|
|
 Previous Article | Table of Contents | Next Article 
Plasmic degradation of crosslinked fibrin. I. Structural analysis of the
particulate clot and identification of new macromolecular-soluble complexes
CW Francis, VJ Marder and SE Martin
Plasmic degradation of crosslinked fibrin has been studied to identify the
proteolytic cleavages that convert the clot into a soluble lysate and also
to identify the derivatives that are likely to circulate during clot
dissolution. Initial polypeptide chain cleavages do not disrupt the solid
clot matrix. With continued exposure to plasmin, high molecular weight
derivatives are produced that remain attached to the clot by noncovalent
forces. Further degradation then results in the liberation into solution of
several large, noncovalently bound complexes. Progressive degradation of
the largest, initially liberated complexes to the terminal derivatives,
DD/E, DD, and E, occurs in solution after their release from the clot. As
the fibrin clot is exposed to plasmin for longer intervals, progressive
dissolution occurs, but the structure of the covalently bound insoluble
fibrin core, the noncovalently attached derivatives, and the liberated
complexes remains constant. Since much of the initially liberated protein
is in complexes larger than DD/E, these derivatives probably represent the
more prevalent plasmic degradation products of crosslinked fibrin in vivo.
Volume 56,
Issue 3,
pp. 456-464,
09/01/1980
Copyright © 1980 by The American Society of Hematology
 CiteULike  Connotea  Del.icio.us  Digg  Reddit  Technorati What's this?
This article has been cited by other articles:
|
|
|
|
 
C. H. Pospisil, A. R. Stafford, J. C. Fredenburgh, and J. I. Weitz
Evidence That Both Exosites on Thrombin Participate in Its High Affinity Interaction with Fibrin
J. Biol. Chem.,
June 6, 2003;
278(24):
21584 - 21591.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
S.-F. Yan, J. Lu, Y. S. Zou, W. Kisiel, N. Mackman, M. Leitges, S. Steinberg, D. Pinsky, and D. Stern
Protein Kinase C-beta and Oxygen Deprivation. A NOVEL Egr-1-DEPENDENT PATHWAY FOR FIBRIN DEPOSITION IN HYPOXEMIC VASCULATURE
J. Biol. Chem.,
April 14, 2000;
275(16):
11921 - 11928.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
R. J. Stewart, J. C. Fredenburgh, B. A. Leslie, B. A. Keyt, J. A. Rischke, and J. I. Weitz
Identification of the Mechanism Responsible for the Increased Fibrin Specificity of TNK-Tissue Plasminogen Activator Relative to Tissue Plasminogen Activator
J. Biol. Chem.,
March 31, 2000;
275(14):
10112 - 10120.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
I. Kohno, K. Inuzuka, Y. Itoh, K. Nakahara, Y. Eguchi, T. Sugo, G. Soe, Y. Sakata, H. Murayama, and M. Matsuda
A monoclonal antibody specific to the granulocyte-derived elastase-fragment D species of human fibrinogen and fibrin: its application to the measurement of granulocyte-derived elastase digests in plasma
Blood,
March 1, 2000;
95(5):
1721 - 1728.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
J. B. Walker and M. E. Nesheim
The Molecular Weights, Mass Distribution, Chain Composition, and Structure of Soluble Fibrin Degradation Products Released from a Fibrin Clot Perfused with Plasmin
J. Biol. Chem.,
February 19, 1999;
274(8):
5201 - 5212.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
J. I. Weitz, B. Leslie, and M. Hudoba
Thrombin Binds to Soluble Fibrin Degradation Products Where it Is Protected From Inhibition by Heparin-Antithrombin but Susceptible to Inactivation by Antithrombin-Independent Inhibitors
Circulation,
February 17, 1998;
97(6):
544 - 552.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
S. Asakura, K. Niwa, T. Tomozawa, Y.-m. Jin, S. Madoiwa, Y. Sakata, T. Sakai, H. Funayama, G. Soe, F. Forgerty, et al.
Fibroblasts Spread on Immobilized Fibrin Monomer by Mobilizing a beta 1-class Integrin, Together with a Vitronectin Receptor alpha vbeta 3 on Their Surface
J. Biol. Chem.,
March 28, 1997;
272(13):
8824 - 8829.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
K. Okada, T. Fujita, K. Minamoto, H. Liao, Y. Naka, and D. J. Pinsky
Potentiation of Endogenous Fibrinolysis and Rescue from Lung Ischemia/Reperfusion Injury in Interleukin (IL)-10-reconstituted IL-10 Null Mice
J. Biol. Chem.,
July 7, 2000;
275(28):
21468 - 21476.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
