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Characterization of Crosslinking Sites in Fibrinogen for Plasminogen Activator Inhibitor 2 (PAI-2)
| Content Provider | Scilit |
|---|---|
| Author | Ritchie, Helen Lawrie, Laura C. Mosesson, Michael W. Booth, Nuala A. |
| Copyright Year | 2006 |
| Description | Journal: Annals of the New York Academy of Sciences PAI‐2 is a serpin that can be crosslinked to fibrin(ogen) via the Gln‐Gln‐Ile‐Gln sequence (residues 83–86). We have characterized the lysine residues in fibrinogen to which PAI‐2 is crosslinked by tissue transglutaminase and factor XIIIa. There was no competition with the crosslinking of $α_{2}$‐antiplasmin, another inhibitor of fibrinolysis, which was specific for Lys 303 in the Aα chain. PAI‐2 was crosslinked to several lysine residues, all in the Aα chain, 148, 176, 183, 230, 413, and 457, but not to Lys 303. The contrast with $α_{2}$‐antiplasmin was clear from studies with truncated fibrinogens and competition by peptides. This was confirmed and extended by mass spectrometry of peptides after protease digestion of crosslinked products, which identified the lysine residues to which the inhibitors were crosslinked. PAI‐2 remained active after cross‐linking and inhibited fibrin breakdown, even by two‐chain t‐PA. Thus, a second inhibitor of fibrinolysis, in addition to $α_{2}$‐antiplasmin, is crosslinked to fibrin and protects it from lysis. |
| Related Links | https://nyaspubs.onlinelibrary.wiley.com/doi/pdf/10.1111/j.1749-6632.2001.tb03508.x |
| Ending Page | 218 |
| Page Count | 4 |
| Starting Page | 215 |
| e-ISSN | 17496632 |
| DOI | 10.1111/j.1749-6632.2001.tb03508.x |
| Journal | Annals of the New York Academy of Sciences |
| Issue Number | 1 |
| Volume Number | 936 |
| Language | English |
| Publisher | Wiley-Blackwell |
| Publisher Date | 2006-01-25 |
| Access Restriction | Open |
| Subject Keyword | Journal: Annals of the New York Academy of Sciences Dentistry and Oral Surgery Plasminogen Activator Inhibitor 2 |
| Content Type | Text |
| Resource Type | Article |
