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hydroxyproline/hypoxia
L'enllaç es desa al porta-retalls
Pàgina 1 des de 115 resultats
von Hippel-Lindau β-domain-luciferase fusion protein as a bioluminescent hydroxyproline sensor for a hypoxia-inducible factor prolyl hydroxylase assay.
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Hypoxia-inducible factor prolyl hydroxylases (HPHs) are responsible for hydroxylation of proline residues in hypoxia-inducible factor-α (HIF-α), resulting in von Hippel-Lindau (VHL)-mediated proteasome degradation of the hydroxylated proteins. Pharmacological inhibition of the enzyme leads to
The Skp1 prolyl hydroxylase from Dictyostelium is related to the hypoxia-inducible factor-alpha class of animal prolyl 4-hydroxylases.
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Skp1 is a cytoplasmic and nuclear protein of eukaryotes best known as an adaptor in SCF ubiquitin-protein isopeptide ligases. In Dictyostelium, Skp1 is subject to 4-hydroxylation at Pro(143) and subsequent O-glycosylation by alpha-linked GlcNAc and other sugars. Soluble cytosolic extracts have Skp1
Expression of arabinogalactan proteins during tomato fruit ripening and in response to mechanical wounding, hypoxia and anoxia.
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Arabinogalactan proteins (AGPs) are highly glycosylated members of the superfamily of hydroxyproline-rich glycoproteins (HRGPs). Despite their implication in many aspects of plant growth and development little is known about their role in tomato fruit ripening (Solanum lycopersicum) and their
The Effects of Chronic Intermittent Hypoxia in Bleomycin-induced lung injury on Pulmonary Fibrosis via Regulating the NF-κB/Nrf2 Signaling Pathway
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Background: Obstructive sleep apnea (OSA) is associated with pulmonary fibrosis. Chronic intermittent hypoxia (CIH) is considered to be a surrogate of OSA. However, its exact role in pulmonary fibrosis remains uncertain. Therefore, we
Response of the left ventricular connective tissue to hypoxia.
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The collagen content (measured as myocardial concentration of hydroxyproline) and dry weight (expressed as ventricle weight to body weight ratio) were determined in the left ventricle of male Sprague-Dawley rats (200--220 g b.wt.) exposed to a simulated altitude of 7,000 m for 18 h a day for 10 days
Protein synthesis in the rat pulmonary trunk during the early development of hypoxia-induced pulmonary hypertension.
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The purpose of this study was to determine the temporal alterations in protein synthesis and accumulation in the rat pulmonary trunk during the early development of hypoxia-induced pulmonary hypertension and to correlate these results with the pattern of development of polycythemia, right
Comparison of fetal, newborn, and adult wound healing by histologic, enzyme-histochemical, and hydroxyproline determinations.
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We compared simultaneous healing processes in fetal, newborn, and maternal rabbits using a miniaturized wound cylinder of expanded Gore-Tex tubing. The tubing was placed subcutaneously in fetal and maternal rabbits on day 23 of pregnancy (term = 31 to 32 days), and in 7-day-old newborn rabbits. At
Quantifying the Binding Interaction between the Hypoxia-Inducible Transcription Factor and the von Hippel-Lindau Suppressor.
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The hypoxia-inducible transcription factors (HIF) play a central role in the human oxygen sensing signaling pathway. The binding of the von Hippel-Lindau tumor suppressor protein (pVHL)-ElonginC-ElonginB complex (VCB) to HIF-1α is highly selective for the trans-4-hydroxylation form of when Pro564 in
Lung growth in hypobaric normoxia, normobaric hypoxia, and hypobaric hypoxia in growing rats. I. Biochemistry.
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Adaptive changes in cellular and connective tissue components of the lung after chronic exposure to reduced ambient oxygen and/or pressure were studied. Four-week-old male Sprague-Dawley rats were randomly divided into five groups (n = 12 each): 1) general control, room air (GC); 2) hypobaric
Prolyl 4-hydroxylases, master regulators of the hypoxia response.
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A decrease in oxygenation is a life-threatening situation for most organisms. An evolutionarily conserved efficient and rapid hypoxia response mechanism activated by a hypoxia-inducible transcription factor (HIF) is present in animals ranging from the simplest multicellular phylum Placozoa to
Inhibition of the catalytic activity of hypoxia-inducible factor-1alpha-prolyl-hydroxylase 2 by a MYND-type zinc finger.
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Hypoxia-induced gene expression is initiated when the hypoxia-inducible factor-1 (HIF-1) alpha subunit is stabilized in response to a lack of oxygen. An HIF-1alpha-specific prolyl-hydroxylase (PHD) catalyzes hydroxylation of the proline-564 and/or -402 residues of HIF-1alpha by an oxygen molecule.
Effect of hypoxia on the synthesis of glycosaminoglycans and collagen by rabbit aortic smooth muscle cells in culture.
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This study evaluated the effect of hypoxia on the connective tissue metabolism of rabbit aortic smooth muscle cells (SMCs) in culture. When the oxygen saturation of the incubation medium was lowered from 20% to 2-3%, synthesis of sulphated glycosaminoglycans (GAGs) and hyaluronic acid, as determined
A fluorescence polarization-based interaction assay for hypoxia-inducible factor prolyl hydroxylases.
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Oxygen-dependent ubiquitination and degradation of hypoxia-inducible factor 1alpha (HIF-1alpha) plays a central role in regulating transcriptional responses to hypoxia. This process requires hydroxylation of specific prolines in HIF-1alpha by HIF prolyl hydroxylase domain (PHD)-containing enzymes,
Prolonged hypoxia accelerates the posttranscriptional process of collagen synthesis in cultured fibroblasts.
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Molecular oxygen is essential for metazoan life. Hypoxia, a reduced oxygen condition, induces systemic and cellular responses for acclimation to the limited oxygen availability. Multicellularity of metazoans is maintained on extracellular matrices. Previously, we demonstrated that acute hypoxia
Analysis of the hypoxia-sensing pathway in Drosophila melanogaster.
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The mechanism by which hypoxia induces gene transcription involves the inhibition of HIF-1alpha (hypoxia-inducible factor-1 alpha subunit) PHD (prolyl hydroxylase) activity, which prevents the VHL (von Hippel-Lindau)-dependent targeting of HIF-1alpha to the ubiquitin/proteasome pathway. HIF-1alpha
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