Pharmaceutical composition for treatment and/or prevention of cancer

A composition and drug technology, applied in the direction of drug combination, medical preparations containing active ingredients, antitumor drugs, etc.

Active Publication Date: 2012-12-12
TORAY IND INC
View PDF14 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 treatment and/or prevention of cancer
  • Pharmaceutical composition for treatment and/or prevention of cancer
  • Pharmaceutical composition for treatment and/or prevention of cancer

Examples

Experimental program
Comparison scheme
Effect test

preparation example Construction

[0046] The preparation of the antigen, the preparation of the antibody, and the pharmaceutical composition related to the present invention will be described below.

[0047]

[0048] 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.

[0049] 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

[0180] Example 1 Identification of a new cancer antigen protein using the SEREX method

[0181] (1) Preparation of cDNA library

[0182] Total RNA was extracted from the testis tissue of healthy dogs by the Acid guanidium-Phenol-Chloroform method (Acid guanidium-Phenol-Chloroform method), and using the Oligotex-dT30 mRNA purification kit (manufactured by Takara Shuzo Co., Ltd.), the polymer was purified according to the instructions attached to the kit. ARNA.

[0183] 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.

[0184] (2) Screening of cDNA library using serum

[0185] The dog testis cDNA phage library prepared above was used for i...

Embodiment 2

[0213] Example 2 Preparation of Human CAPRIN-1

[0214] (1) Preparation of recombinant protein

[0215] 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 described) each 0.4 μM, 0.2 mM dNTP, 1.25 U PrimeSTAR HS polymerase (manufactured by Takara Shuzo Co., Ltd.)) were added to make the total amount of 50 μl of each reagent and accompanying buffer solution, and 98 The cycle of °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 amino acid sequence of SEQ ID NO: 2. After PCR, the amplified DNA wa...

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 which is expressed specifically on the surface of a cancer cell, and provides a use of an antibody, which targets the cancer antigen protein, as a therapeutic and/or prophylactic agent for cancer. Specifically disclosed is a pharmaceutical composition for the treatment and/or prevention of cancer, which is characterized by containing, as an active ingredient, an antibody that is immunologically reactive with a partial polypeptide of CAPRIN-1 represented by the even-numbered sequences of SEQ ID NOS: 2-30, said partial polypeptide comprising the amino acid sequence represented by SEQ ID NO: 37 or an amino acid sequence having 80% or more sequence identity to the amino acid sequence, or a fragment of the antibody.

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 Applications(China)
IPC IPC(8): A61K39/395A61P35/00A61P35/02C07K16/30
CPCC07K16/28C07K2317/732A61K2039/505C07K16/30A61P35/00A61P35/02C07K2317/34A61K39/39558
Inventor 小林真一冈野文义斋藤孝则
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

Browse by: Latest US Patents, China's latest patents, Technical Efficacy Thesaurus, Application Domain, Technology Topic.

© 2024 PatSnap. All rights reserved.Legal|Privacy policy|Modern Slavery Act Transparency Statement|Sitemap