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DIALOG(R)File 72: EMBASE
(c) 2012 Elsevier B.V. All rights reserved.

0086650400 EMBASE/Medline No: 70792427
Fibrin clot structure and fibrinolysis
Weisel J.
University of Pennsylvania, School of Medicine, Philadelphia, PA, United
States
CORRESP. AUTHOR/AFFIL: Weisel J.: University of Pennsylvania, School of
Medicine, Philadelphia, PA, United States
CONFERENCE TITLE: 21st International Congress on Fibrinolysis and　　　　　　<--会議名
Proteolysis
CONFERENCE LOCATION: Brighton United Kingdom 　　　　　　　　　　　　　　　　<--開催地 CONFERENCE DATE: July 1,2012-July 5, 2012　　　　　　　　　　　　　　　　　　　<--開催日

Journal of Thrombosis and Haemostasis ( J. Thromb. Haemost. ) June 1,
2012, 10/6 (e28)
ISSN: 1538-7933
DOI: 10.1111/j.1538-7836.2012.04750.x
DOCUMENT TYPE: Journal; Conference Abstract　　　　　　<--資料の種類：Conference Abstract
RECORD TYPE: Abstract
LANGUAGE: English SUMMARY LANGUAGE: English

Fibrin polymerizes to make clots with a great diversity of structural and
biophysical properties, depending on the circumstances of formation, and
correlations have been established between these properties and many
pathophysiological conditions, such as cardiovascular disease and stroke.
The effectiveness of fibrinolysis results from the combination of regulated
enzymatic activity and the physical characteristics of the fibrin scaffold,
such as the density of fibers and branch points, pore size, and fiber
diameter. The fibrin network structure and its viscoelastic properties are
largely determined by the chemical and environmental conditions of
formation and the kinetics of polymerization, with many factors that can
modulate different steps of polymerization. The rate and nature of
fibrinolysis is related to all of these biophysical and biochemical
properties. Physiologically, clots or thrombi are dissolved from within via
internal lysis. In contrast, with therapeutic thrombolysis, lytic agents
are introduced at one surface and lysis proceeds across the thrombus. In
the latter case, there are complex changes that take place at the lysis
front in a narrow zone. However, at the microscopic and molecular levels
the mechanisms for either general type of fibrinolysis appear to be
similar. Fibrinolysis proceeds by fibers being transected laterally, rather
than digestion of fibers by surface erosion from the outside. In general,
the rate of lysis appears to be faster for clots made up of thicker fibers
than for clots made up of thinner fibers, but also depends on other
biophysical properties of the clot. In addition, platelet aggregation and
clot retraction have dramatic effects on fibrinolysis. Stretching also
affects the rate of lysis of clots. A mathematical model has been developed
to account for many of these observations. Although a great deal is now
known about the process and regulation of fibrinolysis and the molecular
mechanisms involved, many mysteries remain.

DRUG DESCRIPTORS:
fibrin

MEDICAL DESCRIPTORS:
*fibrinolysis; *protein degradation; *fibrin clot
fiber; lysis; polymerization; thrombus; mathematical model; stroke; blood
clot retraction; thrombocyte aggregation; kinetics; cardiovascular disease;
digestion; density; blood clot lysis; stretching; enzyme activity