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2014, Number 4

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Rev Hosp Jua Mex 2014; 81 (4)

Participación de la proteína BIK en los procesos apoptóticos

Gutiérrez-Santana JC, García-Casillas G, Toscano-Garibay JD

Language: Spanish
References: 13
Page: 239-244
PDF size: 249.65 Kb.


ABSTRACT

Cell death (apoptosis) is a process relevant in the development and differentiation of multicellular organism and its alterations raise pathological conditions. Apoptosis is tightly regulated by a family known as BCL-2 proteins conformed by pro- and anti-apoptotic members that share structural domains (BH1-BH4). Some members of this family are exclusively activated in response to death signals with pro-apoptotic function and have homology barely at the BH3 domain (BH3-only proteins). BIK is a BH3-only protein embedded into the membrane of the endoplasmic reticulum inducing changes in Ca+2 levels consequently remodeling mitochondrial cristae and releasing cytochrome C as the initial step of apoptosis. Additionally, BIK cooperates with NOXA to activate BAX through a mitochondrial independent pathway. On the other hand, BIK expression is inducible by anti-estrogenic drugs and it has been related to p53 on MCF7 cells. Also, it has been observed that BIK is actively synthesized in breast cancer cells and is rapidly degraded in a proteasome-dependent manner with its levels being restored when proteasome inhibitors are used. Due to its role as apoptotic regulator BIK has become an important indirect therapeutic target, nonetheless being one of the less studied BH3-only members, its study would generate interesting biotechnological alternatives for a wide number of pathologies.


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