JaLCDOI 10.18926/AMO/53999
フルテキストURL 70_1_13.pdf
著者 Arum Tri Wahyuningsih| Shen, Lianhua| Kobayashi, Kazuko| Sasaki, Takanori| Takenaka, Fumiaki| Hanada, Takahisa| Akehi, Masaru| Akahoshi, Akiya| Ozeki, Eiichi| Ando, Eiji| Matsuura, Eiji|
抄録 Intact β2-glycoprotein I (iβ2GPI) is a glycoprotein that regulates coagulation and fibrinolysis. Nicked β2GPI (nβ2GPI) possesses an angiogenic property at a relatively low concentration, and an antiangiogenic property at a high concentration. Here we investigated the functions of βi 2GPI and nβ2GPI in vascular endothelial growth factor (VEGF)-A-induced endothelial cell proliferation and tube formation. We used noninvasive PET imaging to analyze the in vivo distribution of intravenously injected β2GPI variants in tumor lesions in mice. iβ2GPI was incubated with plasmin to obtain nβ2GPI, and its N-terminal sequence was analyzed. nβ2GPI had at least one other cleavage site upstream of the β2GPIʼs domain V, whereas the former plasmin-cleavage site locates between K317 and T318. Both of intact and nicked β2GPI significantly inhibited the VEGF-A-induced cell proliferation and the tube formation of human umbilical vein endothelial cells (HUVECs). PET imaging visualized considerably distributed intensities of all tested β2GPI variants in tumor lesions of pancreatic tumor cell-xenografts. These results indicate that β2GPI may be physiologically and pathophysiologically important in the regulation of not only coagulation and fibrinolysis, but also angiogenesis.
キーワード β2-glycoprotein I (β2GPI) angiogenesis vascular endothelial growth factor-A (VEGF-A) positron emission tomography (PET) imaging
Amo Type Original Article
発行日 2016-02
出版物タイトル Acta Medica Okayama
出版者 Okayama University Medical School
開始ページ 13
終了ページ 24
ISSN 0386-300X
NCID AA00508441
資料タイプ 学術雑誌論文
言語 English
著作権者 CopyrightⒸ 2016 by Okayama University Medical School
論文のバージョン publisher
査読 有り
PubMed ID 26899605
Web of Science KeyUT 000371288700002