Abstract
The actin cytoskeleton is indispensable for normal cellular function. In particular, several actin-based structures coordinate cellular motility, a process hijacked by tumor cells in order to facilitate their propagation to distant sites. The actin cytoskeleton, therefore, represents a point for chemotherapeutic intervention. The challenge in disrupting the actin cytoskeleton is in preserving actin-driven contraction of cardiac and skeletal muscle. By targeting actin-binding proteins with altered expression in malignancy, it may be possible to achieve tumor-specific toxicity. A number of actin-binding proteins act cooperatively and synergistically to regulate actin structures required for motility. The actin cytoskeleton is characterized by a significant degree of plasticity. Targeting specific actin-binding proteins for chemotherapy will only be successful if no other compensatory mechanisms exist.
Publication types
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Actin Cytoskeleton / chemistry
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Actin Cytoskeleton / drug effects*
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Actin Cytoskeleton / physiology
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Actin-Related Protein 2-3 Complex / genetics
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Actin-Related Protein 2-3 Complex / metabolism
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Cortactin / genetics
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Cortactin / metabolism
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Destrin / genetics
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Destrin / metabolism
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Gelsolin / genetics
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Gelsolin / metabolism
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Humans
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Microfilament Proteins / antagonists & inhibitors*
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Microfilament Proteins / chemistry
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Myosin Type II / genetics
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Myosin Type II / metabolism
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Neoplasms / drug therapy
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Neoplasms / metabolism
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Signal Transduction
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Tropomyosin / genetics
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Tropomyosin / metabolism
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Wiskott-Aldrich Syndrome Protein Family / genetics
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Wiskott-Aldrich Syndrome Protein Family / metabolism
Substances
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Actin-Related Protein 2-3 Complex
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Cortactin
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Destrin
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Gelsolin
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Microfilament Proteins
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Tropomyosin
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Wiskott-Aldrich Syndrome Protein Family
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Myosin Type II