A growing number of studies are looking at causes of cancer at a molecular level – and discovering that hypoxia pathways play a major role. This is because HIF (Hypoxia Inducible Factor) proteins work to prevent cell death. Combined with DNA-repair pathways and the apoptosis mechanism, it’s obvious what disruption of these pathways could lead to.
Antibody studies have focussed on hypoxia-induced autophagy. The HIF-1 pathway is linked to BNIP3 and BNIP3L release, pro-apoptotic genes expressed in certain tumours. It has been shown that BNIP3 expression during hypoxia may result in mitochondrial autophagy, rather than whole-cell death. Thus BNIP3 may play a cell-survival role, decreasing dependency for oxygen. If DNA-repair is compromised, this may lead to cancer development.
Studies into the pRB/E2F protein complex have shown high levels of activity in hypoxia-induced autophagy (HIA) when activated in cancer cells. pRB/E2F has also been shown to inhibit BNIP3 activity.
Immunocytochemistry/Immunofluorescence: BNIP3 Antibody
In February 2009, studies by Bellot et al threw new light on the role of BNIP3 and BNIP3L in cancer development. We at Novus Biologicals supplied Beclin-1 antibodies which were used with BNIP3 and anti-LC3 Igs from other sources. The disruption of the Bcl-2/Beclin-1 complex by BH3 peptides isolated from hypoxia-induced BNIP3 and BNIP3L was also measured.
The Bcl-2/Beclin-1 complex operates a pro-autophagic pathway. The Bellot study showed that atypical BH-3 domains of hypoxia-induced BNIP3 and BNIP3L disrupted this complex, leading to a pro-survival, rather than pro-death response. Replication of mutated DNA could lead to tumour development.
We at Novus Biologicals are continuously expanding our antibody database to aid further innovative studies in this area.
Novus Biologicals offers many BNIP3 reagents for your research needs including:
