High Level of Esterification of Steroids to Long-Chain Fatty Acids in ZR-75-1 Human Breast Cancer Cells

1990 ◽  
Vol 595 (1 Steroid Forma) ◽  
pp. 422-424
Author(s):  
Donald Poirier ◽  
Richard Poulin ◽  
Yves Mérand ◽  
Catherine Thériault ◽  
Fernand Labrie
1994 ◽  
Vol 22 (2) ◽  
pp. 131-141 ◽  
Author(s):  
David P. Rose ◽  
Jodie Rayburn ◽  
Mary Ann Hatala ◽  
Jeanne M. Connolly

2004 ◽  
Vol 381 (2) ◽  
pp. 463-469 ◽  
Author(s):  
Hong ZHAO ◽  
Robert W. HARDY

DRM (detergent-resistant membranes), which are resistant to solublization by non-ionic detergents, have been demonstrated to be involved in many key cell functions such as signal transduction, endocytosis and cholesterol trafficking. Covalent modification of proteins by fatty acylation has been proposed to be an important protein-targeting mechanism for DRM association. However, little is known concerning the effects of LCSFA (long-chain saturated fatty acids) on protein composition of DRM in human cancer cells. In the present study, we found that, in Hs578T human breast cancer cells, the major protein increased in DRM in response to the LCSFA stearate (C18:0) was annexin II. Our results demonstrated that annexin II accumulated in DRM specifically in response to physiological concentrations of stearate and palmitate (C16:0), but not long-chain unsaturated fatty acids, in a time- and concentration-dependent manner. This process was reversible and dependent on cholesterol and intracellular calcium. Although calcium was necessary for this translocation, it was not sufficient to induce the annexin II translocation to DRM. We also demonstrate that stearate induced the acylation of caveolin but not that of annexin II. Association of annexin II with caveolin, although not necessarily direct, specifically occurs in DRM in response to stearate. Finally, bromostearate, a stearate analogue that effectively blocks protein acylation, does not induce annexin II translocation to DRM. We conclude that exogenously added LCSFA strongly induces the translocation of annexin II to DRM in Hs578T human breast cancer cells at least partially by association with acylated caveolin.


Author(s):  
Bruna Silveira Pacheco ◽  
Marco Aurélio Ziemann dos Santos ◽  
Eduarda Schultze ◽  
Rosiane Mastelari Martins ◽  
Rafael Guerra Lund ◽  
...  

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Luciana Gomes ◽  
Marcos Sorgine ◽  
Carlos Luan Alves Passos ◽  
Christian Ferreira ◽  
Ivone Rosa de Andrade ◽  
...  

Abstract Flotillin-1 and flotillin-2 are highly conserved proteins that localize into cholesterol-rich microdomains in cellular membranes. Flotillins are closely related to the occurrence and development of various types of human cancers. Flotillin-1 is highly expressed in breast cancer, and the high expression level of flotillin-1 is significantly correlated with poorer patient survival. Here we studied the relationship between the formation of lipid rafts and the expression of flotillins and lipids in human breast cancer cells. We used the polyphenol compound resveratrol to alter the structure and function of the plasma membrane. Our data revealed an increase in fatty acids in MCF-7 and MDA-MB-231 cells upon resveratrol treatment. Interestingly, we also found an increase in the expression of both flotillin-1 and flotillin-2 in breast tumor cells after treatment. Resveratrol also induced changes in the pattern of flotillin distribution among detergent-resistant lipid rafts fractions in both cell lines and induced the nuclear translocation of flotillin-2. Since resveratrol has been pointed out as a putative cancer therapy agent, our results could have an impact on the understanding of the effects of resveratrol in tumor cells.


Sign in / Sign up

Export Citation Format

Share Document