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Angiogenin-induced protein kinase B/Akt activation is necessary for angiogenesis but is independent of nuclear translocation of angiogenin in HUVE cells

Journal Article · · Biochemical and Biophysical Research Communications
 [1];  [1];  [1];  [2];  [3]
  1. Department of Biochemistry, Chungbuk National University, Cheongju 361-763 (Korea, Republic of)
  2. School of Science Education, Chungbuk National University, Cheongju 361-763 (Korea, Republic of)
  3. Department of Biochemistry, Chungbuk National University, Cheongju 361-763 (Korea, Republic of) and Protein Chip Center, Biotechnology Research Institute, Chungbuk National University, Cheongju 361-763 (Korea, Republic of)
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Angiogenin, a potent angiogenic factor, binds to endothelial cells and is endocytosed and rapidly translocated to and concentrated in the nucleolus where it binds to DNA. In this study, we report that angiogenin induces transient phosphorylation of protein kinase B/Akt in cultured human umbilical vein endothelial (HUVE) cells. LY294002 inhibits the angiogenin-induced protein kinase B/Akt activation and also angiogenin-induced cell migration in vitro as well as angiogenesis in chick embryo chorioallantoic membrane in vivo without affecting nuclear translocation of angiogenin in HUVE cells. These results suggest that cross-talk between angiogenin and protein kinase B/Akt signaling pathways is essential for angiogenin-induced angiogenesis in vitro and in vivo, and that angiogenin-induced PKB/Akt activation is independent of nuclear translocation of angiogenin in HUVE cells.
OSTI ID:
20857958
Journal Information:
Biochemical and Biophysical Research Communications, Journal Name: Biochemical and Biophysical Research Communications Journal Issue: 2 Vol. 352; ISSN 0006-291X; ISSN BBRCA9
Country of Publication:
United States
Language:
English

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Related Subjects

60 APPLIED LIFE SCIENCES
CALCIUM
CATTLE
DNA
EMBRYOS
FETAL MEMBRANES
IN VITRO
IN VIVO
MAGNESIUM
PH VALUE
PHOSPHATES
PHOSPHORYLATION
PROTEINS
TRANSLOCATION
VEINS