Kistrin Inhibits Human Smooth Muscle Cell Interaction with Fibrin

Because of the lack of function-blocking anti-integrin antibodies that react with nonprimate species, the study of the role of integrins in in vivo animal models of atherosclerosis has been limited. In contrast, peptides or small molecules have shown less species specificity and thus may be better t...

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Bibliographic Details
Published in:Thrombosis research 2000-01, Vol.97 (2), p.39-50
Main Authors: O Yee, Karen, Ikari, Yuji, Bodary, Sarah, Schwartz, Stephen M.
Format: Article
Language:English
Subjects:
Aorta - cytology
Atherosclerosis
Biological and medical sciences
Blood Coagulation - drug effects
Cardiology. Vascular system
Cell Adhesion - drug effects
Cell Movement - drug effects
Disintegrins - pharmacology
Fibrin - antagonists & inhibitors
Fibrin - metabolism
Fibrin - physiology
Fibrinolytic Agents - pharmacology
Fibronectin
Heart
Heart failure, cardiogenic pulmonary edema, cardiac enlargement
Humans
Infant, Newborn
Integrin
Integrins - antagonists & inhibitors
Medical sciences
Muscle, Smooth - cytology
Muscle, Smooth - metabolism
Muscle, Smooth - physiology
Oligopeptides - pharmacology
Peptides - pharmacology
Peptides, Cyclic - pharmacology
Platelet Aggregation Inhibitors - pharmacology
Remodeling
Sulfoxides - pharmacology
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Summary:Because of the lack of function-blocking anti-integrin antibodies that react with nonprimate species, the study of the role of integrins in in vivo animal models of atherosclerosis has been limited. In contrast, peptides or small molecules have shown less species specificity and thus may be better tools to use. In an attempt to identify integrin antagonists of potential use against smooth muscle response to injury, we investigated the role of human smooth muscle cell interactions with fibrin by using a panel of integrin antagonists consisting of the snake venom disintegrin, Kistrin, as well as cyclic peptides with well-defined integrin antagonists activities. We demonstrate that Kistrin, a disintegrin that inhibits β1, β2, β3, and β5 integrin interactions, had the most potent inhibitory effect. Based on our results, Kistrin or peptides with similar pan-integrin selectivity patterns are prime candidates for use as anti-integrin antagonists in further studies of atherosclerosis and restenosis.
ISSN:0049-3848
1879-2472
DOI:10.1016/S0049-3848(99)00159-0