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Human HIF1A Protein expressed in Wheat germ - ABIN1306618
Vadivel, Alphonse, Etches, van Haaften, Collins, OReilly, Eaton, Thébaud: Hypoxia-inducible factors promote alveolar development and regeneration. in American journal of respiratory cell and molecular biology 2014
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activation of HIF signaling in osteoprogenitor cells increases blood levels of the chemokine C-X-C motif ligand 12 (show CXCL12 Proteins), which leads to a systemic increase of breast cancer cell proliferation and dissemination through direct activation of the CXCR4 (show CXCR4 Proteins) receptor
HIF regulation of HOIL-1L (show RBCK1 Proteins) targets the phosphorylated PKC-zeta (show PRKCZ Proteins) for degradation and serves as an hypoxia-adaptive mechanism to stabilize the Na,K-ATPase (show ATP1A1 Proteins), avoiding significant lung injury.
our study suggests that HIF1A is a common critical downstream mediator for HLH. We propose that HIF1A activation as the consequence of systemic inflammation, cytokine storm, or ligation of TLR may contribute to HLH development.
Decreased HIF-1alpha may contribute to impaired megakaryopoiesis in immune thrombocytopenia.
The results collectively suggest that in the pressure overload heart failure model, HSF1 (show HSF1 Proteins) promoted formation of macrophages by inducing upregulation of HIF-1 expression, through which heart failure was ameliorated.
Hypoxia-inducible factor 1 alpha deficiency is associated with Renal injury in a mouse model of STZ-induced diabetes.
HIF1alpha activation of Etv2 (show ETV2 Proteins) in embryonic stem cells followed by NOTCH1 (show NOTCH1 Proteins) signaling is required for the generation arterial endothelial cells that are capable of arteriogenesis and revascularization of ischemic tissue.
Results showed that Mn-mediated age-related hearing loss involved an increased level of Hif-1alpha protein with less hydroxylation at proline 564 in spiral ganglion neurons.
Aneurysmal-prone factors induced HIF-1alpha can cause overexpression of MMP-2 (show MMP2 Proteins) and MMP-9 (show MMP9 Proteins) and promote aneurysmal progression.
FSH (show BRD2 Proteins) induces autophagy via upregulation of HIF-1A in mouse granulosa cells.
All these data suggest the possibility that hypoxiamediated PrPC (show PRNP Proteins) serves an important role in angiogenesis. Therefore, the present review summarizes the characteristics of PrPC (show PRNP Proteins), which is produced by HIF1alpha in hypoxia, as it relates to angiogenesis
LncRNA CPS1 (show CPS1 Proteins)-IT1 (show HAUS3 Proteins) suppresses EMT (show ITK Proteins) and metastasis of colorectal cancer by inhibiting hypoxia-induced autophagy through inactivation of HIF-1alpha
both the value and the level of Ki-67 (show MKI67 Proteins) expression were correlated positively with the normalized iodine concentration (NIC (show NCSTN Proteins)) values (r=0.344, P=0.002 and r=0.248, P=0.026); HIF-1alpha expression was correlated positively with the NIC (show NCSTN Proteins) values of the RC (r=0.598, P<0.001)
Our data showed that ampelopsin inhibited angiogenesis with no cytotoxicity by suppressing both VEGFR2 (show KDR Proteins) signaling and HIF-1alpha expression. These results suggest that Hovenia dulcis Thunb. and its active compound ampelopsin exhibit potent antiangiogenic activities and therefore could be valuable for the prevention and treatment of angiogenesis-related diseases including cancer.
the findings of the present study demonstrated that MIF (show AMH Proteins) is a key component in lung cancer progression through promoting the Warburg effect, and that the novel MIF (show AMH Proteins)/NFkappaB (show NFKB1 Proteins)/HIF1alpha axis may prove to be useful for the development of new strategies for treating patients with lung cancer
the present study demonstrated that sevoflurane decreased the malignant behavior of head and neck squamous cell carcinoma cell lines in vitro, which was associated with activation of the HIF-1alpha pathway
The cell surface PDGFRB (show PDGFRB Proteins) is a major link between high glucose and its effectors Hif1a and TGFB (show TGFB1 Proteins) for induction of diabetic mesangial cell hypertrophy.
study suggests that high tumor tissue ascorbate level could limit the expression of HIF-1alpha and its targets in thyroid lesions.
HIF1alpha may be involved in the molecular mechanisms of endometrial dysfunction in women with PCOS, particularly in those who are overweight.
Exogenous proline stimulates type I collagen and HIF-1alpha expression and the process is attenuated by glutamine in human skin fibroblasts.
The results showed that 60-min ischemia of the porcine uterus conducted at the mid-secretory estrous phase caused decreased HIF-1alpha and increased SOD-2 (show SOD2 Proteins) gene expression.
a high expression of hypoxia induced factor-1a (HIF-1a) and heat shock protein 70 (HSP70 (show HSP70 Proteins)) was noted
Induction of ischemic osteonecrosis results in IL-6 (show IL6 Proteins) production in the articular cartilage through an HIF-1-dependent pathway.
Upregulation of VEGF (show VEGFA Proteins) during hypoxia in chondrocyte is mediated partially through HIF-1alpha.
HIF-1alpha activates Sox9 (show SOX9 Proteins) expression and enhances Sox9 (show SOX9 Proteins)-mediated transcriptional activity.
Intramyocardial delivery of mesenchymal stem cells seems to trigger the release of angiogenic HIF-1alpha more effectively than does intracoronary delivery.
immunostaining for HIF-1alpha and HIF-2alpha (show EPAS1 Proteins) was observed during endochondral ossification, whereas only HIF-2alpha (show EPAS1 Proteins) was present at sites of intramembranous ossification
Downregulation of miR (show MYLIP Proteins)-199a derepresses hypoxia-inducible factor-1alpha and Sirtuin 1 (show SIRT1 Proteins) and recapitulates hypoxia preconditioning in cardiac myocytes.
Viable chondrocytes in the superficial layer of the epiphyseal cartilage showed HIF-1alpha activation and VEGF (show VEGFA Proteins) upregulation with subsequent revascularization occurring in the cartilage.
inverse expression and localization pattern of HIF1A and vasohibins during different stages of ovarian function in cow
Hypoxia increased the amounts of HIF1A protein, VEGF (show VEGFA Proteins) mRNA and VEGF (show VEGFA Proteins) protein in cultured bovine luteal cells.
hypoxia-induced changes in vascular cell growth are altered by hyperglycemia via inhibition of HIF-1alpha expression and activity
VEGF (show VEGFA Proteins) has an effect on the expression of its own transcription factor, HIF-1, and on VEGF (show VEGFA Proteins) itself
Identify sphingosine-1-phosphate as a novel and potent nonhypoxic activator of HIF-1.
Suggest supplemental oxygen inhibits HIF-1alpha/VEGF (show VEGFA Proteins) signaling to reduce smooth muscle proliferation in rabbit arteriovenous fistula model.
HIF-1alpha-induced HSP70 (show HSP70 Proteins) overexpression increased the expression levels of ECM (show MMRN1 Proteins) genes and cell viability, and protected chondrocytes from apoptosis. HIF-1alpha may regulate anabolic effects of chondrocytes under hypoxic conditions by regulating HSP70 (show HSP70 Proteins) expression
Transcatheter arterial embolization of liver tumors increases the expression of HIF-1alpha at protein level in the residual viable tumor.
Upregulation of HIF-1 protects cardiac myocyte function after ischemia/reperfusion by maintaining calcium release.
HIF-1alpha expression in early atherosclerosis can promote the formation of neovascularization.
Xells respond to hypoxia through a transcription factor, hypoxia-inducible factor 1
Upregulation of HIF-1 could protect isolated cardiac myocytes against nitrate tolerance through a cyclic GMP protein kinase-independent mechanism and through a kinase-dependent mechanism in myocardial stunning.
rhEPO can down-regulate HIF-1alpha expression in the retina of rabbits with acute high intraocular pressure.
Increased HIF-1 alpha protects the functional effects of cyclic GMP thorough maintenance of cyclic GMP protein kinase activity after ischemic-reperfusion
Our results suggest that these detoxification pathways are mediated by the hypoxia inducible factor HIF-1. Finally, we show that sulfide (show SQRDL Proteins) resistance varies among wild C. elegans and other nematode species, suggesting that tolerance to sulfide (show SQRDL Proteins) was naturally selected in certain habitats.
blocking HIF-1 activity may promote survival in cells with compromised mitochondrial function.
HIF-1-mediated activation of 5-HT (show DDC Proteins) signalling promotes axon regeneration by activating both the RhoA (show RHOA Proteins) and cAMP pathways.
this study reports that neuronal stabilization of HIF-1 mediates these effects in Caenorhabditis elegans through a cell nonautonomous signal to the intestine, which results in activation of the xenobiotic detoxification enzyme flavin-containing monooxygenase-2 (FMO-2 (show FMO2 Proteins)).
AMPK (show PRKAA1 Proteins) and HIF-1 may control immunity and longevity tightly by acting as feedback regulators of ROS (show ROS1 Proteins)
Growth in hypoxia increases longevity in wild-type worms but not in animals lacking HIF-1 or DAF-16. Conversely, hypoxia shortens life span in combination with overexpression of the antioxidant stress response protein SKN-1.
Increased levels of hydrogen peroxide induce a HIF-1-dependent modification of lipid metabolism in AMPK (show PRKAA1 Proteins) compromised C. elegans dauer larvae.
These data show that HIF-1 regulates intestinal iron homeostasis during iron deficiency by activating and inhibiting genes involved in iron uptake and storage.
Data indicate that genes sqrd-1, ethe-1 (show ETHE1 Proteins), cysl-1, cysl-2 and HIF-1 are involved in survival to hydrogen sulfide (show SQRDL Proteins) and hydrogen cyanide.
Data show that stabilization of HIF-1 increases life span robustly under all conditions tested; however, deletion of hif-1 increases life span in a temperature-dependent manner.
This gene encodes the alpha subunit of transcription factor hypoxia-inducible factor-1 (HIF-1), which is a heterodimer composed of an alpha and a beta subunit. HIF-1 functions as a master regulator of cellular and systemic homeostatic response to hypoxia by activating transcription of many genes, including those involved in energy metabolism, angiogenesis, apoptosis, and other genes whose protein products increase oxygen delivery or facilitate metabolic adaptation to hypoxia. HIF-1 thus plays an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease. Alternatively spliced transcript variants encoding different isoforms have been identified for this gene.
, HIF1 alpha
, Hypoxia-inducible factor 1 alpha
, hypoxia-inducible factor 1-alpha
, ARNT-interacting protein
, ARNT interacting protein
, PAS domain-containing protein 8
, basic-helix-loop-helix-PAS protein MOP1
, class E basic helix-loop-helix protein 78
, hypoxia-inducible factor 1 alpha isoform I.3
, hypoxia-inducible factor 1, alpha subunit (basic helix-loop-helix transcription factor)
, hypoxia-inducible factor1alpha
, member of PAS protein 1
, member of PAS superfamily 1
, hypoxia-inducible factor 1 alpha
, hypoxia inducible factor 1 alpha subunit
, hypoxia inducible factor 1, alpha subunit