Hypoxia Inducible Factor 3, alpha Subunit (HIF3A) ELISA Kits

Human Hypoxia Inducible Factor 3, alpha Subunit (HIF3A) interaction partners

1. Study mapped the functional nuclear localization signal (NLS) to the unique C-terminal region of Hif-3alpha and identified two clusters of basic residues critical for its nuclear localization. The two NLS motifs are functionally redundant. These results suggest that Hif-3alpha nuclear localization is mediated through two redundant NLS motifs located in its unique C-terminal region.

2. Expression level of HIF3A is downregulated in gestational diabetes patients. The methylation status of HIF3A promoter region is highly correlated with gestational diabetes.

3. MicroRNA-300 is a tumor suppressor microRNA in non-small cell lung cancer by downregulating HIF3alpha expression.

4. Under normoxia, HIF-3alpha overexpression promoted pancreatic cancer cell invasion and migration and stimulated F-actin polymerization. In summary, HIF-3alpha promotes pancreatic cancer cell invasion and metastasis in vivo and promotes pancreatic cancer cell invasion and metastasis by transcriptionally activating the RhoC-ROCK1 signaling pathway.

5. data suggest an important role of miR-210 in sustaining HIF-1alpha activity via the suppression of HIF-3alpha, regulating cell growth and chemotherapeutic drug resistance in cholangiocarcinoma.

6. AA can protect cardiomyocytes against hypoxia-induced apoptosis through regulating the miR-1290/HIF3A/HIF-1alpha axis, and miR-1290 may be a potential target in the prevention of myocardial ischemia-reperfusion injury

7. NAP peptide prevents outer blood retinal barrier breakdown by reducing HIF1alpha/HIF2alpha, VEGF/VEGFRs, and increasing HIF3alpha expression Moreover it is able to reduce the percentage of apoptotic cells by modulating the expression of two death related genes, BAX and Bcl2.

8. HIF3A methylation was found in the association between the HIF3A rs3826795 polymorphism and alanine aminotransferase among obese children.

9. TIMP2 suppression, in a hypoxic environment, was induced through a regulatory feedback circuit consisting of hypoxia-inducible factor (HIF) 1 alpha, microRNA-210 (miR-210), and HIF-3alpha.

10. Results were discordant with those expected if HIF3A methylation has a causal effect on body mass index (BMI) & provided more evidence for causality in the reverse direction (i.e., an effect of BMI on HIF3A methylation); results also show a long-lasting intergenerational influence of maternal BMI on offspring methylation at this locus, which may confound associations between own adiposity & HIF3A methylation.

11. DNA methylation in HIF3A shares moderate correlation between adipose tissue and blood, and both are associated with BMI. In contrast, methylation in FASN is poorly correlated across tissues, but the DNA methylation in adipose tissue but not blood is highly associated with BMI

12. Reduced lifetimes of the donor were partially restored by coexpression of HIF-1alpha or Bcl-xL, binding proteins of IPAS in the nucleus and mitochondria, respectively.

13. Results confirmed a positive association between BMI and HIF3A DNA promoter methylation in the blood. The tissue-specific results of HIF3A gene expression indicate that subcutaneous adipose tissue is the more functional tissue in which a low expression may adversely affect whole-body insulin sensitivity.

14. Parkin is downregulated under hypoxia and that it interferes with HIF expression based on cellular oxygen tension.

15. miR210 may be a negative regulator of the progression of osteoarthritis, which increases chondrocyte proliferation and prompts extracellular matrix deposition by directly targeting HIF3alpha.

16. This provides a compelling model for how hypoxia-induced miR-429 regulates the switch between HIF-1 adaptive responses to HIF-3 survival responses by rapidly decreasing HIF1A levels while simultaneously slowing the progression of HIF3A expression until the miR-429 levels drop below normoxic levels.

17. The association between increased DNA methylation at HIF3A and increased adiposity is present in neonates.

18. Unsaturated fatty acids are high-affinity ligands of the C-terminal domain from the HIF-3alpha.

19. HIF3A DNA Methylation Is Associated with Childhood Obesity and ALT

20. HIF3alpha has a transcriptional regulatory function, which negatively affects gene expression by competing with HIF1alpha and HIF2alpha in binding to transcriptional elements in target genes during hypoxia. (Review)

Mouse (Murine) Hypoxia Inducible Factor 3, alpha Subunit (HIF3A) interaction partners

1. Phosphorylation of inhibitory PAS domain protein (IPAS) at Ser184 by MAPK-activated protein kinase 2 (MK2 or MAPKAPK2) enhances the proapoptotic function of IPAS.

2. Report suggests that BV-2 microglial cells express HIF-3a under inflammatory conditions and that its activation differed from that of HIF-1a

3. mRNA of HIF-2alpha and Ets-1 were significantly increased by HIF-3alpha ablation. Both factors activate the VE-cadherin gene, the transcriptional repression of these factors by HIF-3alpha is important for silencing the irrelevant expression of the VE-cadherin gene.

4. our data indicated that Tnni2K175del mutation led to abnormally increased hif3a and decreased vegf in bone, which explain, at least in part, the small body size of Tnni2K175del mice

5. Anoxia preconditioning increases anti-ischemic neuronal resistance which to a certain extent correlates with the changes of HIF-1alpha and HIF-3alpha expression.

6. It is a negative regulator of tumorigenesis.(review)

7. alternative splicing and expression of IPAS is induced by hypoxia.

8. These data suggest an involvement of the HIF system in metabolic derangements as for instance caused by diabetes.

9. By generating mice with a targeted disruption of the NEPAS/HIF-3alpha locus, it was found that homozygous mutant mice, NEPAS/HIF-3alpha(-/-), were viable but displayed enlargement of the right ventricle and impaired lung remodeling.

10. Identity of third HIF alpha class member, HIF-3alpha. mRNA expression information by mouse MTN. Experimental proof of dimerization with ARNT/HIF-1beta.

Cow (Bovine) Hypoxia Inducible Factor 3, alpha Subunit (HIF3A) interaction partners

1. No significant conclusions could be drawn with respect to susceptibility to other traits. HIF-3alpha could serve as a useful biomarker for donor selection, superovulation improvement, and assisted fertility.