Hif1 Alpha Subunit
Hif1 Alpha Subunit - Related Videos
09:36
Recombinant α- β- and γ-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays
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Cited by 7 •
2017
This publication presents a protocol showing how to measure the activity of recombinant protein phosphatase 2A catalytic subunit (PP2Ac) in response to recombinant α-synuclein, β-synuclein, or γ-synuclein proteins using a simple colorimetric assay. We show findings regarding α-synuclein specificity toward PP2Ac in mouse brain.
08:55
Characterization of Multi-subunit Protein Complexes of Human MxA Using Non-denaturing Polyacrylamide Gel-electrophoresis
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Cited by 3 •
2016
This article describes a simple and rapid protocol to evaluate the oligomeric state of the dynamin-like GTPase MxA protein from lysates of human cells using a combination of non-denaturing PAGE with western blot analysis.
06:09
In Vitro Reassociation Assay to Measure the Formation of 80S Ribosomal Particles Using Salt-washed Ribosomal Subunits
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2025
Here, we describe a detailed protocol for the in vitro reassociation of purified, salt-washed eukaryotic ribosomal subunits for the analysis of 80S particle formation. This method is illustrated by analyzing ribosomal subunits isolated from a wild-type strain of Saccharomyces cerevisiae and a mutant strain deficient in the ribosomal protein eL24.
01:30
Detection of Phosphorylated Alpha-Synuclein Using Western Blotting
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2025
Add a loading buffer containing a detergent, a reducing agent, and a tracking dye.
03:25
Immunostaining of Neurons Treated with Alpha-Synuclein Aggregates
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2025
This video demonstrates the immunostaining of neurons treated with alpha-synuclein (αS) aggregates. The neurons are first treated with αS aggregates. They are then fixed, permeabilized, and treated with a blocking solution. Primary antibodies are added, followed by a fluorescently labeled secondary antibodies and a nuclear stain. The sample is then mounted and observed under a microscope.
FAQs
Under normal oxygen conditions, prolyl hydroxylation acts as a turnover signal rather than merely a chemical modification. It enables recognition by von Hippel-Lindau protein, which directs HIF-1 alpha toward proteasomal degradation. Consequently, oxygen availability controls how long the subunit persists, linking a molecular modification to the strength and duration of the cellular response.
During hypoxia, reduced prolyl hydroxylation changes the fate of HIF-1 alpha. The subunit can accumulate, move into the nucleus, and pair with HIF-1 beta. This dimer then recognizes hypoxia-response elements in DNA, converting an oxygen-sensitive stability change into coordinated transcriptional regulation rather than an isolated protein-level response.
HIF-1 alpha supplies the oxygen-responsive change, while HIF-1 beta provides the required dimer partner described in the HIF-1 complex. Their association creates the transcription factor that binds hypoxia-response elements. This explains why altered abundance of the alpha subunit can influence a broad gene program, including glycolysis, angiogenesis, erythropoiesis, and cell survival.
A useful comparison examines the subunit under normal oxygen conditions and hypoxia, then follows the sequence described for oxygen sensing: prolyl hydroxylation, recognition by von Hippel-Lindau protein, proteasomal turnover, nuclear entry, dimerization with HIF-1 beta, and binding to hypoxia-response elements. Relating these stages helps connect protein stability with downstream transcriptional activity.
An increase in HIF-1 alpha during hypoxia is interpreted together with its downstream location and partners, not as an isolated measurement. Stabilization, nuclear entry, association with HIF-1 beta, and binding to hypoxia-response elements provide a sequence of evidence for pathway activation. The expected transcriptional consequences include genes supporting glycolysis, angiogenesis, erythropoiesis, and cell survival.
Because the subunit links oxygen availability to several adaptive gene programs, its regulation provides a framework for examining diseases in which oxygen homeostasis is important. The same pathway can be studied through its effects on glycolysis, angiogenesis, erythropoiesis, and cell survival. These connections make HIF-1 alpha relevant across cancer, ischemia, and pulmonary disorders.