Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0699790 (colon cancer)
28,837 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The screening of cDNA expression libraries derived from human tumors with autologous antibody (SEREX) has proven to be a powerful method for defining the structure of tumor antigens recognized by the humoral immune system. In the present study, 48 distinct antigens (NY-CO-1-NY-CO-48) reactive with autologous IgG were identified by SEREX analysis in 4 patients with colon cancer. Sequencing analysis showed that 17 of the cDNA clones were previously uncharacterized molecules and 31 represented known gene products. The individual cDNA clones were analyzed in the following manner: a search for mutations or other structural changes; an analysis of mRNA expression in a panel of normal tissues; and a frequency analysis of the antibody response to the expressed product in the sera of colon cancer patients and normal individuals. The initial analysis showed NY-CO-13 to be a mutated version of the p53 tumor suppressor gene. Three of the 48 antigens showed a differential pattern of mRNA expression, with NY-CO-27 (galectin-4) expressed primarily in gastrointestinal tract, and NY-CO-37 and -38 showing a pattern of tissue-specific isoforms. With regard to immunogenicity, 20 of the 48 antigens were detected by allogeneic sera; 14 of these were reactive with sera from both normal donors and cancer patients, and 6 other clones (NY-CO-8, -9, -13, -16, -20 and -38) reacted exclusively with sera from colon cancer patients (ranging from 14% to 27%). Our results on colon cancer illustrate both the complexity and the potential of the SEREX approach for analysis of the humoral immune response against human cancer.
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PMID:Characterization of human colon cancer antigens recognized by autologous antibodies. 961 Jul 21

We have cloned and characterized the cDNA, expression pattern, and subcellular localization of the human and murine orthologs of the centrosomal colon cancer autoantigen protein (CCCAP). We identified both the transcriptional start site of murine CCCAP (mCCCAP) and its TATA-less promoter within BAC genomic clones of the mCCCAP 5' region. The mCCCAP transcript is ubiquitously present in mouse tissues, but at very low copy number. The 2151 bp open reading frame of mCCCAP encodes an 83 kDa protein that possesses a large C-terminal coiled-coil domain, which is able to homo-oligomerize in the yeast 2-hybrid system. Endogenous mCCCAP localizes to the centrosomes of murine BALB/c 3T3 fibroblasts during both interphase and mitosis. This centrosomal localization was not disrupted by nocodazole-induced depolymerization of the microtubule cytoskeleton, suggesting that mCCCAP is an integral component of the centrosome rather than simply a microtubule-associated protein. We also cloned human CCCAP (hCCCAP). The 2139 bp open reading frame of hCCCAP encodes an 82.5 kDa protein that is 71% identical to mCCCAP at the amino acid level and has the same predicted secondary structure. Ectopically expressed full-length hCCCAP in human U2-osteosarcoma cells also displayed centrosomal localization during interphase and mitosis. This pattern of localization was abolished by truncations of the N- and C-terminus of the protein. We further discovered that the C-terminal portion of hCCCAP is identical to the human colon cancer autoantigen NY-CO-8 (Human Gene Nomenclature symbol SDCCAG8).
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PMID:Identification and characterization of the novel centrosome-associated protein CCCAP. 1255 64