Premium
Neutrophils from MMP‐9‐ or neutrophil elastase‐deficient mice show no defect in transendothelial migration under flow in vitro
Author(s) -
Allport Jennifer R.,
Lim YawChyn,
Shipley J. Michael,
Senior Robert M.,
Shapiro Steven D.,
Matsuyoshi Norihisa,
Vestweber Dietmar,
Luscinskas Francis W.
Publication year - 2002
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1189/jlb.71.5.821
Subject(s) - proteases , elastase , neutrophil elastase , adherens junction , neutrophil extracellular traps , biology , microbiology and biotechnology , endothelium , matrix metalloproteinase , immunology , in vitro , inflammation , endothelial stem cell , cell , cadherin , biochemistry , enzyme , endocrinology
Recent evidence has suggested a role for neutrophil proteases during certain inflammatory responses. We demonstrated previously that neutrophil proteases can degrade components of the adherens junctions during neutrophil‐endothelial adhesion. We tested the hypothesis that degradation of VE‐cadherin at lateral junctions by elastase or MMP‐9 facilitates neutrophil transendothelial migration. Neutrophils from MMP‐9 or elastase null mice and strain‐matched control mice expressed high levels of LFA‐1, Mac‐1, and L‐selectin on their cell surface. Under flow conditions, wild‐type and deficient neutrophils rolled, arrested, and transmigrated activated murine endothelium. There was no difference in the total numbers of interacting neutrophils or in the percentage of transmigrated cells. In addition, deficient neutrophils remained capable of degrading murine endothelial VE‐cadherin. These results indicate that although neutrophil proteases may play a role in the acute inflammatory response, neutrophil elastase or MMP‐9 is not essential for neutrophil transendothelial migration in this murine system.