Recombinant domain v of β2-glycoprotein i inhibits the formation of a 7-ketocholesteryl-9-carboxynonanoate and β2- glycoprotein i complex

Yingbiao Zhang; Wenzhe Li; Yan Chi; Renjun Wang; Dan Wang; Fan Zhang; Zhe Liu; Eiji Matsuura; Qingping Liu

doi:10.1093/jb/mvq111

Recombinant domain v of β₂-glycoprotein i inhibits the formation of a 7-ketocholesteryl-9-carboxynonanoate and β₂- glycoprotein i complex

Yingbiao Zhang, Wenzhe Li, Yan Chi, Renjun Wang, Dan Wang, Fan Zhang, Zhe Liu, Eiji Matsuura, Qingping Liu

Research output: Contribution to journal › Article › peer-review

4 Citations (Scopus)

Abstract

Our prior study has been reported the formation of the oxidized low-density lipoprotein (oxLDL)/β2-glycoproteinI (β2-GPI)/autoantibody complex facilitated the antiphospholipid syndrome (APS) process. The domain V of β2-GPI binds to the negatively charged molecules, e.g. 7-ketochoresteryl-9- caboxynonanoate (oxLig-1) derived from the oxLDL and mediates the interaction between oxLDL and β2-GPI. In the present study, the oxLig-1/β2-GPI/ anti-β2-GPI Ab (WB-CAL-1) model was established. The recombinant domain V of β2-GPI (rβ2-GPI DV) expressed in Escherichia coli competitively inhibits the interaction between β2-GPI and oxLig-1 in the enzyme-linked immunoassay. Moreover, the rβ2-GPI DV significantly inhibits the formation of the oxLig-1/β2-GPI/autoantibody complex in an APS patient. The present work suggests a novel possibility that rβ2-GPI DV could be used to inhibit the formation of oxLDL/β2-GPI/autoantibody complex, and give us a hint for the development of new therapeutic strategies to prevent the APS process.

Original language	English
Pages (from-to)	35-42
Number of pages	8
Journal	Journal of biochemistry
Volume	149
Issue number	1
DOIs	https://doi.org/10.1093/jb/mvq111
Publication status	Published - Jan 2011

Keywords

Antiphospholipid syndrome
oxLDL
oxLig-1
β
β domain V

ASJC Scopus subject areas

Biochemistry
Molecular Biology

Access to Document

10.1093/jb/mvq111

Cite this

Recombinant domain v of β₂-glycoprotein i inhibits the formation of a 7-ketocholesteryl-9-carboxynonanoate and β₂- glycoprotein i complex. / Zhang, Yingbiao; Li, Wenzhe; Chi, Yan; Wang, Renjun; Wang, Dan; Zhang, Fan; Liu, Zhe; Matsuura, Eiji; Liu, Qingping.

In: Journal of biochemistry, Vol. 149, No. 1, 01.2011, p. 35-42.

Research output: Contribution to journal › Article › peer-review

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title = "Recombinant domain v of β2-glycoprotein i inhibits the formation of a 7-ketocholesteryl-9-carboxynonanoate and β2- glycoprotein i complex",

abstract = "Our prior study has been reported the formation of the oxidized low-density lipoprotein (oxLDL)/β2-glycoproteinI (β2-GPI)/autoantibody complex facilitated the antiphospholipid syndrome (APS) process. The domain V of β2-GPI binds to the negatively charged molecules, e.g. 7-ketochoresteryl-9- caboxynonanoate (oxLig-1) derived from the oxLDL and mediates the interaction between oxLDL and β2-GPI. In the present study, the oxLig-1/β2-GPI/ anti-β2-GPI Ab (WB-CAL-1) model was established. The recombinant domain V of β2-GPI (rβ2-GPI DV) expressed in Escherichia coli competitively inhibits the interaction between β2-GPI and oxLig-1 in the enzyme-linked immunoassay. Moreover, the rβ2-GPI DV significantly inhibits the formation of the oxLig-1/β2-GPI/autoantibody complex in an APS patient. The present work suggests a novel possibility that rβ2-GPI DV could be used to inhibit the formation of oxLDL/β2-GPI/autoantibody complex, and give us a hint for the development of new therapeutic strategies to prevent the APS process.",

keywords = "Antiphospholipid syndrome, oxLDL, oxLig-1, β, β domain V",

author = "Yingbiao Zhang and Wenzhe Li and Yan Chi and Renjun Wang and Dan Wang and Fan Zhang and Zhe Liu and Eiji Matsuura and Qingping Liu",

note = "Funding Information: National Nature Science Fundation of China (No: 30371380, and No: 30571733).",

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AU - Zhang, Yingbiao

AU - Li, Wenzhe

AU - Chi, Yan

AU - Wang, Renjun

AU - Wang, Dan

AU - Zhang, Fan

AU - Liu, Zhe

AU - Matsuura, Eiji

AU - Liu, Qingping

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AB - Our prior study has been reported the formation of the oxidized low-density lipoprotein (oxLDL)/β2-glycoproteinI (β2-GPI)/autoantibody complex facilitated the antiphospholipid syndrome (APS) process. The domain V of β2-GPI binds to the negatively charged molecules, e.g. 7-ketochoresteryl-9- caboxynonanoate (oxLig-1) derived from the oxLDL and mediates the interaction between oxLDL and β2-GPI. In the present study, the oxLig-1/β2-GPI/ anti-β2-GPI Ab (WB-CAL-1) model was established. The recombinant domain V of β2-GPI (rβ2-GPI DV) expressed in Escherichia coli competitively inhibits the interaction between β2-GPI and oxLig-1 in the enzyme-linked immunoassay. Moreover, the rβ2-GPI DV significantly inhibits the formation of the oxLig-1/β2-GPI/autoantibody complex in an APS patient. The present work suggests a novel possibility that rβ2-GPI DV could be used to inhibit the formation of oxLDL/β2-GPI/autoantibody complex, and give us a hint for the development of new therapeutic strategies to prevent the APS process.

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