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Inactivation of bad by site‐specific phosphorylation: The checkpoint for ischemic astrocytes to initiate or resist apoptosis
Author(s) -
Chen Xiao Qian,
Lau Lok Ting,
Fung YinWan Wendy,
Yu Albert Cheung Hoi
Publication year - 2005
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/jnr.20396
Subject(s) - apoptosis , phosphorylation , microbiology and biotechnology , chemistry , neuroscience , biology , biochemistry
Bcl‐2‐associated death protein (Bad), a member of the Bcl family, directs astrocytes in primary cultures to enter or resist apoptosis during ischemia in vitro. Under ischemia, Bad was the only Bcl family member whose expression was upregulated significantly during the early stages of an ischemic insult. Increased endogenous Bad was translocated from the cytoplasm to mitochondria to induce apoptosis in astrocytes. Concurrently, ischemia also induced Bad phosphorylation specifically on Ser112 to promote survival. This site‐specific phosphorylation of Bad was mediated by an early activation of the mitogen‐activated protein kinase/extracellular signal‐regulated protein kinase (MAPK/ERK) intracellular signaling pathway. This study demonstrates that ischemia‐induced Bad plays a dual role in determining whether astrocytes enter or resist apoptosis after an ischemic insult. © 2005 Wiley‐Liss, Inc.