Poly(ADP-ribosyl) polymerase in life and death of neural cells

Ahel, Josip (2014) Poly(ADP-ribosyl) polymerase in life and death of neural cells. Bachelor's thesis, Faculty of Science > Department of Biology.

Language: Croatian

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Poly(ADP-ribose) is a post-translational modification of proteins synthesized by the poly(ADP-ribosyl) polimerase family enzymes from NAD+. Poly(ADP-ribosyl)ation is a reversible reaction with specific enzymes catalysing the hydrolysis of poly(ADP-ribose). Poly(ADP-ribosyl)ation systems are found in all six eukaryotic supergroups. In this paper, I offer a review of up-to-date findings about the roles of poly(ADP-ribosyl)ation in DNA repair, chromatin reoragnization, transcription regulation, necrosis and apoptosis, with emphasis on the function of poly(ADP-ribosyl)ation in the nervous system. In these processes, poly(ADP-ribosyl) polimerases play a key role regulating the activity of numerous proteins directly engaged in these processes. This is achieved by forming poly(ADP-ribose) scaffolds or by direct modification of target proteins. Moreover, excessive poly(ADP-ribosyl) polimerase activity may lead to necrotic cell death by energy shock or to parthanatos caused by translocation of mitochondrial death signals. In the nervous system, excessive poly(ADPribosyl) polimerase activity can be caused by the excitotoxic action of glutamate and by acute conditions, such as stroke and traumatic injuries, during which cells experience oxidative stress, significant activation of inflammatory processes and poly(ADP-ribosyl) polimerasemediated neurodegeneration. Poly(ADP-ribosyl) glycohydrolase and terminal (ADP-ribose) glycohydrolase most likely also play significant roles in the aforementioned processes as disfunctionality in these two proteins has severe neurodegenerative effects.

Item Type: Thesis (Bachelor's thesis)
Supervisor: Matulić, Maja
Date: 2014
Number of Pages: 13
Subjects: NATURAL SCIENCES > Biology
Divisions: Faculty of Science > Department of Biology
Depositing User: Silvana Šehić
Date Deposited: 13 Nov 2014 13:30
Last Modified: 13 Nov 2014 13:30
URI: http://digre.pmf.unizg.hr/id/eprint/3272

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