Source:http://linkedlifedata.com/resource/pubmed/id/11801661
Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
|
| pubmed:dateCreated |
2002-1-21
|
| pubmed:abstractText |
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 alpha-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 (Delta(hp)MMP-19), does not associate with the surface, the hemopexin-like domain appears to be critical for the cell surface attachment of human MMP-19.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
AIM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD14,
http://linkedlifedata.com/resource/pubmed/chemical/Hemopexin,
http://linkedlifedata.com/resource/pubmed/chemical/Matrix Metalloproteinases, Secreted,
http://linkedlifedata.com/resource/pubmed/chemical/Metalloendopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/matrix metalloproteinase 19
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Feb
|
| pubmed:issn |
0022-1767
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
1
|
| pubmed:volume |
168
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1244-51
|
| pubmed:dateRevised |
2007-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:11801661-Amino Acid Sequence,
pubmed-meshheading:11801661-Antigens, CD14,
pubmed-meshheading:11801661-Cell Adhesion,
pubmed-meshheading:11801661-Cell Differentiation,
pubmed-meshheading:11801661-Cell Fractionation,
pubmed-meshheading:11801661-Cell Line,
pubmed-meshheading:11801661-Cell Membrane,
pubmed-meshheading:11801661-Gene Expression Profiling,
pubmed-meshheading:11801661-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:11801661-HL-60 Cells,
pubmed-meshheading:11801661-HeLa Cells,
pubmed-meshheading:11801661-Hemopexin,
pubmed-meshheading:11801661-Humans,
pubmed-meshheading:11801661-Jurkat Cells,
pubmed-meshheading:11801661-Leukocytes, Mononuclear,
pubmed-meshheading:11801661-Matrix Metalloproteinases, Secreted,
pubmed-meshheading:11801661-Metalloendopeptidases,
pubmed-meshheading:11801661-Molecular Sequence Data,
pubmed-meshheading:11801661-Myeloid Cells,
pubmed-meshheading:11801661-Up-Regulation
|
| pubmed:year |
2002
|
| pubmed:articleTitle |
Matrix metalloproteinase-19 is expressed in myeloid cells in an adhesion-dependent manner and associates with the cell surface.
|
| pubmed:affiliation |
Department of Immunology, University of Konstanz, Konstanz, Germany.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|