Application of natural type, breaking type or No. 5 domain delation variant type beta 2 glycoprotein I in preparing medicine for inhibiting blood vessel newborn

A technology of angiogenesis and deletion mutation, applied in drug combination, glycopeptide components, metabolic diseases, etc., can solve problems such as high cost, variable inhibition degree, complicated operation, etc.

Inactive Publication Date: 2008-03-19
于德民 +1
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  • Abstract
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  • Application Information

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Problems solved by technology

In addition, it has been found that chimeric proteins of VEGF receptors and anti-VEGF monoclonal antibodies can inhibit the formation of intraocular neovascularization, but there are problems such as complicated operation, high cost, and varying degree of inhibition

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  • Application of natural type, breaking type or No. 5 domain delation variant type beta 2 glycoprotein I in preparing medicine for inhibiting blood vessel newborn
  • Application of natural type, breaking type or No. 5 domain delation variant type beta 2 glycoprotein I in preparing medicine for inhibiting blood vessel newborn
  • Application of natural type, breaking type or No. 5 domain delation variant type beta 2 glycoprotein I in preparing medicine for inhibiting blood vessel newborn

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Embodiment 1

[0039] Materials and Methods

[0040] Reagent

[0041] For the amino acid sequences of native β2 glycoprotein I, V domain-deleted mutant β2 glycoprotein I (DI-IV) and I domain-deleted mutant β2 glycoprotein I (DII-V), see http: / / www.ncbi .nlm.nih.gov / entrez / viewer.fcgi? db=protein&id=28814 with serial number CAA40977.

[0042] Split β2 glycoprotein I (cβ 2 GPI) sequence see Hunt JE, Simpson RJ, Krilis SA. Identification of a region of beta2-glycoprotein I critical for lipid binding and anti-cardiolipin antibody cofactoractivity. Proc Natl Acad Sci U S A. 1993 Mar 15; 90 (6): 2141-5.

[0043] Plasma-derived native β2GPI (nβ 2 GPI) was purchased from Haematologic Technologies Inc (Essex Junction, VT).

[0044] Several preparation methods of β2 glycoprotein I:

[0045] (1) Expression and purification of V domain-deleted mutant β2 glycoprotein I (DI-IV) and I domain-deleted mutant β2 glycoprotein I (DII-V):

[0046] 1. Construction of a baculovirus vector containing a targe...

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Abstract

The invention discloses the application of a beta-2-glucoprotein-I of the natural type, the cracking type or the V structure domain deletion mutant type in preparing for a novel drug of restraining the angiogenesis. The test testifies that the natural type beta-2-glucoprotein-I (n beta2GPI), the cracking type beta-2-glucoprotein-I (c beta2GPI) and the V structure domain deletion mutant type beta-2-glucoprotein-I (DI-IV) can restrain the angiogenesis of the endothelial cell. The functional mechanism of the invention is that the invention influences the expression and photophosphorylation of an accepter of an endothelial cell growth factor to retain the signal conducting path of the accepter and retain the lower fifty genetic expressions and further retain the multiplication, the migration and the angiogenesis of the endothelial cell. The invention can provide novel preventing and remedying measures for clinical treatment of the diseases of the angiogenesis, such as the multiplication type retina lesion of the diabetes etc.

Description

technical field [0001] The present invention relates to the use of β2 glycoprotein I, in particular to the use of β2 glycoprotein I in the preparation of drugs for inhibiting angiogenesis. Background technique [0002] β2 glycoprotein I (β 2 GPI) is a plasma protein rich in phospholipid binding sites (rich in human plasma), consisting of 326 amino acids, including 5 short homologous repeat sequences and 4 N-linked glycosylation sites, forming A fishhook-like three-dimensional structure. beta 2 The first four domains of GPI are similar in structure, while the fifth domain contains a conserved positive charge region Cys 281 -Cys 288 , which is the main site of phospholipid binding. beta 2 GPI in Domain V Lys 317 -Thr 318 The hydrophobic ring between them can be proteolyzed by plasmin and FXIa, which can block the binding to negative phospholipids and inhibit the β 2 Inhibitory effect of GPI on FXI activation. Studies have shown that most antiphospholipid antibodies a...

Claims

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Application Information

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Patent Type & Authority Applications(China)
IPC IPC(8): A61K38/14A61P3/10A61P27/02
Inventor 于德民于珮齐建成陈莉明卫丽君张景云
Owner 于德民
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