Matrix metalloproteinase-19 is expressed in myeloid cells in an adhesion-dependent manner and associates with the

Simon Mauch1, Cornelia Kolb, Birgit Kolb

  • 1Department of Immunology, University of Konstanz, Konstanz, Germany.

Insights

Human matrix metalloproteinase-19 (MMP-19) is expressed on myeloid cells and lung fibroblasts. Its cell surface attachment is noncovalent, mediated by the hemopexin-like domain, and can be regulated by adhesion.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Immunology

Background:

  • Human matrix metalloproteinase-19 (MMP-19), also known as RASI, was previously isolated from rheumatoid arthritis synovium.
  • MMP-19 is expressed on the cell surface of activated peripheral blood mononuclear cells (PBMCs).

Purpose of the Study:

  • To analyze the regulation and cell surface expression of human MMP-19 in various human cell lines and blood cells.
  • To elucidate the mechanism of MMP-19 cell surface association.

Main Methods:

  • Analysis of MMP-19 expression in lung fibroblasts and myeloid cell lines (THP-1, HL-60).
  • Fractionation of PBMCs into CD14- and CD14+ populations.
  • Up-regulation studies using phorbol esters (PMA) and adhesion.
  • Investigation of cell surface association using phospholipase C, acidic treatment, high salt treatment, and a truncated MMP-19 mutant.

Main Results:

  • MMP-19 is predominantly expressed in lung fibroblasts and myeloid cell lines THP-1 and HL-60.
  • CD14+ PBMCs express MMP-19, with production up-regulated by PMA or adhesion.
  • Adhesion-dependent expression is modulated by alpha-tocopherol.
  • MMP-19 associates noncovalently with the cell surface via its hemopexin-like domain.

Conclusions:

  • Human MMP-19 is expressed on lung fibroblasts and myeloid cells, particularly CD14+ PBMCs.
  • Cell surface association of MMP-19 is mediated by its hemopexin-like domain through noncovalent interactions.
  • MMP-19 expression and adhesion-dependent regulation offer potential therapeutic targets.

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