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The matrikine N-α-PGP couples extracellular matrix fragmentation to endothelial permeability. | LitMetric

The matrikine N-α-PGP couples extracellular matrix fragmentation to endothelial permeability.

Sci Adv

Department of Medicine, University of Alabama at Birmingham, Birmingham, AL 35294, USA ; Program in Protease and Matrix Biology, University of Alabama at Birmingham, Birmingham, AL 35294, USA ; Lung Health Center, University of Alabama at Birmingham, Birmingham, AL 35294, USA ; Medical Service at Birmingham VA Medical Center, Birmingham, AL 35233, USA ; Department of Cell, Developmental, and Integrative Biology, University of Alabama at Birmingham, Birmingham, AL 35294, USA.

Published: January 2015

AI Article Synopsis

Article Abstract

The compartmentalization and transport of proteins and solutes across the endothelium is a critical biologic function altered during inflammation and disease, leading to pathology in multiple disorders. The impact of tissue damage and subsequent extracellular matrix (ECM) fragmentation in regulating this process is unknown. We demonstrate that the collagen-derived matrikine acetylated proline-glycine-proline (N-α-PGP) serves as a critical regulator of endothelial permeability. N-α-PGP activates human endothelial cells via CXC-chemokine receptor 2 (CXCR2), triggering monolayer permeability through a discrete intracellular signaling pathway. In vivo, N-α-PGP induces local vascular leak after subcutaneous administration and pulmonary vascular permeability after systemic administration. Furthermore, neutralization of N-α-PGP attenuates lipopolysaccharide-induced lung leak. Finally, we demonstrate that plasma from patients with acute respiratory distress syndrome (ARDS) induces VE-cadherin phosphorylation in human endothelial cells, and this activation is attenuated by N-α-PGP blockade with a concomitant improvement in endothelial monolayer impedance. These results identify N-α-PGP as a novel ECM-derived matrikine regulating paracellular permeability during inflammatory disease and demonstrate the potential to target this ligand in various disorders characterized by excessive matrix turnover and vascular leak such as ARDS.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4517288PMC
http://dx.doi.org/10.1126/sciadv.1500175DOI Listing

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