Migration of Neutrophils across Human Pulmonary Endothelial Cells Is Not Blocked by Matrix Metalloproteinase or Serine Protease Inhibitors

It has long been speculated that neutrophils deploy proteases to digest subendothelial matrix as they migrate from the bloodstream. Direct evidence for the involvement of proteases in neutrophil transendothelial migration is, however, lacking. To address this issue we used transmission electron micr...

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Published inAmerican journal of respiratory cell and molecular biology Vol. 20; no. 6; pp. 1209 - 1219
Main Authors Mackarel, A. Jill, Cottell, David C, Russell, Kenneth J, FitzGerald, Muiris X, O'Connor, Clare M
Format Journal Article
LanguageEnglish
Published United States Am Thoracic Soc 01.06.1999
American Thoracic Society
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Abstract It has long been speculated that neutrophils deploy proteases to digest subendothelial matrix as they migrate from the bloodstream. Direct evidence for the involvement of proteases in neutrophil transendothelial migration is, however, lacking. To address this issue we used transmission electron microscopy to verify the presence of continuous basal lamina beneath pulmonary endothelial cells grown on microporous filters, and then examined the effects of protease inhibitors on neutrophil migration through the endothelial cells and their associated subcellular matrix. Inhibitors of the two major matrix-degrading protease groups present in neutrophils, the matrix metalloproteinases (MMPs) and serine proteases, were assessed for their ability to modulate neutrophil transendothelial migration in response to the chemoattractant n-formylmethionyl leucylphenylalanine (FMLP). Neither the naturally occurring MMP inhibitor, tissue inhibitor of metalloproteinase-1, nor the hydroxamic acid-based inhibitors GM-6001, BB-3103, or Ro 31-9790 had any significant effect on FMLP-stimulated neutrophil migration across endothelial cells and associated basal lamina, with >/= 80% of neutrophils migrating through the system, even in the presence of inhibitors, at concentrations that totally inhibited all the gelatinase B (MMP-9) released upon stimulation with FMLP. Similarly, with serine protease inhibitors no significant inhibition of neutrophil migration was observed with a naturally occurring inhibitor, secretory leukocyte protease inhibitor, or a low molecular-weight synthetic inhibitor, Pefabloc SC. These results indicate that neither MMP nor serine protease digestion of sub-endothelial matrix is required for successful neutrophil transendothelial migration.
AbstractList It has long been speculated that neutrophils deploy proteases to digest subendothelial matrix as they migrate from the bloodstream. Direct evidence for the involvement of proteases in neutrophil transendothelial migration is, however, lacking. To address this issue we used transmission electron microscopy to verify the presence of continuous basal lamina beneath pulmonary endothelial cells grown on microporous filters, and then examined the effects of protease inhibitors on neutrophil migration through the endothelial cells and their associated subcellular matrix. Inhibitors of the two major matrix-degrading protease groups present in neutrophils, the matrix metalloproteinases (MMPs) and serine proteases, were assessed for their ability to modulate neutrophil transendothelial migration in response to the chemoattractant n-formylmethionyl leucylphenylalanine (FMLP). Neither the naturally occurring MMP inhibitor, tissue inhibitor of metalloproteinase-1, nor the hydroxamic acid-based inhibitors GM-6001, BB-3103, or Ro 31-9790 had any significant effect on FMLP-stimulated neutrophil migration across endothelial cells and associated basal lamina, with >/= 80% of neutrophils migrating through the system, even in the presence of inhibitors, at concentrations that totally inhibited all the gelatinase B (MMP-9) released upon stimulation with FMLP. Similarly, with serine protease inhibitors no significant inhibition of neutrophil migration was observed with a naturally occurring inhibitor, secretory leukocyte protease inhibitor, or a low molecular-weight synthetic inhibitor, Pefabloc SC. These results indicate that neither MMP nor serine protease digestion of sub-endothelial matrix is required for successful neutrophil transendothelial migration.
It has long been speculated that neutrophils deploy proteases to digest subendothelial matrix as they migrate from the bloodstream. Direct evidence for the involvement of proteases in neutrophil transendothelial migration is, however, lacking. To address this issue we used transmission electron microscopy to verify the presence of continuous basal lamina beneath pulmonary endothelial cells grown on microporous filters, and then examined the effects of protease inhibitors on neutrophil migration through the endothelial cells and their associated subcellular matrix. Inhibitors of the two major matrix-degrading protease groups present in neutrophils, the matrix metalloproteinases (MMPs) and serine proteases, were assessed for their ability to modulate neutrophil transendothelial migration in response to the chemoattractant n-formylmethionyl leucylphenylalanine (FMLP). Neither the naturally occurring MMP inhibitor, tissue inhibitor of metalloproteinase-1, nor the hydroxamic acid-based inhibitors GM-6001, BB-3103, or Ro 31-9790 had any significant effect on FMLP-stimulated neutrophil migration across endothelial cells and associated basal lamina, with >/= 80% of neutrophils migrating through the system, even in the presence of inhibitors, at concentrations that totally inhibited all the gelatinase B (MMP-9) released upon stimulation with FMLP. Similarly, with serine protease inhibitors no significant inhibition of neutrophil migration was observed with a naturally occurring inhibitor, secretory leukocyte protease inhibitor, or a low molecular-weight synthetic inhibitor, Pefabloc SC. These results indicate that neither MMP nor serine protease digestion of sub-endothelial matrix is required for successful neutrophil transendothelial migration.
Author O'Connor, Clare M
Cottell, David C
FitzGerald, Muiris X
Russell, Kenneth J
Mackarel, A. Jill
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  doi: 10.1042/bj2490327
– ident: B31
  doi: 10.1165/ajrcmb.13.3.7654388
– ident: B38
  doi: 10.1002/path.1700820103
– ident: B21
  doi: 10.1021/bi00146a017
– ident: B40
  doi: 10.1182/blood.V65.3.513.513
– ident: B23
  doi: 10.1111/j.1476-5381.1989.tb12673.x
– volume: 33
  start-page: 429
  year: 1983
  ident: B39
  publication-title: J. Reticuloendothel. Soc.
  contributor:
    fullname: Lipscomb M. F.
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Snippet It has long been speculated that neutrophils deploy proteases to digest subendothelial matrix as they migrate from the bloodstream. Direct evidence for the...
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SubjectTerms Cell Movement
Cells, Cultured
Dose-Response Relationship, Drug
Endothelium - metabolism
Endothelium, Vascular - metabolism
Endothelium, Vascular - ultrastructure
Extracellular Matrix - metabolism
Humans
Lung - metabolism
Metalloendopeptidases - pharmacology
Neutrophils - metabolism
Neutrophils - ultrastructure
Serine Proteinase Inhibitors - pharmacology
Title Migration of Neutrophils across Human Pulmonary Endothelial Cells Is Not Blocked by Matrix Metalloproteinase or Serine Protease Inhibitors
URI http://ajrcmb.atsjournals.org/cgi/content/abstract/20/6/1209
https://www.ncbi.nlm.nih.gov/pubmed/10340940
https://www.proquest.com/docview/207649695
https://search.proquest.com/docview/69780956
Volume 20
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