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vasoconstriction-inhibiting factor
- Development stage
- Preclinical
- Lead developer
- Maastricht University
- Modality
- Peptides
- Administration
- Subcutaneous
01
Overview
Vasoconstriction-inhibiting factor (VIF) is an endogenous 35-amino-acid peptide derived from the cleavage of chromogranin A (CgA) by proprotein convertase subtilisin/kexin type 2 (PCSK2) and carboxypeptidase E (CPE). Originally identified as a vasoregulatory peptide that modulates the vasoconstrictive effects of angiotensin II via the angiotensin II type 2 receptor (AT2R), VIF has also been characterized as a potent endogenous calcimimetic of the calcium-sensing receptor (CaSR). By binding to and activating CaSR, VIF peptide inhibits vascular calcification in vascular smooth muscle cells (VSMCs) by decreasing calcium influx, reducing reactive oxygen species (ROS) production, decreasing apoptosis, and increasing the production of carboxylated matrix Gla protein (cMGP). It is being investigated for the prevention and treatment of vascular calcification, particularly in patients with chronic kidney disease (CKD).
- Other names
- VIFVIF peptidevasoconstriction inhibiting factor
02
Targets
CaSR (Extracellular calcium-sensing receptor)AGTR2 (AT2)
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