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PKC-θ is a negative regulator of TRAIL-induced and FADD-mediated apoptotic spectrin aggregation
Author(s) -
Izabela Michalczyk,
Monika Toporkiewicz,
Patrycja M. Dubielecka,
Anna Chorzalska,
Aleksander F. Sikorski
Publication year - 2015
Publication title -
folia histochemica et cytobiologica
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.384
H-Index - 40
eISSN - 1897-5631
pISSN - 0239-8508
DOI - 10.5603/fhc.a2016.0006
Subject(s) - fadd , regulator , spectrin , apoptosis , microbiology and biotechnology , chemistry , biophysics , cancer research , biology , biochemistry , cell , caspase , programmed cell death , cytoskeleton , gene
During studies on chemotherapy-induced apoptosis in lymphoid cells, we noted that aggregation of spectrin occurred early in apoptosis, i.e. before activation of initiator caspase(s) and prior to exposure of phosphatidylserine (PS). We also found that protein kinase C theta (PKC-θ) co-localized with spectrin in these aggregates. Our previously published studies indicated that in formation of early apoptotic spectrin aggregates, either PKC-θ or other apoptosis-related proteins are involved. Taking into consideration above data, we decided to test the effect of PKC-θ and Fas-associated death domain protein (FADD) on spectrin aggregation in these cells during tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)-induced apoptosis.

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