Open AccessProduction of proteolytic enzymes in mast cells, fibroblasts, vascular smooth muscle and endothelial cells cultivated under normoxic or hypoxic conditions
Author(s) -
Hana Maxová,
Lucie Bačáková,
Lisa Vaccari,
Jaovotná,
H Tomášová,
M Vízek,
J Herget
Publication year - 2010
Publication title -
physiological research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.647
H-Index - 70
eISSN - 1802-9973
pISSN - 0862-8408
DOI - 10.33549/physiolres.931909
Subject(s) - chymase , tryptase , proteases , matrix metalloproteinase , mast cell , extracellular matrix , proteolytic enzymes , hypoxia (environmental) , chemistry , biology , extracellular , microbiology and biotechnology , biochemistry , enzyme , immunology , organic chemistry , oxygen
Matrix metalloproteinases (MMPs) is a family of proteolyticenzymes involved in remodeling of extracellular matrix. Althoughproteolytic enzymes are produced by many cell types, mast cellsseem to be more important than other types in remodeling ofpulmonary arteries during hypoxia. Therefore, we tested in vitroproduction of MMPs and serine proteases in four cell types (mastcells, fibroblasts, vascular smooth muscle cells and endothelialcells) cultivated for 48 h under normoxic or hypoxic (3 % O2)conditions. MMP-13 was visualized by immunohistochemistry,MMP-2 and MMP-9 were detected by zymography in cell lysates.Enzymatic activities (MMPs, tryptase and chymase) wereestimated in the cultivation media. Hypoxia had a minimal effecton total MMP activity in the cultivation media of all types of cells,but immunofluorescence revealed higher intensity of MMP-13 inthe cells exposed to hypoxia except of fibroblasts. Tryptaseactivity was three times higher and chymase activity twice higherin mast cells cultivated in hypoxia than in those cultured innormoxia. Among all cell types studied here, mast cells are themost abundant source of proteolytic enzymes under normoxicand hypoxic conditions. Moreover, in these cells hypoxiaincreases the production of both specific serine proteasestryptase and chymase, which can act as MMPs activators.