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*
Department of Immunology, University of Konstanz, Konstanz, Germany; and
Institute of Biochemistry, Christian-Albrechts University of Kiel, Kiel, Germany
We have previously reported the isolation of the human matrix
metalloproteinase (MMP)-19 (also referred to as RASI) from a synovium
of a patient suffering from rheumatoid arthritis and its expression at
the cell surface of activated PBMC. In this study, we have analyzed the
regulation and cell surface expression of human MMP-19 in several human
cell lines and blood-derived cells. Among the cell lines analyzed,
MMP-19 is largely expressed by lung fibroblasts as well
as by myeloid cell lines THP-1 and HL-60. After fractionating PBMC into
CD14- and CD14+ populations we found that only
the latter one expresses MMP-19. Although the myeloid
cell lines as well as CD14+ cells express
MMP-19 without stimulation, its production can be
up-regulated by phorbol esters (PMA) or by adhesion. The
adhesion-dependent expression was down-regulated or even abrogated by
blockade of adhesion or interfering with adhesion-controlling signaling
using 
-tocopherol. We have shown that MMP-19 associates with the
cell surface of myeloid cells. This cell surface association was not
affected by phospholipase C. However, acidic treatment of the
THP-1-derived cell membranes abolished the immunoprecipitation of
MMP-19 thereof. Moreover, a high salt treatment of THP-1 cells
diminished the MMP-19 detection on the cell surface. This implicates a
noncovalent attachment of MMP-19 to the cell surface. Because a
truncated form of the MMP-19, in which the hemopexin-like domain was
deleted (
hpMMP-19), does not associate with the surface,
the hemopexin-like domain appears to be critical for the cell surface
attachment of human MMP-19.
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