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[Cancer Research 64, 456-462, January 15, 2004]
© 2004 American Association for Cancer Research

Advances in Brief

Protein Kinase C {zeta} Transactivates Hypoxia-Inducible Factor {alpha} by Promoting Its Association with p300 in Renal Cancer

Kaustubh Datta1, Jinping Li1, Resham Bhattacharya1, Levon Gasparian1, Enfeng Wang1 and Debabrata Mukhopadhyay2

1 Departments of Pathology, Beth Israel Deaconess Medical Center and Harvard Medical School, Boston, Massachusetts, and
2 Department of Biochemistry and Molecular Biology and Cancer Center, Rochester, Minnesota

Hydroxylation at an asparagine residue at the COOH-terminal activation domain of hypoxia-inducible factor (HIF)-1/2 {alpha}s is essential for its inactivation under normoxic condition. To date, the mechanism by which HIF-{alpha} avoids the inhibitory effect of asparagine hydroxylase in renal cell carcinoma (RCC) in normoxia is undefined. We have shown herein that protein kinase C (PKC) {zeta} has an important role in HIF-{alpha} activation in RCC. By using dominant negative mutant and small interference RNA approaches, we have demonstrated that the association between HIF-{alpha} and p300 is modulated by PKC{zeta}. Moreover, a novel signaling pathway involving phosphatidylinositol 3'-kinase and PKC{zeta} has been shown to be responsible for the activation of HIF-{alpha} by inhibiting the mRNA expression of FIH-1 (factor inhibiting HIF-1) in RCC and thereby promoting the transcription of hypoxia-inducible genes such as vascular permeability factor/vascular endothelial growth factor.




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