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Author Tan, Xian Wen| Takenaka, Fumiaki| Takekawa, Hironori| Matsuura, Eiji|
Keywords Biological sciences Antibody Biochemistry Lipid peroxidation Health sciences Oxidized LDL (oxLDL) β2-glycoprotein I (β2GPI) OxLDL-β2GPI Lateral flow immunoassay (LFIA) Enzyme-linked immunosorbent assay (ELISA) Point-of-care
Published Date 2020-06-08
Publication Title Heliyon
Volume volume6
Issue issue6
Publisher Elsevier
Start Page e04114
ISSN 2405-8440
Content Type Journal Article
language 英語
OAI-PMH Set 岡山大学
Copyright Holders © 2020 The Authors
File Version publisher
PubMed ID 32551380
DOI 10.1016/j.heliyon.2020.e04114
Related Url isVersionOf https://doi.org/10.1016/j.heliyon.2020.e04114
JaLCDOI 10.18926/AMO/53999
FullText URL 70_1_13.pdf
Author Arum Tri Wahyuningsih| Shen, Lianhua| Kobayashi, Kazuko| Sasaki, Takanori| Takenaka, Fumiaki| Hanada, Takahisa| Akehi, Masaru| Akahoshi, Akiya| Ozeki, Eiichi| Ando, Eiji| Matsuura, Eiji|
Abstract 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.
Keywords β2-glycoprotein I (β2GPI) angiogenesis vascular endothelial growth factor-A (VEGF-A) positron emission tomography (PET) imaging
Amo Type Original Article
Published Date 2016-02
Publication Title Acta Medica Okayama
Volume volume70
Issue issue1
Publisher Okayama University Medical School
Start Page 13
End Page 24
ISSN 0386-300X
NCID AA00508441
Content Type Journal Article
language 英語
Copyright Holders CopyrightⒸ 2016 by Okayama University Medical School
File Version publisher
Refereed True
PubMed ID 26899605
Web of Science KeyUT 000371288700002