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A 70-kDa amino-terminal fibronectin fragment supports gelatin binding to macrophages and decreases gelatinase activity.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Penc, S. F. Kaplan, John E. |
| Copyright Year | 1998 |
| Abstract | We previously reported that a macrophage response that increased binding to 125I-radiolabeled soluble denatured collagen (gelatin) was induced by preincubation of macrophage with a 70-kDa amino-terminal fibronectin fragment and soluble nonlabeled gelatin [S. F. Penc, F. A. Blumenstock, J. E. Kaplan (1995) J. Leukoc. Biol. 58, 501-509]. We now report that neither protein synthesis nor recycling of receptors between the cell surface and interior were required for this response. However, removal of cell surface components with trypsin demonstrated that induced gelatin binding required native cell surface constituents. It was found that in the presence of the 70-kDa fibronectin fragment and gelatin, matrix metalloprotease-2 (MMP-2) and matrix metalloprotease-9 (MMP-9) activity in the cell layers was significantly decreased or undetectable, respectively. Similar levels of increased gelatin binding could be reproduced after inhibition of matrix-degrading metalloprotease activity with 1'10-phenanthroline. These results demonstrate that a macrophage specific response that decreased gelatinase activity and increased gelatin binding was initiated by interaction with a 70-kDa fibronectin fragment and gelatin. |
| File Format | PDF HTM / HTML |
| Alternate Webpage(s) | http://www.jleukbio.org/content/64/3/351.full.pdf |
| PubMed reference number | 9738662v1 |
| Volume Number | 64 |
| Issue Number | 3 |
| Journal | Journal of leukocyte biology |
| Language | English |
| Access Restriction | Open |
| Subject Keyword | Gelatin Gelatinases Matrix Metalloproteinase 2 Matrix Metalloproteinase 9 Matrix Metalloproteinases, Membrane-Associated Metalloproteases Recycling Undetectable anatomical layer metallopeptidase activity |
| Content Type | Text |
| Resource Type | Article |