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Hypoxia inducible factor 3, alpha subunit

HIF-3alpha, IPAS, HIF3A
The protein encoded by this gene is the alpha-3 subunit of one of several alpha/beta-subunit heterodimeric transcription factors that regulate many adaptive responses to low oxygen tension (hypoxia). The alpha-3 subunit lacks the transactivation domain found in factors containing either the alpha-1 or alpha-2 subunits. It is thought that factors containing the alpha-3 subunit are negative regulators of hypoxia-inducible gene expression. Multiple alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Mar 2011] (from NCBI)
Top mentioned proteins: HIF-1alpha, HIF-2alpha, CAN, vascular endothelial growth factor, HAD
Papers on HIF-3alpha
Epigenomic profiling of DNA methylation in paired prostate cancer versus adjacent benign tissue.
Stanford et al., Maastricht, Netherlands. In Prostate, Dec 2015
The top-ranked differentially methylated genes included three genes that were associated with both promoter hypermethylation and reduced gene expression: SCGB3A1, HIF3A, and AOX1.
Hypoxia-inducible factor 3-alpha expression is associated with the stable chondrocyte phenotype.
Johnstone et al., Saint Louis, United States. In J Orthop Res, Nov 2015
The objective of this study was to characterize HIF-3α (HIF3A) expression during chondrocyte differentiation in vitro and in native cartilage tissues.
HIF3A association with adiposity: the story begins before birth.
GUSTO Study Group et al., Singapore, Singapore. In Epigenomics, Sep 2015
AIM: Determine if the association of HIF3A DNA methylation with weight and adiposity is detectable early in life.
DNA Methylation Variants at HIF3A Locus, B-Vitamin Intake, and Long-term Weight Change: Gene-Diet Interactions in Two U.S. Cohorts.
Qi et al., Shanghai, China. In Diabetes, Sep 2015
The first epigenome-wide association study of BMI identified DNA methylation at an HIF3A locus associated with BMI.
Epigenome-wide association study (EWAS) of BMI, BMI change and waist circumference in African American adults identifies multiple replicated loci.
Boerwinkle et al., Minneapolis, United States. In Hum Mol Genet, Sep 2015
Seventy-six BMI-related probes, 164 WC-related probes and 8 BMI change-related probes passed the threshold for significance in ARIC (P < 1 × 10(-7); Bonferroni), including probes in the recently reported HIF3A, CPT1A and ABCG1 regions.
Increased Serine-Arginine (SR) Protein Phosphorylation Changes Pre-mRNA Splicing in Hypoxia.
Kanopka et al., Vilnius, Lithuania. In J Biol Chem, Aug 2015
Inhibitory PAS domain protein (IPAS), a dominant negative regulator of hypoxia-inducible gene expression, is generated from hypoxia inducible transcription factor-3α (HIF-3α) pre-mRNA by an alternative splicing mechanism.
Impact of age, BMI and HbA1c levels on the genome-wide DNA methylation and mRNA expression patterns in human adipose tissue and identification of epigenetic biomarkers in blood.
Ling et al., Copenhagen, Denmark. In Hum Mol Genet, Aug 2015
Methylation at previously reported HIF3A sites correlated significantly with BMI in females only.
HIF3A DNA Methylation Is Associated with Childhood Obesity and ALT.
Ma et al., Beijing, China. In Plos One, 2014
Recent studies suggest that epigenetic modifications, especially DNA methylation, could contribute to explain part of the missing heritability, and two epigenetic genome-wide analysis studies (EWAS) have reported that Hypoxia Inducible Factor 3 Alpha Subunit (HIF3A) methylation was associated with BMI or BMI change.
DNA methylation and body-mass index: a genome-wide analysis.
Samani et al., Leicester, United Kingdom. In Lancet, 2014
The associations with three of these probes--cg22891070, cg27146050, and cg16672562, all of which are in intron 1 of HIF3A--were confirmed in both the primary and second replication cohorts.
Roles of the human hypoxia-inducible factor (HIF)-3α variants in the hypoxia response.
Myllyharju et al., Oulu, Finland. In Cell Mol Life Sci, 2011
data indicate that the HIF-3alpha variants may have more versatile and specific roles in the regulation of the hypoxia response than previously anticipated
Pro-apoptotic activity of inhibitory PAS domain protein (IPAS), a negative regulator of HIF-1, through binding to pro-survival Bcl-2 family proteins.
Sogawa et al., Sendai, Japan. In Cell Death Differ, 2011
The association of IPAS with Bcl-x(L) was also observed in living cells by the FLIM-based FRET analysis, indicating direct binding between the two proteins.
Tumour necrosis factor-α suppresses the hypoxic response by NF-κB-dependent induction of inhibitory PAS domain protein in PC12 cells.
Sogawa et al., Sendai, Japan. In J Biochem, 2011
NF-kB activation in PC12 cells upregulates IPAS gene expression without activating HIF-1a and HIF-2a.
Brief anoxia preconditioning and HIF prolyl-hydroxylase inhibition enhances neuronal resistance in organotypic hippocampal slices on model of ischemic damage.
Skibo et al., Ukraine. In Brain Res, 2011
Anoxia preconditioning increases anti-ischemic neuronal resistance which to a certain extent correlates with the changes of HIF-1alpha and HIF-3alpha expression.
[Hypoxia-inducible factor-3alpha as a negative regulator of tumorigenesis].
Kondo et al., Tokyo, Japan. In Seikagaku, 2011
It is a negative regulator of tumorigenesis.(review)
[Metastasis and hypoxia-inducible factor].
Nakagawa et al., Japan. In Gan To Kagaku Ryoho, 2010
HIFs consist of a constitutively expressed subunit of HIF-1beta and an oxygen-regulated subunit of HIF-1alpha (or HIF-2alpha and HIF-3alpha).
Hypoxia and hypoxia-inducible factor in renal disease.
Fujita et al., Tokyo, Japan. In Nephron Exp Nephrol, 2007
Intracellular accumulation of HIF induces the coordinated expression of a number of adaptive genes against hypoxic insult.Three isoforms of HIF-alpha subunits have been identified, HIF-1alpha, HIF-2alpha, and HIF-3alpha, of which HIF-2alpha is involved in the regulation of erythropoietin as well as oxidative stress.
Hypoxia and the HIF system in kidney disease.
Eckardt et al., Tokyo, Japan. In J Mol Med (berl), 2007
HIF consists of a constitutive beta-subunit and one of alternative oxygen-regulated HIF alpha-subunits (HIF-1alpha, HIF-2alpha, and HIF-3alpha), and HIF-2alpha is responsible for erythropoietin production.
Discovery of cancer biomarkers through the use of mouse models.
Hanash et al., Ann Arbor, United States. In Cancer Lett, 2007
This is illustrated in a study in which we have applied a three-dimensional intact protein analysis system (IPAS) to elucidate detectable protein changes in serum from immunodeficient mice with lung xenografts from orthotopically implanted human A549 lung adenocarcinoma cells.
Hypoxia-inducible factor-1 (HIF-1).
Costa et al., New York City, United States. In Mol Pharmacol, 2006
HIF-1 consists of a constitutively expressed subunit HIF-1beta and an oxygen-regulated subunit HIF-1alpha (or its paralogs HIF-2alpha and HIF-3alpha).
Inhibitory PAS domain protein is a negative regulator of hypoxia-inducible gene expression.
Poellinger et al., Stockholm, Sweden. In Nature, 2001
Here we describe an inhibitory PAS (Per/Arnt/Sim) domain protein, IPAS, which is a basic helix-loop-helix (bHLH)/PAS protein structurally related to HIFs.
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