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Human apolipoprotein(a) kringle V inhibits angiogenesis in vitro and in vivo by interfering with the activation of focal adhesion kinases

Authors
 Jang-Seong Kim  ;  Hyun-Kyung Yu  ;  Jin-Hyung Ahn  ;  Ho-Jeong Lee  ;  Soon-Won Hong  ;  Kyung-Hwan Jung  ;  Soo-Ik Chang  ;  Yong-Kil Hong  ;  Young-Ae Joe  ;  Si-Myung Byun  ;  Suk-Keun Lee  ;  Soo-Il Chung  ;  Yeup Yoon 
Citation
 BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, Vol.313(3) : 534-540, 2004-01 
Journal Title
 BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 
ISSN
 0006-291X 
Issue Date
2004-01
MeSH
Actins / metabolism ; Amino Acid Sequence ; Animals ; Apolipoproteins / chemistry* ; Apoprotein(a) ; Blotting, Western ; Cell Movement ; Cells, Cultured ; Chick Embryo ; Chorion / metabolism ; Collagen / pharmacology ; DNA, Complementary / metabolism ; Dose-Response Relationship, Drug ; Drug Combinations ; Electrophoresis, Polyacrylamide Gel ; Endothelium, Vascular / cytology ; Endothelium, Vascular / pathology ; Focal Adhesion Kinase 1 ; Focal Adhesion Protein-Tyrosine Kinases ; Genetic Vectors ; Humans ; Kringles ; Laminin / pharmacology ; Lipoprotein(a) / chemistry* ; Mitogen-Activated Protein Kinase 1 / metabolism ; Mitogen-Activated Protein Kinase 3 ; Mitogen-Activated Protein Kinases / metabolism ; Molecular Sequence Data ; Neovascularization, Pathologic ; Phosphorylation ; Protein Structure, Tertiary ; Protein-Tyrosine Kinases / chemistry* ; Protein-Tyrosine Kinases / metabolism ; Proteoglycans / pharmacology ; Recombinant Proteins / metabolism ; Time Factors ; Tyrosine / metabolism ; Umbilical Veins / cytology ; Wound Healing
Abstract
Apolipoprotein(a) [apo(a)] contains the largest numbers of kringle domains identified to date. Of these, apo(a) kringle V shows significant sequence homology with plasminogen kringle 5, which is reported to be a potent angiogenesis inhibitor. To determine the effects of apo(a) kringle V on angiogenesis, it was expressed as a soluble protein (termed rhLK8) in Pichia pastoris and its in vitro and in vivo anti-angiogenic properties were examined. rhLK8 inhibited the migration of human umbilical vein endothelial cells in vitro in a dose-dependent manner. This function was associated with the down-regulation of the activation of focal adhesion kinase and the inhibition of the consequent formation of actin stress fibers/focal adhesions. rhLK8 also inhibited new capillary formation in vivo, as assessed by the chick chorioallantoic membrane assay and the Matrigel plug assay. These results indicate that rhLK8 may be an effective angiogenesis inhibitor both in vitro and in vivo.
Full Text
https://www.sciencedirect.com/science/article/pii/S0006291X03025488
DOI
10.1016/j.bbrc.2003.11.148
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Pathology (병리학교실) > 1. Journal Papers
Yonsei Authors
Hong, Soon Won(홍순원) ORCID logo https://orcid.org/0000-0002-0324-2414
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/178805
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