Full Text:   <3128>

CLC number: Q81

On-line Access: 2024-08-27

Received: 2023-10-17

Revision Accepted: 2024-05-08

Crosschecked: 0000-00-00

Cited: 1

Clicked: 5873

Citations:  Bibtex RefMan EndNote GB/T7714

-   Go to

Article info.
Open peer comments

Journal of Zhejiang University SCIENCE B 2008 Vol.9 No.9 P.701-706

http://doi.org/10.1631/jzus.B0820090


Arylamine N-acetyltransferases: a new inhibitor of apoptosis in HepG2 cells


Author(s):  Yu-bin JI, Shi-yong GAO

Affiliation(s):  Postdoctoral Research Station of the Institute of Materia Medica, Center for Life Sciences and Environmental Sciences, Harbin University of Commerce, Harbin 150076, China; more

Corresponding email(s):   sygao2002@163.com

Key Words:  Arylamine N-acetyltransferases (NATs), Apoptosis, HepG2, Camptothecin (CAM)


Yu-bin JI, Shi-yong GAO. Arylamine N-acetyltransferases: a new inhibitor of apoptosis in HepG2 cells[J]. Journal of Zhejiang University Science B, 2008, 9(9): 701-706.

@article{title="Arylamine N-acetyltransferases: a new inhibitor of apoptosis in HepG2 cells",
author="Yu-bin JI, Shi-yong GAO",
journal="Journal of Zhejiang University Science B",
volume="9",
number="9",
pages="701-706",
year="2008",
publisher="Zhejiang University Press & Springer",
doi="10.1631/jzus.B0820090"
}

%0 Journal Article
%T Arylamine N-acetyltransferases: a new inhibitor of apoptosis in HepG2 cells
%A Yu-bin JI
%A Shi-yong GAO
%J Journal of Zhejiang University SCIENCE B
%V 9
%N 9
%P 701-706
%@ 1673-1581
%D 2008
%I Zhejiang University Press & Springer
%DOI 10.1631/jzus.B0820090

TY - JOUR
T1 - Arylamine N-acetyltransferases: a new inhibitor of apoptosis in HepG2 cells
A1 - Yu-bin JI
A1 - Shi-yong GAO
J0 - Journal of Zhejiang University Science B
VL - 9
IS - 9
SP - 701
EP - 706
%@ 1673-1581
Y1 - 2008
PB - Zhejiang University Press & Springer
ER -
DOI - 10.1631/jzus.B0820090


Abstract: 
Objective: To explore how arylamine N-acetyltransferases (NATs) is related to cell apoptosis. Methods: NAT activity in apoptotic hepG2 cells was measured using high performance liquid chromatography (HPLC); the apoptosis rate of hepG2 cells acted upon by an NAT inhibitor was measured using flow cytometry. Results: NAT activity was lowered in apoptotic hepG2 cells; apoptosis rate induced by camptothecin (CAM) increased after inhibition of NAT activity in hepG2 cells. Conclusion: NAT can inhibit apoptosis in hepG2 cells.

Darkslateblue:Affiliate; Royal Blue:Author; Turquoise:Article

Reference

[1] Bozhkov, P.V., Suarez, M.F., Filonova, L.H., Daniel, G., Zamyatnin, A.A.Jr., Rodriguez-Nieto, S., Zhivotovsky, B., Smertenko, A., 2005. Cysteine protease mcII-Pa executes programmed cell death during plant embryogenesis. Proc. Natl. Acad. Sci. USA, 102(40):14463-14468.

[2] Fan, T.J., Han, L.H., Cong, R.S., Liang, J., 2005. Caspase family proteases and apoptosis. Acta Biochim. Biophys. Sin. (Shanghai), 37(11):719-727.

[3] Gao, J.X., Zhou, Y.Q., Zhang, R.H., Ma, X.L., Liu, K.J., 2005. Caspase-3 plays a required role in PC12 cell apoptotic death induced by roscovitine. Sheng Li Xue Bao, 57(6):755-760 (in Chinese).

[4] Harwood, S.M., Yaqoob, M.M., Allen, D.A., 2005. Caspase and calpain function in cell death: bridging the gap between apoptosis and necrosis. Ann. Clin. Biochem., 42(6):415-431.

[5] Hein, D.W., Rustan, T.D., Doll, M.A., Bucher, K.D., Ferguson, R.J., Feng, Y., Furman, E.J., Gray, K., 1992. Acetyltransferases and susceptibility to chemicals. Toxicol. Lett., 64-65:123-130.

[6] Hein, D.W., Doll, M.A., Rustan, T.D., Gray, K., Feng, Y., Ferguson, R.J., Grant, D.M., 1993. Metabolic activation and deactivation of arylamine carcinogens by recombinant human NAT1 and polymorphic NAT2 acetyltransferases. Carcinogenesis, 14(8):1633-1638.

[7] Hein, D.W., Rustan, T.D., Ferguson, R.J., Doll, M.A., Gray, K., 1994. Metabolic activation of aromatic and heterocyclic N-hydroxyarylamines by wild-type and mutant recombinant human NAT1 and NAT2 acetyltransferases. Arch. Toxicol., 68(2):129-133.

[8] Ho, P.K., Hawkins, C.J., 2005. Mammalian initiator apoptotic caspases. FEBS J., 272(21):5436-5453.

[9] King, C.M., Land, S.J., Jones, R.F., Debiec-Rychter, M., Lee, M.S., Wang, C.Y., 1997. Role of acetyltransferases in the metabolism and carcinogenicity of aromatic amines. Mutat. Res., 376(1-2):123-128.

[10] Rodrigues-Lima, F., Delomenie, C., Goodfellow, G.H., Grant, D.M., Dupret, J.M., 2001. Homology modelling and structural analysis of human arylamine N-acetyltransferase NAT1: evidence for the conservation of a cysteine protease catalytic domain and an active-site loop. Biochem. J., 356(2):327-334.

[11] Sinclair, J.C., Sandy, J., Delgoda, R., Sim, E., Noble, M.E., 2000. Structure of arylamine N-acetyltransferase reveals a catalytic triad. Nat. Struct. Biol., 7(7):560-564.

[12] Turk, D., Guncar, G., Podobnik, M., Turk, B., 1998. Revised definition of substrate binding sites of papain-like cysteine proteases. Biol. Chem., 379(2):137-147.

[13] Wang, G.Y., Zhang, J.W., Lü, Q.H., Xu, R.Z., Dong, Q.H., 2007. Berbamine induces apoptosis in human hepatoma cell line SMMC7721 by loss in mitochondrial transmembrane potential and caspase activation. Journal of Zhejiang University SCIENCE B, 8(4):248-255.

[14] Weber, W.W., Hein, D.W., 1985. N-acetylation pharmacogenetics. Pharmacol. Rev., 37(1):25-79.

[15] Zhang, Y.H., Peng, H.Y., Xia, G.H., Wang, M.Y., Han, Y., 2004. Anticancer effect of two diterpenoid compounds isolated from Annona glabra Linn. Acta Pharmacol. Sin., 25(7):937-942.

Open peer comments: Debate/Discuss/Question/Opinion

<1>

Please provide your name, email address and a comment





Journal of Zhejiang University-SCIENCE, 38 Zheda Road, Hangzhou 310027, China
Tel: +86-571-87952783; E-mail: cjzhang@zju.edu.cn
Copyright © 2000 - 2024 Journal of Zhejiang University-SCIENCE