Hostname: page-component-78c5997874-v9fdk Total loading time: 0 Render date: 2024-11-14T05:52:45.682Z Has data issue: false hasContentIssue false
  • English
  • Français

Multiple Approaches to Visualizing Fibrin Clot Structure and Assembly

Published online by Cambridge University Press:  02 July 2020

John W. Weisel
John W. Weisel*
Affiliation:
Department of Cell and Developmental Biology, University of Pennsylvania School of Medicine, Philadephia, PA19104-6058
Get access

Extract

Fibrin clot formation is necessary for maintaining the integrity of the vasculature via physiological processes of hemostasis and wound healing and is also involved in pathological processes, such as thrombosis and atherosclerosis. A variety of structural and biophysical approaches has been used to examine intermediates in the formation of clots and to visualize in vitro clots and ex vivo thrombi.

Structures at all stages of polymerization have been examined to learn about molecular mechanisms of assembly. Fibrinogen is a polyfunctional, multi-domain protein that is essential for platelet aggregation and for the formation of the three-dimensional network of fibrin fibers which is the structural basis of the clot. Distinctive functions for several of fibrinogen's domains in the fibrin assembly process have been elucidated. Enzymatic removal of the fibrinopeptides exposes binding sites in the central region which then interact with complementary sites at the ends of a neighboring molecule to yield fibrin oligomers.

Type
From Scanning Probe Microscopy to High Resolution Ultrasound: New Versions of the Vasculature
Information
Microscopy and Microanalysis , Volume 3 , Issue S2: Proceedings: Microscopy & Microanalysis '97, Microscopy Society of America 55th Annual Meeting, Microbeam Analysis Society 31st Annual Meeting, Histochemical Society 48th Annual Meeting, Cleveland, Ohio, August 10-14, 1997 , August 1997 , pp. 329 - 330
Copyright
Copyright © Microscopy Society of America 1997

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Veklich, Y.I. et al., J. Biol. Chem., 268(1993)13577.Google Scholar
Gorkun, O.V. et al., Biochemistry, 33(1994)6986.10.1021/bi00188a031CrossRefGoogle Scholar
Weisel, et al., J. Mol. Biol, 232(1993)285.10.1006/jmbi.1993.1382CrossRefGoogle Scholar
Collet, J.-P. et al., Biophys. J., 70(1996)50010.1016/S0006-3495(96)79596-6CrossRefGoogle Scholar
Woodhead, J.L. et al., J. Biol. Chem., 271(1996)4946.Google Scholar
Baradet, T.C. et al., Biophys. J., 68(1995)1551.10.1016/S0006-3495(95)80327-9CrossRefGoogle Scholar
I thank all of my colleagues and collaborators, especially Drs. Veklich, Nagaswami and Woodhead, and acknowledge the support of NIH grants HL30954 and RR2483 and of the University Research Foundation.Google Scholar