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Analyzing the Functions of Mast Cells In Vivo Using 'Mast Cell Knock-in' Mice
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Mast Cell Protease 7 Promotes Angiogenesis by Degradation of Integrin Subunits
Devandir A de Souza Junior1, Carolina Santana2, Gabriel V Vieira3
1Department of Cell and Molecular Biology and Pathogenic Bioagents, Ribeirão Preto Medical School, University of São Paulo, Ribeirão Preto 14.049-900, Brazil. dasjunior@hotmail.com.
Cells
|April 25, 2019
Summary
Recombinant mouse mast cell protease-7 (rmMCP-7) directly degrades integrin subunits, initiating angiogenesis. This protease is sufficient to drive new blood vessel formation by impacting endothelial cell migration and tube formation.
Area of Science:
- Biochemistry
- Cell Biology
- Physiology
Background:
- Previous studies showed recombinant mouse mast cell protease-7 (rmMCP-7) stimulates endothelial cell spreading and matrix penetration in vitro.
- Angiogenesis, the formation of new blood vessels, is crucial for development and disease.
Purpose of the Study:
- To assess the in vivo angiogenesis potential of rmMCP-7.
- To investigate the relationship between rmMCP-7 and integrins during angiogenesis.
Main Methods:
- Directed in vivo angiogenesis assay (DIVAA™) to evaluate rmMCP-7's angiogenic capacity.
- In vitro studies using SVEC4-10 endothelial cells to analyze integrin subunit levels after rmMCP-7 incubation.
- Experiments with proteasome inhibitors to differentiate degradation pathways.
Main Results:
- rmMCP-7 induced significant vessel invasion in the DIVAA™ model, unlike controls.
- rmMCP-7 reduced integrin subunits αv and β1 levels on endothelial cells.
- Integrin degradation by rmMCP-7 was observed directly and via the ubiquitin/proteasome system.
- rmMCP-7 promoted endothelial cell migration, tube formation, and loop formation, even with proteasome inhibition.
Conclusions:
- rmMCP-7 directly degrades integrin subunits, which is sufficient to initiate angiogenesis.
- This study demonstrates for the first time that mMCP-7 mediates angiogenesis through integrin degradation.
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