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Mutated amyloid protein

A technology for amyloid and protein, applied to peptide/protein components, anti-animal/human immunoglobulins, genetic material components, etc., can solve problems such as weakened side effects and undetermined improvement methods

Inactive Publication Date: 2007-10-10
森启
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

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Problems solved by technology

As for the side effects of vaccine therapy, although it has been pointed out that there are amyloid antigenic sites that use the amino terminal side of Aβ4-10 as an antigen, making the induced antibody IgG2b type isotype, and passing oral administration through the intestinal tract Possibility of reducing side effects by methods such as immunization, but it has not been determined as an improvement method

Method used

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Examples

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Effect test

Embodiment 1

[0106] Determination of base sequence of deletion variant APP

[0107] Genomic DNA was extracted from the blood of patients with familial Alzheimer's disease, and using the obtained DNA as a template, based on the currently known disease-causing genes Presenile Gene 1 (PSEN1), Presenile Gene 2 (PSEN2) and APP, the encoding After the full base sequence of the cDNA was amplified by PCR, it was analyzed by ABI company PRISM 310 sequencer (Perkin-Elmer, CA). As a result, a mutation of one site (deletion of 3 bases gaa at positions 1852-1854 of SEQ ID NO: 1) was found in the amyloid protein coding region (SEQ ID NO: 1) of the wild-type APP gene cDNA.

Embodiment 2

[0109] Determination of the Structure of Amyloid Protein Synthesized from Deletion Mutant APP Gene cDNA

[0110] The mutated APP gene cDNA obtained in Example 1 was studied with the cleavage site of β-protein secretase or γ-protein secretase because of the variation in the amyloid protein. Then, APP is expressed, and the expression vector of mutated APP gene cDNA is introduced into human cultured HEK cells known to produce and secrete amyloid protein. After 2 days of expression, the culture supernatant was obtained, and the fraction immunoprecipitated with an anti-amyloid antibody was analyzed in Shimadzu AXIMA-CFR. The results are shown in Figure 1.

[0111] As shown in FIG. 1 , the experimentally observed value of the molecular weight of Aβ1-40 (ΔE), which is the amyloid protein secreted by the mutated APP gene cDNA expressed in human cultured HEK cells, was 4200.51. This is roughly consistent with the theoretically calculated molecular weight of 4200.69 for the Glu that l...

Embodiment 3

[0113] Quantification of amyloid protein synthesized from deletion variant APP

[0114] It was proved that the deletion mutant APP expressed in human cultured HEK cells produced and secreted two kinds of mutant amyloid proteins roughly the same as wild-type APP as shown in Table 1.

[0115] Aβ42 (pg / ml)

[0116] It should be noted that the control in Table 1 refers to the use of an empty expression vector dissolved in physiological saline. In addition, Aβ42 represents Aβ1-42 and Aβ1-43 or Aβ1-42(ΔE) and Aβ1-43(ΔE), and Aβ40 represents Aβ1-40 or Aβ1-40(ΔE).

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Abstract

It is intended to provide a novel amyloid protein (human variant amyloid protein) useful as an antigen molecule or the like for improving a vaccine therapy. This human variant amyloid protein is a protein with deletion of Glu at 22nd, Ala at 21st, or Asp at 23rd in a normal (wildtype) amyloid protein (A1-40. A1-42, or A1-43) consisting of 40, 42, or 43 amino acids.

Description

technical field [0001] The present invention relates to a variant amyloid protein present in a patient with familial Alzheimer's disease and its utilization. Background technique [0002] Amyloid is a tissue lesion that occurs not only in Alzheimer's disease, Down's disease (congenital dementia), but also in normal aging brain tissue. The amyloid protein is composed of 40 to 42 / 43 amino acids rich in hydrophobic amino acids, and is produced by hydrolytic cleavage of the amyloid precursor protein (amyloid precursor protein, hereinafter referred to as "APP") as its precursor of. APP is a transmembrane type 1 membrane protein composed of 695, 751 or 770 amino acids, and its amino acid terminal is outside the cell. The difference in the number of amino acids determines the presence or absence of active sites of protease inhibitors called Kunitz-type located on the outside of the cell. [0003] In nerve cells, APP composed of 695 amino acids (hereinafter referred to as "APP695...

Claims

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Application Information

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Patent Type & Authority Applications(China)
IPC IPC(8): C12N15/09A01K67/027A61K31/7088C12N5/10A61K39/395A61K45/00A61K48/00A61P25/28A61P43/00C07K7/06C07K7/08C07K14/47C07K16/18A61K38/00C12Q1/02G01N33/15G01N33/50G01N33/68C12N5/07C12N5/071
CPCC07K16/18A61K31/7088A61K38/00A61K39/0007C07K14/4711G01N33/6896A61P25/08A61P25/28A61P43/00C07K7/06C12N15/09C07K7/08A61K39/395
Inventor 森启富山贵美岛田裕之
Owner 森启
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