Novel HIF2A mutations disrupt oxygen sensing, leading to polycythemia, paragangliomas, and somatostatinomas Blood, Mar 2013; 121: 2563 - 2566.
[anti-HA]
Regulation of the PI3-K/Akt Survival Pathway in the Rat Endometrium Biol Reprod, Mar 2013; 88: 79.
[Akt3]
RNA elements directing in vivo assembly of the 7SK/MePCE/Larp7 transcriptional regulatory snRNP Nucleic Acids Res., Mar 2013; 10.1093/nar/gkt159.
[LA]
Ruxolitinib as potential targeted therapy for patients with JAK2 rearrangements Haematologica, Mar 2013; 98: 404 - 408.
[JAK2]
Hypoxia contributes significantly to the pathophysiology of major categories of human disease, including myocardial and cerebral ischemia, cancer, pulmonary hypertension, congenital heart disease and chronic obstructive pulmonary disease. HIF-1 is a nuclear protein involved in mammalian oxygen homeostasis. This occurs as a posttranslational modification by prolyl hydroxylation. HIF-1 is a heterodimer composed of HIF-1 alpha and HIF-1 beta subunits. Both subunits are constantly translated. However, under normoxic conditions, human HIF-1 alpha is hydroxylated at Pro402 or Pro564 by a set of HIF prolyl hydroxylases, is polyubiquinated, and eventually degraded in proteosomes. Under hypoxic conditions, the lack of hydroxylation prevents HIF degradation and increases transcriptional activity. Therefore, the concentration of HIF-1 alpha increases in the cell. In contrast, HIF-1 beta remains stable under either condition. HIF-1 beta is a series of aryl hydrocarbon receptor nuclear translocator (ARNT) gene products. (1,5,6)
Related Pathway
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HEK293T cells were transfected with the pCMV6-ENTRY control or pCMV6-ENTRY ARNT (RC216724) cDNA for 48 hrs and lysed. Equivalent amounts of cell lysates (5 ug per lane) were separated by SDS-PAGE and immunoblotted with anti-ARNT.
