Abstract:
:The first recombinant endostatin that elicited strong antitumor activity was expressed in Escherichia coli and administered as a suspension. Under these conditions, the protein retained its full antiangiogenic activity. Lack of requirement for a folded structure prompted us to investigate antitumor properties of synthetic peptides corresponding to different regions of endostatin. Here, we show that the entire antitumor, antimigration, and antipermeability activities of endostatin are mimicked by a 27-amino-acid peptide corresponding to the NH2-terminal domain of endostatin. This peptide contains three histidines that are responsible for zinc binding. Mutations of the zinc-binding histidines abolished its antitumor and antimigration activities, but not antipermeability properties.
journal_name
Cancer Resjournal_title
Cancer researchauthors
Tjin Tham Sjin RM,Satchi-Fainaro R,Birsner AE,Ramanujam VM,Folkman J,Javaherian Kdoi
10.1158/0008-5472.CAN-04-1833subject
Has Abstractpub_date
2005-05-01 00:00:00pages
3656-63issue
9eissn
0008-5472issn
1538-7445pii
65/9/3656journal_volume
65pub_type
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