Kringle 5 causes cell cycle arrest and apoptosis of endothelial cells. Biochem Biophys Res Commun 1999 May 19;258(3):668-73
Date
05/18/1999Pubmed ID
10329443DOI
10.1006/bbrc.1999.0612Scopus ID
2-s2.0-0033583830 (requires institutional sign-in at Scopus site) 73 CitationsAbstract
Angiostatin which contains the first four kringle domains of plasminogen has been documented to be a potent inhibitor of angiogenesis. More recently, another kringle structure within plasminogen but outside angiostatin, known as kringle 5 (K5), was found to inhibit endothelial cell proliferation and migration. Here, we report the cloning and expression of mouse kringle 5 (rK5) in a bacterial expression system. The protein was purified to homogeneity using a Ni-NTA column. rK5 inhibited both proliferation and migration of endothelial cells with ED50's of 10 nM and < 500 nM, respectively. In addition, we show for the first time that rK5 causes cell cycle arrest and apoptosis, shedding further insight into rK5's mechanism of action. Finally, we show that these actions are endothelial cell specific.
Author List
Lu H, Dhanabal M, Volk R, Waterman MJ, Ramchandran R, Knebelmann B, Segal M, Sukhatme VPAuthor
Ramani Ramchandran PhD Professor in the Pediatrics department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
Amino Acid SequenceAngiostatins
Animals
Apoptosis
Cattle
Cell Movement
Cells, Cultured
DNA
Endothelium, Vascular
G1 Phase
In Situ Nick-End Labeling
Kringles
Mice
Molecular Sequence Data
Peptide Fragments
Plasminogen
Recombinant Proteins
Sequence Homology, Amino Acid