The anti-apoptotic factor Bcl-2 is over-expressed in B-cell lymphoma cells as their main survival mechanism by binding to IP3R2 on the endoplasmic reticulum (ER). In this study, a cell-penetrating version of the BIRD-2 peptide (Bcl-2/IP3R Disrupter-2 peptide with a TAT sequence) made by LifeTein was used to break up the complex formed by Bcl-2 and IP3R2 in human diffuse large B-cell lymphoma (DLBCL) cells. Ca2+ signaling-related events are suggested to be the killing mechanism of BIRD-2 peptide on DLBCL cells.
BIRD-2, a peptide that specifically disrupts the Bcl2/IP3R complex, was utilized to further verify the mitochondrial Ca2+ regulatory mechanism via the Bmal1-Bcl2/IP3R signaling pathway. It was found that BIRD-2 aggravated mitochondrial Ca2+ overload and apoptosis in vitro.
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Bird-2 Peptides & B-Cell Lymphoma
Reference:
Inhibiting Bcl-2 via its BH4 domain in DLBCL cancers to provoke pro-apoptotic Ca2+ signaling
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