Effect of tamoxifen and retinoic acid on bradykinin induced proliferation in MCF-7 cells

Journal of Cellular Biochemistry
Paola SearovicClaudia G Saez

Abstract

Chemopreventive approaches for the treatment of breast cancer have been validated clinically and with in vitro studies. The combined action of tamoxifen/all-trans retinoic acid was advantageous in MCF-7 cells, reducing cell proliferation, Bcl-2 and c-Myc protein levels and increasing E-Cadherin protein levels and Gap junctional Intercellular Communication. We further investigated their combined effect in the presence of bradykinin, a pro-inflammatory agent, previously reported to contribute to the proliferation of breast cancer cells. Bradykinin increased MCF-7 cell proliferation, c-Myc levels and ERK1/2 activity. The co-incubation of bradykinin-MCF-7 cells with tamoxifen/all-trans retinoic acid reduced cell proliferation, ERK1/2 activity, as well as Bcl-2, c-Myc, and bradykinin receptor-2 levels, without altering the enhanced E-cadherin levels induced by tamoxifen/all-trans retinoic acid. We showed that the anti-tumoral effect of tamoxifen/all-trans retinoic acid is beneficial in MCF-7 breast cancer cells grown in a bradykinin-pro-mitogenic environment, an effect that might be, at least in part, through the MAPK pathway and B2-bradykinin receptor inhibition.

References

Sep 1, 1991·Proceedings of the National Academy of Sciences of the United States of America·A E McEachernK Jarnagin
Mar 1, 1985·Peptides·R J Vavrek, J M Stewart
Jan 1, 1994·The Journal of Cell Biology·J C Reed
Mar 6, 1996·Journal of the National Cancer Institute·Y KangR R Perry
Dec 13, 1996·The Journal of Biological Chemistry·A BlaukatW Müller-Esterl
May 1, 1997·Breast Cancer Research and Treatment·S J Nass, R B Dickson
Jan 7, 1999·Brazilian Journal of Medical and Biological Research = Revista Brasileira De Pesquisas Médicas E Biológicas·J B Pesquero, M Bader
Aug 13, 1999·The American Journal of Physiology·V VelardeA A Jaffa
Dec 22, 1999·Immunopharmacology·H MaedaT Akaike
May 16, 2000·Endocrine-related Cancer·H S Jacobs
Mar 7, 2001·Lancet·F Balkwill, A Mantovani
May 24, 2001·The Journal of Urology·L Barki-Harrington, Y Daaka
Oct 8, 2003·Current Pharmaceutical Design·J M Stewart
Oct 8, 2003·Experimental Biology and Medicine·Rebecca SimsteinBarbara Beckman
Dec 11, 2003·The Journal of Veterinary Medical Science·Sohyun ParkSungIl Cho
Jul 29, 2004·Journal of Cellular Physiology·S GrecoSanto Marsigliante
May 16, 2007·Progress in Histochemistry and Cytochemistry·Lorenza González-MariscalErika Garay
Jan 10, 2008·International Immunopharmacology·Claudio M Costa-NetoPedro P C Souza

❮ Previous
Next ❯

Citations

Feb 22, 2012·Expert Opinion on Therapeutic Targets·Carlos D FigueroaKanti D Bhoola
Jun 3, 2014·Toxicology·Mariana P C RibeiroJosé B A Custódio
Mar 7, 2015·Journal of Nuclear Medicine : Official Publication, Society of Nuclear Medicine·Kuo-Shyan LinFrançois Bénard

❮ Previous
Next ❯

Related Concepts

Related Feeds

Cadherins and Catenins

Cadherins (named for "calcium-dependent adhesion") are a type of cell adhesion molecule (CAM) that is important in the formation of adherens junctions to bind cells with each other. Catenins are a family of proteins found in complexes with cadherin cell adhesion molecules of animal cells: alpha-catenin can bind to β-catenin and can also bind actin. β-catenin binds the cytoplasmic domain of some cadherins. Discover the latest research on cadherins and catenins here.

BCL-2 Family Proteins

BLC-2 family proteins are a group that share the same homologous BH domain. They play many different roles including pro-survival signals, mitochondria-mediated apoptosis and removal or damaged cells. They are often regulated by phosphorylation, affecting their catalytic activity. Here is the latest research on BCL-2 family proteins.