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Hypoxia

FIH-1/HIF-1AN - a transcriptional regulator of HIF-1 alpha in oxygen sensing and beyond

FIH-1/HIF-1AN (factor inhibiting hypoxia-inducible factor-1/ HIF1AN) is a 40.3kDa protein which is expressed as asparaginyl hydroxylase enzyme in various multicellular organisms from worms/flies to mouse/rat and human beings.

Carbonic anhydrase IX (CAIX) - a reliable histochemical marker of hypoxia

Carbonic anhydrase IX is a member of the carbonic anhydrase family. This family consists of catalytic enzymes capable of converting carbon dioxide and water into carbonic acid, protons, and bicarbonate ions. This family of molecules is abundantly expressed in all mammalian tissues and helps to govern the pH in normal tissues. CAIX is very stable and found in the membrane. It is also one of the most hypoxically-inducible genes, thus establishing its application as a reliable and consistent hypoxia histochemical marker.

PCSK9: To neuron or not to neuron

PCSK9 (Proprotein convertase subtilisin/kexin type 9) is a member of the proteinase K subfamily of the secretory subtilase family. It is first produced as a soluble zymogen that then undergoes an autocatalytic processing within the endoplasmic reticulum (ER). PCSK9 functions in cholesterol homeostasis as well as cortical neuron differentiation. Mutations in this gene are associated with a third form of autosomal dominant familial hypercholesterolemia (HCHOLA3).

HIF-1 beta: A Dimerization Partner of HIF-1 alpha Required for an Adaptive Response to Hypoxia

Hypoxia contributes significantly to the pathophysiology of major categories of human disease, including myocardial and cerebral ischemia, cancer, pulmonary hypertension, congenital heart disease and chronic obstructive pulmonary disease. Hypoxia-inducible factor 1 (HIF-1) is a nuclear protein involved in mammalian oxygen homeostasis.

HIF-2 alpha, Tumor Suppression and Cell Survival

HIF-2 alpha is one subunit within the HIF-2 nuclear protein that regulates cellular responses to hypoxia (low oxygen tension conditions). Hydroxylation post-translational modifications on particular HIF residues target them for degradation. Luo, et al.

Marking Hypoxia and Cancer with CAIX

Carbonic anhydrase IX (CAIX) is a member of the carbonic anhydrase family - enzymes that enable the rapid conversion of carbon dioxide and water into carbonic acid, protons, and bicarbonate ions. Carbonic anhydrases have a widespread role in regulating pH in normal tissues and are abundantly found in all mammalian tissues. CAIX itself is one of the most hypoxically-inducible genes due to its stability and membrane location.

HIF Prolyl Hydroxylase 1: A Key Regulator of HIF1A Levels

Hypoxia inducible factors (HIFs) are transcription factors that regulate the cellular response to decreases in oxygen levels. Under conditions of hypoxia HIFs activate the transcription of a diverse range of genes, resulting in increased oxygen delivery to the cell or metabolic adaptation.

HIF-1 Alpha: Infographic

Encoded by the HIF1A gene, HIF-1 alpha has a critical role in cellular response to hypoxia. In hypoxic conditions, HIF-1 alpha activates the transcription of several genes to facilitate metabolic reaction for lack of oxygen. In normoxic conditions, HIF-1 alpha is degraded by the proteasome system.

Learn more about HIF-1 Alpha in our infographic below.

HIF-1 Alpha Infogrphic

PHD2: Sensing Cellular Hypoxia

Prolyl-hydroxylase Domain Containing Protein 2 (PHD2) is one of four hydroxylase enzymes that function as oxygen sensors. They are responsible for the post-translational modification of hypoxia-inducible factor 1 alpha (HIF-1 alpha), a component of the transcriptional complex involved in oxygen homeostasis.

LC3B Empowers Protein Quality Control by Autophagy

LC3B, also known as microtubule-associated protein 1 light chain 3 beta (MAP1LC3B), is an autophagy gene that contributes appreciably to protein degradation. Autophagy is a highly synchronized and dynamic catabolic degradation activity that plays an essential role in cellular maintenance, development, antigen presentation and cell death.

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