Idiosyncratic antigen protein, and antigen peptide of liver cancer orchis pellet

A protein-specific technology, applied in the direction of peptide/protein components, specific peptides, peptides, etc.

Inactive Publication Date: 2007-11-14
PEKING UNIV
View PDF1 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

At the same time, the cell's intrinsic self-defense mechanism may also induce the production of antagonistic molecules

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
  • Idiosyncratic antigen protein, and antigen peptide of liver cancer orchis pellet
  • Idiosyncratic antigen protein, and antigen peptide of liver cancer orchis pellet
  • Idiosyncratic antigen protein, and antigen peptide of liver cancer orchis pellet

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0033] Example 1. Gene Analysis

[0034] TFDP-3 (HCA661) is a new gene screened from the patient's liver cancer tissue with serum by SEREX method. According to bioinformatics analysis, the TFDP-3 (HCA661) gene is located on the X chromosome of the human gene and is a gene consisting of a single exon. The size of the transcript is 1,680bp, the coding frame is 1,218bp, the start and end points are 90-1,307, and it encodes a protein of 405 amino acids (as shown in Figure 1). This protein is a new member of the DP family of transcription factors, and has a high degree of similarity (75.2% amino acid identity; 82.0% amino acid similarity) to its DP family homologue TFDP-1. The comparative analysis of the amino acid sequences of the two is shown in Figure 3. Similar to TFDP-1, the amino acid sequence of TFDP-3 includes an evolutionarily conserved DNA binding domain (AA108-AA191) and an evolutionarily conserved heterodimerization structure domain (AA192-AA264), and, in the DNA-bind...

Embodiment 2

[0035] Example 2. TFDP-3 (HCA661) mRNA Northern blot analysis

[0036] For Northem blot analysis, total RNA was extracted from HCC specimens and corresponding noncancerous tissue specimens as well as testicular tissue. RNA integrity was analyzed by electrophoresis. During electrophoresis, the loading amount of total RNA per well was 30 mg, and then transferred to the membrane. with specificity 32 The P-labeled cDNA probe was hybridized to nitrocellulose membrane overnight at 65°C. Wash three times with 0.1×SSC / 0.1% SDS solution, each time for 30 minutes, and perform autoradiography at -70°C. The size of the full-length mRNA is compared with the degree of migration of 28S and 18S ribosomal RNA.

[0037] Due to the high similarity of nucleotide sequences, the results of Northern blot hybridization (as shown in Figure 4) showed that two strong bands appeared in the RNA of the testis tissue, which were ~1.7kb and 2.1kb respectively. Only a ~1.7 kb band appeared in the RNA of ...

Embodiment 3

[0038] Example 3. Expression distribution of TFDP-3 (HCA661) in HCC and adjacent non-cancerous tissue samples

[0039] The expression profile of TFDP-3 (HCA661) mRNA was analyzed by RT-PCR, and the results are listed in Table 1. Tissues included 16 normal tissue cDNAs purchased from Clontech: brain, heart, kidney, liver, lung, pancreas, placenta, skeletal muscle, colon, ovary, peripheral blood leukocytes, prostate, small intestine, spleen, testis, and thymus, from HCC tissue The total RNA extracted from the matched adjacent non-cancerous tissue was reverse transcribed into cDNA. The TFDP-3(HCA661) fragment was amplified using specific primer pairs. Glyceraldehyde 3-phosphate dehydrogenase (G3PDH) mRNA was used as an internal reference. The primers used are as follows: TFDP-3, forward, 5'-TACACT CGG CCT GGA AGA ATT G-3'; reverse, 5'-TCT TCC TCC TCG ACT GCT G-3', size, 1,244 base pairs (bp).

[0040] Among the 16 kinds of normal tissues, only the testis detected the high leve...

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

This invention relates to hepatic cancer-testis specific anti-genetic protein and anti-genetic peptide. The anti-genetic protein has the amino acid sequence shown in SEQ ID No. 1 (from AA 108-AA 191). The anti-genetic protein and anti-genetic peptide can be used as E2F activity-blocking agent in PRB/E2F signal transduction, and have antagonistic effects on homologous analogue TEDP-1. The tumor antigen protein can decompose in cells to obtain peptide fragments, which can bind with the main histocompatibility complex (MHC)-I molecules, and be recognized by T cells. The anti-genetic protein and anti-genetic peptide can be applied in anti-tumor drugs.

Description

technical field [0001] The invention relates to a liver cancer-testis specific antigen protein and antigen peptide. Background technique [0002] Tumor-testis (cancer-testis, referred to as CT) antigen protein is the most identified class of tumor antigens, and their coding genes are characterized by expression in many types of tumors, such as melanoma, lung cancer, sarcoma and It is expressed in bladder cancer, but it is not expressed in normal tissues except testis, and it is expressed in a certain amount in placenta, ovary and pancreas. Because the testis is an immune privileged site, this type of antigen is considered to be a tumor-specific antigen in therapy, and it is the most promising type of antigen for tumor immunotherapy. At present, this type of antigen is mainly used clinically, such as MAGE-1 and NY-ESO-1, which have a high positive rate in certain types of tumors and have good immunogenicity. , has a good prospect when used in tumor immunotherapy. [0003] ...

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): C07K14/435C07K14/47C07K19/00A61K38/17A61P35/00C12N15/12
Inventor 陈慰峰乔欢庞学雯王俞田婵
Owner PEKING UNIV
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