NDLI: Assessment of HDACi-Induced Protein Cleavage by Caspases.

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Assessment of HDACi-Induced Protein Cleavage by Caspases.

Content Provider	Semantic Scholar
Author	Treude, Fabian Gladbach, Tobias Plaster, Jacqueline Hartkamp, J. L. L. F.
Copyright Year	2017
Abstract	Aberrant histone deacetylase (HDAC) activity often correlates with neoplastic transformation and inhibition of HDACs by small molecules has emerged as a promising strategy to treat hematological malignancies in particular. Treatment with HDAC inhibitors (HDACis) often prompts tumor cells to undergo apoptosis, thereby causing a caspase-dependent cleavage of target proteins. An unexpectedly large number of proteins are in vivo caspase substrates and defining caspase-mediated substrate specificity is a major challenge. In this chapter we demonstrate that the hematopoietic transcription factor PU.1 becomes cleaved after treatment of acute myeloid leukemia (AML) cells with the HDACis LBH589 (panobinostat) or MS-275 (entinostat). To define caspase specificity for PU.1, an in vitro caspase assay including caspases 1-10 with in vitro-translated PU.1 is described in detail.
Starting Page	11
Ending Page	22
Page Count	12
File Format	PDF HTM / HTML
Alternate Webpage(s)	http://www.springer.com/cda/content/document/cda_downloaddocument/9781493965250-c1.pdf?SGWID=0-0-45-1592971-p180162867
PubMed reference number	27761810v1
Volume Number	1510
Journal	Methods in molecular biology
Language	English
Access Restriction	Open
Subject Keyword	Angiotensin-Converting Enzyme Inhibitors Apoptosis Cleaved cell Hematologic Neoplasms Histone deacetylase inhibitor Histones LBH589 Leukemia, Myelocytic, Acute MS 27-275 Myeloid Leukemia Neoplastic Cell Transformation SPI1 gene Small Molecule TRANSCRIPTION FACTOR caspase entinostat panobinostat
Content Type	Text
Resource Type	Article

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