ArticleScientific reports2018
Vasoinhibin comprises a three-helix bundle and its antiangiogenic domain is located within the first 79 residues.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 16 citations in OpenAlex.
- Levosulpiride Increases the Levels of Prolactin and Antiangiogenic Vasoinhibin in the Vitreous of Patients with Proliferative Diabetic Retinopathy.Translational vision science & technology · 2020Trial
- 14K prolactin derived 14-mer antiangiogenic peptide targets bradykinin-/nitric oxide-cGMP-dependent angiogenesis.FEBS open bio · 2024Article
- Immunometric and functional measurement of endogenous vasoinhibin in human sera.Frontiers in endocrinology · 2024Article
- Vasoinhibin's Apoptotic, Inflammatory, and Fibrinolytic Actions Are in a Motif Different From Its Antiangiogenic HGR Motif.Endocrinology · 2023Article
- Human Placental Tissue Contains A Placental Lactogen-Derived Vasoinhibin.Journal of the Endocrine Society · 2022Article
- The HGR motif is the antiangiogenic determinant of vasoinhibin: implications for a therapeutic orally active oligopeptide.Angiogenesis · 2022Article
- Prolactin and vasoinhibin are endogenous players in diabetic retinopathy revisited.Frontiers in endocrinology · 2022Review
- Short prolactin isoforms are expressed in photoreceptors of canine retinas undergoing retinal degeneration.Scientific reports · 2021Article
- Development of Vasoinhibin-Specific Monoclonal Antibodies.Frontiers in endocrinology · 2021Article
- Regulator of Angiogenesis and Vascular Function: A 2019 Update of the Vasoinhibin Nomenclature.Frontiers in endocrinology · 2019Article
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
Abstract
Vasoinhibin belongs to a family of angiogenesis inhibitors generated when the fourth α-helix (H4) of the hormone prolactin (PRL) is removed by specific proteolytic cleavage. The antiangiogenic properties are absent in uncleaved PRL, indicating that conformational changes create a new bioactive domain. However, the solution structure of vasoinhibin and the location of its bioactive domain are unknown. Molecular dynamic simulation (MD) showed that the loss of H4 exposes the hydrophobic nucleus of PRL and leads to the compression of the molecule into a three-helix bundle that buries the hydrophobic nucleus again. Compression occurs by the movement of loop 1 (L1) and its interaction with α-helix 1 (H1) generating a new L1 conformation with electrostatic and hydrophobic surfaces distinct from those of PRL, that may correspond to a bioactive domain. Consistent with this model, a recombinant protein containing the first 79 amino acids comprising H1 and L1 of human PRL inhibited the proliferation and migration of endothelial cells and upregulated the vasoinhibin target genes, IL1A and ICAM1. This bioactivity was comparable to that of a conventional vasoinhibin having the 123 residues encompassing H1, L1, Η2, L2, and Η3 of human PRL. These findings extend the vasoinhibin family to smaller proteins and provide important structural information, which will aid in antiangiogenic drug development.
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