Al technical title is built by PatSnap Al team. It summarizes the technical point description of the patent document.
An amino acid, selected from the technology, applied in the field of cancer treatment, bioscience
Active Publication Date: 2014-04-16
ONCOTHERAPY SCI INC
View PDF29 Cites 7 Cited by
Summary
Abstract
Description
Claims
Application Information
AI Technical Summary
This helps you quickly interpret patents by identifying the three key elements:
Problems solved by technology
Method used
Benefits of technology
Problems solved by technology
However, previous studies failed to confirm whether these peptide fragments have the ability to induce CTL targeting tumor cells expressing MPHOSPH1 gene and HLA-A2 antigen
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
Click on the blue label to locate the original text in one second.
Reading with bidirectional positioning of images and text.
Smart Image
Examples
Experimental program
Comparison scheme
Effect test
Embodiment
[0444] Materials and methods
[0445] cell line
[0446] T2, HLA-A*0201-positive B-lymphoblastoid cell line, HLA-A*0206-positive B-lymphoblastoid cell line, HT1376, J82, COS7 and UM-UC3 were purchased from ATCC. MKN-45 was purchased from JCRB.
[0447] Candidate selection for peptides derived from MPHOSPH1
[0448] Using the binding prediction software "BIMAS" (http: / / www-bimas.cit.nih.gov / molbio / hla_bind) (Parker et al., J Immunol 1994,152(1):163-75; Kuzushima et al., Blood 2001, 98(6):1872-81) predicted 9- and 10-mer peptides derived from MPHOSPH1 (GenBank Accession No: EAW63006 (SEQ ID NO: 40)) that bind the HLA-A*0201 molecule. These peptides were synthesized by BioSynthesis (Lewisville, Texas) according to standard solid phase synthesis and purified by reverse phase high performance liquid chromatography (HPLC). The purity (>90%) and identity of the peptides were determined by analytical HPLC and mass spectrometry, respectively. Peptides were dissolved in dimet...
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
Login to view more
Abstract
As discussed in greater detail herein, isolated epitope peptides derived from MPHOSPH1 bind to an HLA antigen and induce cytotoxic T lymphocytes (CTL) and thus are suitable for use in the context of cancer immunotherapy, more particularly cancer vaccines. The inventive peptides encompass both the above-mentioned MPHOSPH1-derived amino acid sequences and modified versions thereof, in which one, two, or several amino acids are substituted, deleted, inserted or added, provided such modified versions retain the requisite CTL inducibility of the original sequences. Further provided are polynucleotides encoding any of the aforementioned peptides as well as pharmaceutical agents or compositions that include any of the aforementioned peptides or polynucleotides. The peptides, polynucleotides, and pharmaceutical agents or compositions of this invention find particular utility in either or both of the treatment and prevention of cancers and tumors, including, for example, bladder cancer, breast cancer, cervical cancer, cholangiocellular carcinoma, CML, colorectal cancer, gastric cancer, NSCLC, lymphoma, osteosarcoma, prostate cancer, renal cancer and soft tissue tumor.
Description
technical field [0001] The present invention relates to the field of biological sciences, more specifically to the field of cancer treatment. Specifically, the present invention relates to novel peptides useful as cancer vaccines, and drugs for treating and / or preventing tumors. [0002] priority [0003] This application claims the benefit of US Provisional Application 61 / 522,991, filed August 12, 2011, which is hereby incorporated by reference in its entirety. Background technique [0004] It has been demonstrated that cytotoxic T lymphocytes (CTLs) can recognize epitope peptides derived from tumor-associated antigens (TAAs) appearing on major histocompatibility complex (MHC) class I molecules, and then kill tumor cells. Since the discovery of the melanoma antigen (MAGE) family, many other TAAs have been discovered mainly by immunological means (NPL1, Boon T, Int J Cancer 1993 May 8,54(2):177-80; NPL2, Boon T & van der Bruggen P, J Exp Med 1996 Mar 1, 183(3):725-9). So...
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
Application Date:The date an application was filed.
Publication Date:The date a patent or application was officially published.
First Publication Date:The earliest publication date of a patent with the same application number.
Issue Date:Publication date of the patent grant document.
PCT Entry Date:The Entry date of PCT National Phase.
Estimated Expiry Date:The statutory expiry date of a patent right according to the Patent Law, and it is the longest term of protection that the patent right can achieve without the termination of the patent right due to other reasons(Term extension factor has been taken into account ).
Invalid Date:Actual expiry date is based on effective date or publication date of legal transaction data of invalid patent.