Family of proteins BCL-2

Skenderović, Anamarija (2010) Family of proteins BCL-2. Bachelor's thesis, Faculty of Science > Department of Biology.

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Abstract

To maintain homeostasis in a number of cells in the body of vertebrates, billions of cells die every day in the process called apoptosis. Apoptosis is executed through the action of cystein proteases caspases induced by different stress signals. However, in the process of apoptosis an important role has a family of proteins called BCL-2. These proteins were initially declared only as antiapoptotic proteins that greatly contribute to the tumorogenesis. In the last fifteen years, on the other side, structurally were isolated very similar proteins whose activation led to apoptosis. Similarities between antiapoptotic and proapoptotic BCL-2 proteins are reflected in the highly conserved BH domains, in the shape of the enzyme active site - a deep hydrophobic BC groove closed with several amphipathic helixes, and in the way of activation / inhibition. In addition, active site geometrically and thermodynamically matches a BH3 region of this group of proteins. In order to induce apoptosis, proapoptotic proteins bind to the outer mitochondrial membrane and oligomerize to form protein channels for cytochrome c release from the mitochondrial matrix – the signal for caspase activation. Antiapoptotic BCL-2 proteins interact with proapoptotic members and directly inactivate them in order to protect membrane integrity. The mitochondrial membrane is not the only place of their action. There were done many experiments suggesting the role of these proteins in the maintenance Ca2+ concentration in the ER and cytosol and in the process called autophagy – evolutionary alternative for the apoptosis process. BCL-2 proteins are regulated at transcriptional, posttranscriptional and posttranslational level. Interactions with other members of the BCL-2 family are also important for regulation: antiapoptotic and effector proteins inhibit each other, and proteins containing only BH3 domain act as activators of effector proteins and / or inhibitors of proapoptotic proteins.

Item Type: Thesis (Bachelor's thesis)
Supervisor: Matulić, Maja
Date: 2010
Number of Pages: 16
Subjects: NATURAL SCIENCES > Biology
Divisions: Faculty of Science > Department of Biology
Depositing User: Silvana Šehić
Date Deposited: 02 Dec 2014 13:53
Last Modified: 02 Dec 2014 13:53
URI: http://digre.pmf.unizg.hr/id/eprint/3421

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