Journal
IUBMB LIFE
Volume 61, Issue 6, Pages 613-626Publisher
WILEY
DOI: 10.1002/iub.215
Keywords
endostatin; clinical trials; zinc binding; folding criteria; receptor
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Endostatin, a 20-kDa C-terminal proteolytic fragment of collagen XVIII, is a specific endogenous angiogenesis inhibitor discovered more than a decade. The structure, stability,, and mechanism of actions of endostatin have been extensively investigated (luring the past 12 years, among which controversial reports remain unclarified. The in mysteries include the following: 11) Why, controversial efficacies were observed with endostatin regarding tumor inhibition? Particularly, why does an N-terminal modified endostatin show good clinical responses in China, whereas the clinical trials of the wild type endostatin were terminated at the early stage of phase II in the USA? 2) What is the contribution of zinc-binding to the stability and biological functions of endostatin? 3) Why does insoluble endostatin shrink tumors? 4) How to ensure that endostatin is correctly, refolded? 5) How does endostatin exert its biological functions? Recent progress regarding the biophysical properties, biological functions, signaling path-ways, and clinical trials of endostatin tire reviewed here. Surprising findings show that the integrity of the N-terminal sequence, the capability of zinc-binding, and the correct folding are three essential elements for assurance of structural stability and biological functions of endostatin. This review, provides clues to understand the mysteries of endostatin and its derivatives. (C) 2009 IUBMB IUBMB Life, 61(6): 613-626, 2009
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