Pharmaceutical composition for cancer treatment and/or prevention

A sequence numbering and antibody technology, applied in drug combinations, medical preparations containing active ingredients, anti-tumor drugs, etc.

Active Publication Date: 2016-11-16
TORAY IND INC
View PDF16 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0006] In addition, based on the report of Non-Patent Document 10, which considers CAPRIN-1 to be a cell membrane protein, Patent Documents 2 and 3 describe that CAPRIN-1, as a cell membrane protein, can be used as a target of antibody drugs for cancer treatment under the name of M11S1 ( In the examples, there is no description about the treatment using the antibody against this protein at all)

Method used

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
View more

Image

Smart Image Click on the blue labels to locate them in the text.
Viewing Examples
Smart Image
  • Pharmaceutical composition for cancer treatment and/or prevention
  • Pharmaceutical composition for cancer treatment and/or prevention
  • Pharmaceutical composition for cancer treatment and/or prevention

Examples

Experimental program
Comparison scheme
Effect test

preparation example Construction

[0056] The preparation of the antigen, the preparation of the antibody, and the pharmaceutical composition related to the present invention will be described below.

[0057]

[0058] The protein or its fragment used as a sensitizing antigen for obtaining the antibody against CAPRIN-1 used in the present invention can be derived from humans, dogs, cows, horses, mice, rats, chickens, etc. The types of animals are not limited. However, the protein or fragment thereof is preferably selected in consideration of suitability for mother cells used in cell fusion, and generally, mammalian-derived proteins are preferred, and human-derived proteins are particularly preferred. For example, when CAPRIN-1 is human CAPRIN-1, human CAPRIN-1 protein and / or partial peptides thereof, cells expressing human CAPRIN-1, etc. can be used.

[0059] The base sequence and amino acid sequence of human CAPRIN-1 and its homologues can be obtained, for example, by accessing GenBank (US NCBI), using algor...

Embodiment 1

[0196] Example 1 Identification of a new cancer antigen protein using the SEREX method

[0197] (1) Preparation of cDNA library

[0198] Total RNA was extracted from testicular tissues of healthy dogs by the Acid guanidium-Phenol-Chloroform method (Acid guanidium-Phenol-Chloroform method), and purified using the Oligotex-dT30 mRNA Purification Kit (manufactured by Takara Shuzo Co., Ltd.) according to the instructions attached to the kit. Poly A RNA.

[0199] The thus obtained mRNA (5 µg) was used to synthesize a dog testis cDNA phage library. The cDNA phage library was prepared using cDNA Synthesis Kit, ZAP-cDNA Synthesis Kit, and ZAP-cDNA GigapackIII Gold Cloning Kit (manufactured by STRATAGENE), and the library was prepared according to the instructions attached to the kit. The size of the cDNA phage library produced was 7.73×10 5 pfu / ml.

[0200] (2) Screening of cDNA library using serum

[0201] The dog testis cDNA phage library prepared above was used for immune scre...

Embodiment 2

[0223] The preparation of the new human cancer antigen protein of embodiment 2

[0224] (1) Preparation of recombinant protein

[0225] Based on the gene of sequence number 1 obtained in Example 1, the recombinant protein of the human homologous gene was prepared by the following method. PCR was carried out as follows: 1 μl of cDNA whose expression could be confirmed by RT-PCR using the cDNA of various tissues and cells produced in Example 1, two primers (SEQ ID Nos. 38 and 39) containing SacI and XhoI restriction enzyme cleavage sequences 0.4 μM each, 0.2 mM dNTP, 1.25 U PrimeSTAR HS polymerase (manufactured by Takara Shuzo Co., Ltd.)), each reagent and accompanying buffer were added to make the total amount 50 μl, and a Thermal Cycler (manufactured by BIO RAD Co., Ltd.) was used. The cycle of 98°C-10 seconds, 68°C-2.5 minutes was repeated 30 times. In addition, the above-mentioned two types of primers are primers for amplifying the region encoding the entire length of the ...

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to view more

PUM

No PUM Login to view more

Abstract

The present invention identifies a cancer antigen protein specifically expressed on the surface of cancer cells, and uses an antibody targeting the cancer antigen protein as a therapeutic and / or preventive agent for cancer. Specifically, the present invention provides a drug for cancer A pharmaceutical composition for treatment and / or prevention, characterized in that it contains as an active ingredient an antibody or fragment thereof that is immunoreactive with a partial polypeptide of CAPRIN‑1 represented by an even-numbered sequence number in sequence numbers 2 to 30, said The partial polypeptide of CAPRIN-1 has the amino acid sequence shown in SEQ ID NO: 37, or an amino acid sequence having 80% or more sequence identity with the amino acid sequence.

Description

technical field [0001] The present invention relates to novel medical uses of antibodies against CAPRIN-1 or fragments thereof as therapeutic and / or preventive agents for cancer. Background technique [0002] Cancer is the number one cause of death among all diseases, and the current treatment is mainly surgery, combined with radiotherapy and chemotherapy. Despite the development of new surgical methods and the discovery of new anticancer drugs in recent years, the status quo is that except for some cancers, the results of cancer treatment have not improved much. In recent years, with the advancement of molecular biology and cancer immunology, antibodies specific to cancer, cancer antigens recognized by cytotoxic T cells, and genes encoding cancer antigens have been identified. The expectation of a target-specific cancer treatment method is increasing (Non-Patent Document 1). [0003] In cancer therapy methods, in order to reduce side effects, it is desirable that a peptid...

Claims

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to view more

Application Information

Patent Timeline
no application Login to view more
Patent Type & Authority Patents(China)
IPC IPC(8): A61K39/395A61P35/00A61P35/02C07K16/30
CPCA61K2039/505A61P35/00A61P35/02C07K16/3015C07K16/3053C07K2317/34A61K39/39558C07K16/30
Inventor 冈野文义斋藤孝则小林真一井户隆喜成田义规
Owner TORAY IND INC
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Try Eureka
PatSnap group products