Review Article

Hypoxia-Inducible Factor-1 in Physiological and Pathophysiological Angiogenesis: Applications and Therapies

Figure 1

Schematic representation of HIF-α gene structures and DNA binding. (a) HIF-1α and HIF-2α contain the following domains: a nuclear localisation domain (NLS), DNA binding and dimerisation domains (bHLH/PAS), oxygen-dependent degradation domain (ODDD), and cofactor interaction and transcriptional activity domains (N-TAD/C-TAD). HIF-3α lacks a C-TAD domain. NLS: nuclear localisation signal; bHLH: basic helix-loop-helix domain; PAS: Per-ARNT-Sim motif; ODDD: oxygen-dependent degradation domain; N-TAD: N-terminal transactivation domain; C-TAD: C-terminal transactivation domain. (b) Dimerisation of HIF-1α with HIF-1β under hypoxic conditions results in the formation of the HIF-1 transcription factor, which binds to hypoxia response elements (HREs) and activates the transcription of O2-dependent genes (according to [134]).
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