Pathobiology of Renal Carcinogenesis

1992 ◽  
pp. 9-26 ◽  
Author(s):  
P. Bannasch ◽  
H. Zerban
Keyword(s):  
Renal Carcinogenesis

Aberrant regulation of carbohydrate metabolism and metamorphosis during renal carcinogenesis

1986 ◽  
Vol 25 ◽  
pp. 279-284 ◽  
Author(s):  
Peter Bannasch ◽  
Hans Jörg Hacker ◽  
Hiroyuki Tsuda ◽  
Heide Zerban
Keyword(s):  
Carbohydrate Metabolism ◽  
Renal Carcinogenesis ◽  
Regulation Of Carbohydrate Metabolism

scholarly journals Cell Proliferation and Renal Carcinogenesis

1993 ◽  
Vol 101 ◽  
pp. 115 ◽  
Author(s):  
Brian G. Short
Keyword(s):  
Cell Proliferation ◽  
Renal Carcinogenesis

scholarly journals Transgenic rescue from embryonic lethality and renal carcinogenesis in the Nihon rat model by introduction of a wild-type Bhd gene

Oncogene ◽  
2005 ◽  
Vol 25 (20) ◽  
pp. 2885-2889 ◽  
Author(s):  
Y Togashi ◽  
T Kobayashi ◽  
S Momose ◽  
M Ueda ◽  
K Okimoto ◽  
...  
Keyword(s):  
Rat Model ◽  
Embryonic Lethality ◽  
Wild Type ◽  
Renal Carcinogenesis ◽  
Nihon Rat

Renal Carcinogenesis

1976 ◽  
pp. 1-56 ◽  
Author(s):  
J.M. Hamilton
Keyword(s):  
Renal Carcinogenesis

Influence of Vitamin C on Estrogen-Induced Renal Carcinogenesis in Syrian Hamster

2015 ◽  
pp. 132-139
Author(s):  
Joachim G. Liehr ◽  
William J. Wheeler ◽  
Annie M. Ballatore
Keyword(s):  
Vitamin C ◽  
Syrian Hamster ◽  
Renal Carcinogenesis

scholarly journals The Hypoxia-Inducible Factor 2α N-Terminal and C-Terminal Transactivation Domains Cooperate To Promote Renal Tumorigenesis In Vivo

2007 ◽  
Vol 27 (6) ◽  
pp. 2092-2102 ◽  
Author(s):  
Qin Yan ◽  
Steven Bartz ◽  
Mao Mao ◽  
Lianjie Li ◽  
William G. Kaelin
Keyword(s):  
Transcriptional Activation ◽  
Hypoxia Inducible Factor ◽  
Gene Activation ◽  
Tumor Formation ◽  
Transactivation Domain ◽  
Renal Carcinogenesis ◽  
Von Hippel Lindau ◽  
Transactivation Domains ◽  
Relative Contribution

ABSTRACT Hypoxia-inducible factor (HIF) is a heterodimeric transcription factor, consisting of an alpha subunit and a beta subunit, that controls cellular responses to hypoxia. HIFα contains two transcriptional activation domains called the N-terminal transactivation domain (NTAD) and the C-terminal transactivation domain (CTAD). HIFα is destabilized by prolyl hydroxylation catalyzed by EglN family members. In addition, CTAD function is inhibited by asparagine hydroxylation catalyzed by FIH1. Both hydroxylation reactions are linked to oxygen availability. The von Hippel-Lindau tumor suppressor protein (pVHL) is frequently mutated in kidney cancer and is part of the ubiquitin ligase complex that targets prolyl hydroxylated HIFα for destruction. Recent studies suggest that HIF2α plays an especially important role in promoting tumor formation by pVHL-defective renal carcinoma cells among the three HIFα paralogs. Here we dissected the relative contribution of the two HIF2α transactivation domains to hypoxic gene activation and renal carcinogenesis and investigated the regulation of the HIF2α CTAD by FIH1. We found that the HIF2α NTAD is capable of activating both artificial and naturally occurring HIF-responsive promoters in the absence of the CTAD. Moreover, we found that the HIF2α CTAD, in contrast to the HIF1α CTAD, is relatively resistant to the inhibitory effects of FIH1 under normoxic conditions and that, perhaps as a result, both the NTAD and CTAD cooperate to promote renal carcinogenesis in vivo.

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