PARP-1 cleavage fragments: signatures of cell-death proteases in neurodegenerationReport as inadecuate




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Cell Communication and Signaling

, 8:31

First Online: 22 December 2010Received: 16 July 2010Accepted: 22 December 2010

Abstract

The normal function of poly ADP-ribose polymerase-1 PARP-1 is the routine repair of DNA damage by adding poly ADP ribose polymers in response to a variety of cellular stresses. Recently, it has become widely appreciated that PARP-1 also participates in diverse physiological and pathological functions from cell survival to several forms of cell death and has been implicated in gene transcription, immune responses, inflammation, learning, memory, synaptic functions, angiogenesis and aging. In the CNS, PARP inhibition attenuates injury in pathologies like cerebral ischemia, trauma and excitotoxicity demonstrating a central role of PARP-1 in these pathologies. PARP-1 is also a preferred substrate for several -suicidal- proteases and the proteolytic action of suicidal proteases caspases, calpains, cathepsins, granzymes and matrix metalloproteinases MMPs on PARP-1 produces several specific proteolytic cleavage fragments with different molecular weights. These PARP-1 signature fragments are recognized biomarkers for specific patterns of protease activity in unique cell death programs. This review focuses on specific suicidal proteases active towards PARP-1 to generate signature PARP-1 fragments that can identify key proteases and particular forms of cell death involved in pathophysiology. The roles played by some of the PARP-1 fragments and their associated binding partners in the control of different forms of cell death are also discussed.

Electronic supplementary materialThe online version of this article doi:10.1186-1478-811X-8-31 contains supplementary material, which is available to authorized users.

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Author: Ganta Vijay Chaitanya - Jonathan S Alexander - Phanithi Prakash Babu

Source: https://link.springer.com/







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