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Prolyl Hydroxylase Domain Proteins (PHDs)
- Target
- PHDs
- Molecular classification
- Enzyme, Dioxygenase
01
Overview
Prolyl hydroxylase domain proteins (PHDs) are a family of dioxygenase enzymes that regulate the stability of hypoxia-inducible factors (HIFs) by hydroxylating specific proline residues on HIF-alpha subunits. This hydroxylation marks HIF-alpha for degradation under normoxic conditions. PHDs play a crucial role in the cellular response to hypoxia and are implicated in various diseases, including cancer and ischemic conditions. There are three main isoforms: PHD1, PHD2, and PHD3, each with distinct tissue expression patterns and roles.
- Other names
- EGLN1EGLN2EGLN3
02
Mechanism of action
Inhibition of PHD enzymatic activity, leading to increased HIF-alpha levels and activation of HIF-dependent gene transcription.
03
Biological functions
Regulation of HIF-alpha stabilityOxygen sensingRegulation of gene transcription
04
Disease associations
CancerIschemiaAnemiaInflammationCardiovascular disease
05
Safety considerations
Potential for erythrocytosisPossible effects on tumor growthCardiovascular risks
06
Interacting drugs
PHD inhibitors (e.g., Roxadustat, Daprodustat, Molidustat)
07
Biomarkers
HIF-alpha levelsErythropoietin (EPO) levelsVEGF levels
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