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

Abstract

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.

Authors:
 [1];  [1];  [2];  [1];  [3];  [4]
  1. Department of Biochemistry, Chungbuk National University, Cheongju 361-763 (Korea, Republic of)
  2. (Korea, Republic of)
  3. School of Science Education, Chungbuk National University, Cheongju 361-763 (Korea, Republic of)
  4. 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). E-mail: sichang@cbnu.ac.kr
Publication Date:
OSTI Identifier:
20857958
Resource Type:
Journal Article
Resource Relation:
Journal Name: Biochemical and Biophysical Research Communications; Journal Volume: 352; Journal Issue: 2; Other Information: DOI: 10.1016/j.bbrc.2006.11.047; PII: S0006-291X(06)02519-8; Copyright (c) 2006 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; CALCIUM; CATTLE; DNA; EMBRYOS; FETAL MEMBRANES; IN VITRO; IN VIVO; MAGNESIUM; PH VALUE; PHOSPHATES; PHOSPHORYLATION; PROTEINS; TRANSLOCATION; VEINS

Citation Formats

Kim, Hye-Mi, Kang, Dong-Ku, Protein Chip Center, Biotechnology Research Institute, Chungbuk National University, Cheongju 361-763, Kim, Hak Yong, Kang, Sang Sun, and Chang, Soo-Ik. Angiogenin-induced protein kinase B/Akt activation is necessary for angiogenesis but is independent of nuclear translocation of angiogenin in HUVE cells. United States: N. p., 2007. Web. doi:10.1016/j.bbrc.2006.11.047.
Kim, Hye-Mi, Kang, Dong-Ku, Protein Chip Center, Biotechnology Research Institute, Chungbuk National University, Cheongju 361-763, Kim, Hak Yong, Kang, Sang Sun, & Chang, Soo-Ik. Angiogenin-induced protein kinase B/Akt activation is necessary for angiogenesis but is independent of nuclear translocation of angiogenin in HUVE cells. United States. doi:10.1016/j.bbrc.2006.11.047.
Kim, Hye-Mi, Kang, Dong-Ku, Protein Chip Center, Biotechnology Research Institute, Chungbuk National University, Cheongju 361-763, Kim, Hak Yong, Kang, Sang Sun, and Chang, Soo-Ik. Fri . "Angiogenin-induced protein kinase B/Akt activation is necessary for angiogenesis but is independent of nuclear translocation of angiogenin in HUVE cells". United States. doi:10.1016/j.bbrc.2006.11.047.
@article{osti_20857958,
title = {Angiogenin-induced protein kinase B/Akt activation is necessary for angiogenesis but is independent of nuclear translocation of angiogenin in HUVE cells},
author = {Kim, Hye-Mi and Kang, Dong-Ku and Protein Chip Center, Biotechnology Research Institute, Chungbuk National University, Cheongju 361-763 and Kim, Hak Yong and Kang, Sang Sun and Chang, Soo-Ik},
abstractNote = {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.},
doi = {10.1016/j.bbrc.2006.11.047},
journal = {Biochemical and Biophysical Research Communications},
number = 2,
volume = 352,
place = {United States},
year = {Fri Jan 12 00:00:00 EST 2007},
month = {Fri Jan 12 00:00:00 EST 2007}
}
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