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Brain Res Mol Brain Res. 1999 Apr 20;67(2):303-15.

Characterization of a neuronal kappaB-binding factor distinct from NF-kappaB.

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Department of Geriatrics, University of Arkansas for Medical Sciences, J.L. McClellan Memorial Veterans Affairs Medical Center, 4300 W. Seventh St., Little Rock, AR 72205, USA.


Transcription factors that bind kappaB enhancer elements have begun to garner wide attention in neurobiology. Data suggest that activation of kappaB-binding factors in neurons can be protective against various neurotoxins, but other data have connected NF-kappaB to cell death. In electrophoretic mobility shift assays of kappaB-binding activity, we have found that the predominant activity in rat brain tissue, in primary neurons, and in neuronal cell lines has a mobility inconsistent with that of bona fide NF-kappaB (RelA-p50 heterodimer). We have tentatively termed this activity neuronal kappaB-binding factor (NKBF). Competition assays with various DNA probes distinguished NKBF from NF-kappaB. Probes that efficiently bind the p50 homodimer were able to compete with a conventional NF-kappaB probe for NKBF binding, but NKBF did not react with antibodies to p50 (or any other known Rel family members). Furthermore, UV-crosslinking indicated that NKBF is composed of two polypeptides of 82 kDa and 27 kDa. Although NKBF activity can be elevated in a manner independent of new macromolecular synthesis, it does not appear to be modulated by IkappaB. Finally, no NF-kappaB was induced by glutamate in highly enriched neuronal cultures, although it was induced in neuron-glia cocultures. These data suggest that the primary kappaB-binding transcription factor in neurons is a novel protein complex distinct from NF-kappaB.

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