Accession Number : ADA300398
Title : Breast Mucin Tumor-Specific Epitopes for Cancer Immunotherapy.
Descriptive Note : Annual rept. 1 Aug 94-31 Jul 95,
Corporate Author : TEXAS TECH UNIV HEALTH SCIENCES CENTER AMARILLO
Personal Author(s) : Dombrowski, Kenneth E.
PDF Url : ADA300398
Report Date : 21 AUG 1995
Pagination or Media Count : 71
Abstract : The objectives of the research program are to study the structure-immunogenicity relationships of a hypoglycosylated human tumor-specific mucin common to breast and other adenocarcinomas, and the regulation of tumor-specific lymphoid cells that respond to the tumor-specific immunogen. Hypoglycosylation of breast mucin leads to exposure of a tumor-specific epitope (TSE). The structural and immunogenic properties of the TSE are being examined using synthetic mucin peptides and recombinant mucin proteins that contain the TSE and/or mutations in potential glycosylation sites surrounding the TSE. Protein structure and glycosylation patterns of these proteins are being examined by biochemical and physical spectroscopic techniques (i.e., 1H-NMR, mass spectrometry, and surface analytical spectroscopies). Immunogenicity is being examined by the ability of by tumor- specific antibodies and tumor-specific cytotoxic T lymphocytes to reorganize the TSE. Understanding of the structure-immunogenicity relationships of tumor-specific immunogens, as well as the regulation of the lymphoid cells responding to the immunogen, is essential for maximizing the use of synthetic peptide immunogens and tumor-specific cells as a potential adoptive immunotherapy for patients with cancer, and the development of a potential vaccine against this disease.
Descriptors : *IMMUNIZATION, *VACCINES, *CHEMOTHERAPY, *CANCER, *MAMMARY GLANDS, *IMMUNOGENS, *MUCIN, *BREAST CANCER, METHODOLOGY, SPECTROSCOPY, PHYSICAL PROPERTIES, STRUCTURAL PROPERTIES, CELLS, PEPTIDES, BIOCHEMISTRY, PROTEINS, NEOPLASMS, MUTATIONS, ANTIBODIES, MASS SPECTROMETRY, LYMPHATIC SYSTEM.
Subject Categories : Anatomy and Physiology
Distribution Statement : APPROVED FOR PUBLIC RELEASE