, Keun-Hyeung Lee, Jonghwa Won, Jae-Seung Kang

Abstract

Aurintricarboxylic acid (ATA) prevents apoptosis in a diverse range of cell types including PC12 cells. It is known to stimulate tyrosine phosphorylation of signaling proteins including Shc proteins, phosphatidylinositol 3-kinase, phospholipase C-g and mitogen-activated protein kinases (MAPKs). However, it has been unclear how ATA increases the phosphorylation of these proteins as it was believed to be membrane impermeable. We found that ATA translocates across the plasma membrane of PC12 cells and have confirmed that it is a potent inhibitor of protein tyrosine phosphatases (PTP ases). Other PTPase inhibitors also prevented apoptosis independent of ATA. These observations indicate that ATA exerts its anti-apoptotic effect on PC12 cells at least in part by inhibiting certain PTPase(s).

Keywords: Apoptosis, Aurintricarboxylic Acid, Inhibitor, PC12 Cells, Permeability, Protein Tyrosine Phosphatase

Mol. Cells
Jun 30, 2023 Vol.46 No.6, pp. 329~398
COVER PICTURE
The cellular proteostasis network is adaptively modulated upon cellular stress, thereby protecting cells from proteostasis collapse. Heat shock induces the translocation of misfolded proteins and the chaperone protein HSP70 into nucleolus, where nuclear protein quality control primarily occurs. Nuclear RNA export factor 1 (green), nucleolar protein fibrillarin (red), and nuclei (blue) were visualized in NIH3T3 cells under basal (left) and heat shock (right) conditions (Park et al., pp. 374-386).

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