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Bcl‐xL‐c‐FLIP L Anti‐apoptotic Interaction in Microvascular Endothelial Cells
Author(s) -
Sawant Devendra A
Publication year - 2016
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.30.1_supplement.1034.15
Subject(s) - flip , apoptosis , bcl xl , microbiology and biotechnology , cytoplasm , cytochrome c , transfection , flow cytometry , programmed cell death , mitochondrion , biology , caspase 8 , caspase 3 , cell culture , biochemistry , genetics
Apoptosis or cell death is carried out by a series of caspase activity which can be activated either by intrinsic / mitochondrial or by extrinsic / receptor mediated pathways. The apoptotic pathway is negatively regulated at the receptor level by c‐FLIP, which blocks caspase‐8 activation, and at the mitochondrial level by anti‐apoptotic Bcl‐xL. Researchers have shown earlier that c‐FLIP L protein overexpression upregulates Bcl‐xL protein expression in the endothelial cells undergoing apoptosis during ischemia‐reperfusion injury. However, no study has shown that Bcl‐xL overexpression can regulate c‐FLIP L activity in endothelial cells. Hence, the current research study tries to elucidate a possible novel interaction between Bcl‐xL and c‐FLIP L . The objective of this study is twofold; first, to demonstrate that Bcl‐xL overexpression causes translocation of c‐FLIP L from the nucleus into the cytoplasm and second, to determine whether this translocation actually helps c‐FLIP L to demonstrate its anti‐apoptotic activity. The results from immunofluorescence study and immunoblot analysis of sub‐cellular fractionation have demonstrated that c‐FLIP L translocate in cytoplasm from nucleus in microvascular endothelial cells transfected with recombinant Bcl‐xL protein. Caspase‐8 assay and apoptotic /cell death assay using flow cytometry will further demonstrate that Bcl‐xL can regulate c‐FLIP L anti‐apoptotic activity in microvascular endothelial cells. Thus, illustrating Bcl‐xL‐c‐FLIP L anti‐apoptotic interaction could explain key pathophysiological mechanisms involved in various disease processes. Support or Funding Information Alderson Broaddus University College of Medical Science, Philippi, WV.