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Matrix metalloproteinases 2 and 9 increase permeability of sheep pleura in vitro
Authors:Eleni?Apostolidou  mailto:elaposto@med.uth.gr"   title="  elaposto@med.uth.gr"   itemprop="  email"   data-track="  click"   data-track-action="  Email author"   data-track-label="  "  >Email author,Efrosyni?Paraskeva,Konstantinos?Gourgoulianis,Paschalis-Adam?Molyvdas,Chrissi?Hatzoglou
Affiliation:(1) Department of Physiology, University of Thessaly Medical School, Larissa, Biopolis, 41110, Greece;(2) Department of Respiratory Medicine, University of Thessaly Medical School, University Hospital of Larissa, Larissa, Biopolis, 41110, Greece
Abstract:

Background

Matrix metalloproteinases (MMPs) 2 and 9 are two gelatinase members which have been found elevated in exudative pleural effusions. In endothelial cells these MMPs increase paracellular permeability via the disruption of tight junction (TJ) proteins occludin and claudin. In the present study it was investigated if MMP2 and MMP9 alter permeability properties of the pleura tissue by degradation of TJ proteins in pleural mesothelium.

Results

In the present study the transmesothelial resistance (RTM) of sheep pleura tissue was recorded in Ussing chambers after the addition of MMP2 or MMP9. Both enzymes reduced RTM of the pleura, implying an increase in pleural permeability. The localization and expression of TJ proteins, occludin and claudin-1, were assessed after incubation with MMPs by indirect immunofluorescence and western blot analysis. Our results revealed that incubation with MMPs did not alter neither proteins localization at cell periphery nor their expression.

Conclusions

MMP2 and MMP9 increase the permeability of sheep pleura and this finding suggests a role for MMPs in pleural fluid formation. Tight junction proteins remain intact after incubation with MMPs, contrary to previous studies which have shown TJ degradation by MMPs. Probably MMP2 and MMP9 augment pleural permeability via other mechanisms.
Keywords:
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