PARP-1 cleavage fragments: signatures of cell-death proteases in neurodegeneration
By G. V. Chaitanya, J. Alexander, P. Babu. Cell Communication and Signaling, 2010
840 citations recorded by the source corpus.
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.
Subfields: Electrical and Electronic Engineering, Molecular Biology, Oncology
View Paper: https://www.semanticscholar.org/paper/67d43dcf44cc02b516ab1f3139ce71ea40265d58
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Citations in the corpus
- Ischemia/Reperfusion (2016, neutral): “strate of several so-called “suicide” proteases, which include the calpains and MMPs (124).”
- On PAR with PARP: cellular stress signaling through poly(ADP-ribose) and PARP-1. (2012, background): “Although PARP1 activation is required for the initiation of the above cell death programs, PARP-1 may be cleaved and inactivated by various proteases, including caspases, calpain, cathepsins, and granzymes (Chaitanya et al. 2010).”