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Volume 51 (11): 1393-1410, 2003
Copyright ©The Histochemical Society, Inc.
REVIEW |
Perlecan and Tumor Angiogenesis
Department of Cell Biology, University of Alabama at Birmingham, Birmingham, Alabama, and Division of Biomedical Sciences, Faculty of Medicine, Imperial College of Science, Technology and Medicine, London, United Kingdom
Correspondence to: Dr. John R. Couchman, Div. of Biomedical Sciences, Sir Alexander Fleming Building, Imperial College of Science, Technology and Medicine, Exhibition Road, South Kensington, London SW7 2AZ, UK. E-mail: j.couchman{at}ic.ac.uk
Perlecan is a major heparan sulfate proteoglycan (HSPG) of basement membranes (BMs) and connective tissues. The core protein of perlecan is divided into five domains based on sequence homology to other known proteins. Commonly, the N-terminal domain I of mammalian perlecan is substituted with three HS chains that can bind a number of matrix molecules, cytokines, and growth factors. Perlecan is essential for metazoan life, as shown by genetic manipulations of nematodes, insects, and mice. There are also known human mutations that can be lethal. In vertebrates, new functions of perlecan emerged with the acquisition of a closed vascular system and skeletal connective tissues. Many of perlecan's functions may be related to the binding and presentation of growth factors to high-affinity tyrosine kinase (TK) receptors. Data are accumulating, as discussed here, that similar growth factor-mediated processes may have unwanted promoting effects on tumor cell proliferation and tumor angiogenesis. Understanding of these attributes at the molecular level may offer opportunities for therapeutic intervention.
(J Histochem Cytochem 51:1393–1410, 2003)
Key Words: perlecan • heparan sulfate proteoglycan • tumor angiogenesis • vascular endothelial growth • factor • fibroblast growth factor
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