VEGF (vascular endothelial growth factor)

VEGF — vascular endothelial growth factor — is the family of dimeric glycoprotein ligands that bind VEGFR receptor tyrosine kinases on vascular endothelial cells. The VEGF-A isoform binding to VEGFR2 is the central upstream signal in the most-cited BPC-157 angiogenic mechanism.

Definition

VEGF is a family of secreted dimeric glycoproteins comprising five mammalian members (VEGF-A, VEGF-B, VEGF-C, VEGF-D, and placental growth factor PlGF) plus virally encoded VEGF-E. The members differ in their receptor specificity: VEGF-A is the canonical angiogenic ligand and binds VEGFR1 and VEGFR2; VEGF-C and VEGF-D bind VEGFR3 and are the primary lymphangiogenic ligands. VEGF-A alone exists in several splice isoforms (VEGF-A121, VEGF-A165, VEGF-A189, VEGF-A206 in humans) that differ in their heparin-binding and matrix-anchoring properties.

VEGF expression is induced by hypoxia via the hypoxia-inducible-factor (HIF) transcriptional response, by inflammatory cytokines, by mechanical stretch in vascular beds, and by tissue injury. The compound is the master upstream regulator of physiological and pathological neovascularisation and is the target of multiple FDA-approved anti-angiogenic biologics in oncology and ophthalmology contexts.

How VEGF is studied in peptide research

VEGF involvement in a peptide’s mechanism is established by measuring VEGF expression (ELISA on cell-culture supernatant or tissue lysate, quantitative PCR for transcript) alongside the corresponding receptor-activation readout downstream. Pharmacological blockade with anti-VEGF antibodies (bevacizumab, ranibizumab) or VEGFR-blocking antibodies and small molecules is used to confirm causation. When the blockade abolishes the peptide’s observed angiogenic or perfusion-modulating effect, the VEGF-VEGFR axis is implicated.

For BPC-157 the dominant published mechanism is VEGFR2 activation on the vascular endothelium with downstream Akt phosphorylation and endothelial nitric oxide synthase signalling (PMID 27847966). The receptor-engagement framing implicates the VEGF axis at the upstream end of the cascade. The Sikiric group’s blood-vessel review consolidates the wider vascular-signalling literature for the compound (PMID 23782145), and the nitric-oxide-system work links the cascade to downstream NO output (PMID 23755725). The major-vessel-occlusion work extends the model to ischemia-reperfusion contexts where VEGF-driven collateral recruitment is a plausible downstream contributor (PMID 35125818).

Related terms

• VEGFR2
• Angiogenesis
• Akt signalling
• eNOS
• HIF / hypoxia-inducible factor
• Growth factor
• Tyrosine kinase receptor

Compounds where VEGF appears in the mechanism literature

• BPC-157 — VEGFR2 activation is the most-cited mechanism, placing VEGF at the upstream end of the receptor-engagement cascade
• TB-500 — VEGF-independent angiogenic signalling via integrin-linked kinase pathways, mechanistically distinct but with overlapping vascular outcomes
• GHK-Cu — copper-dependent angiogenic and ECM-remodelling signalling examined alongside the VEGF axis in adjacent tissue-repair contexts

References

1. Hsieh MJ et al. Therapeutic potential of pro-angiogenic BPC157 is associated with VEGFR2 activation and up-regulation. J Mol Med (Berl) 2017;95(3):323-333. [PMID 27847966]
2. Seiwerth S et al. BPC 157 and blood vessels. Curr Pharm Des 2014;20(7):1121-1125. [PMID 23782145]
3. Sikiric P et al. Stable gastric pentadecapeptide BPC 157-NO-system relation. Curr Pharm Des 2014;20(7):1126-1135. [PMID 23755725]
4. Sikiric P et al. Cytoprotective gastric pentadecapeptide BPC 157 resolves major vessel occlusion disturbances. World J Gastroenterol 2022;28(1):1-22. [PMID 35125818]

Glossary entries describe research-context use of peptide-research terminology. They do not constitute medical, veterinary, or clinical advice. Every compound in the Ronin catalog is sold strictly for laboratory and research use only.