Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0027819 (neuroblastoma)
 27,800 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A rare case of adult neuroblastoma is presented. A 20-year-old woman complaining of fever and left abdominal tumor was admitted on July 14, 1984 and diagnosed as left nonhormonal adrenal tumor after DIP, CT scanning, and hormonal assay in serum and urine. Left radical nephrectomy was done and the histological diagnosis was neuroblastoma. The chemotherapy of EDX, 5FU was done in 5 courses, but the patient had multiple metastasis and died on November 30, 1984. Neuroblastoma in the adult is rare and 40 cases (greater than 15-year-old) have been reported in the past 5 years, 20 of which were olfactory neuroblastoma. Particularly in urological sites, only 13 cases (greater than 15-year-old) have been reported for the past 20 years. Thus it is a characteristic of adult neuroblastoma that the occurrence in the retroperitoneal cavity is very low, compared with 60-70% of neuroblastoma in children.
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PMID:[Adult neuroblastoma: a case report]. 381 47

Amyloid beta-peptide (Abeta) plays a central role in the pathogenesis of Alzheimer's disease (AD). It is toxic to neurons, but the mechanism for its action remains largely unknown. Here, we have identified a novel death-inducing protein, Abeta-related DIP (AB-DIP), by two-hybrid screening of the human brain cDNA library and confirmed the binding of Abeta with AB-DIP by coimmunoprecipitation. Overexpression of AB-DIP-induced cell death and coexpression of Abeta enhanced the cell death. During apoptosis, the 97-kDa AB-DIP was cleaved to a 62-kDa protein (AB-DIP p62) at the caspase cleavage site, LEKD. It is more important that cotransfection of Abeta with AB-DIP produced the AB-DIP p62 fragment. Small interfering RNA-mediated knockdown of AB-DIP protein expression significantly protected neuroblastoma cells from Abeta-induced neurotoxicity. AB-DIP may mediate the neurotoxicity of Abeta, and therefore, AB-DIP may be a potential, therapeutic target for AD.
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PMID:Amyloid beta peptide binds a novel death-inducing protein, AB-DIP. 1592 95

Amyloid beta protein (Abeta)-related death-inducing protein (AB-DIP) is a novel Abeta binding protein expressed ubiquitously. Here we demonstrate that overexpression of AB-DIP in SH-SY5Y neuroblastoma cells causes G2/M arrest. By deletion mutant analysis, we have identified the minimal region within AB-DIP required for G2/M arrest. We have also shown that microtubule-interfering agents (MIAs) such as nocodazole, vinblastine, paclitaxel, and vincristine, known to arrest cells at G2/M, also phosphorylate AB-DIP. However, etoposide, which causes genotoxic stress; tunicamycin, an ER stress inducer; and rotenone, which causes mitochondrial damage, fail to phosphorylate AB-DIP, implying that phosphorylation of AB-DIP is specific to microtubule-disruption-induced G2/M arrest. By using different classes of kinase inhibitors, we also demonstrate that a putative tyrosine kinase phosphorylates AB-DIP. Mono- or multisite mutations of tyrosine or serine/threonine residues confirmed that mutation of tyrosine residues but not serine/threonine residues greatly reduces nocodazole-induced phosphorylation of AB-DIP. Furthermore, phosphorylation of AB-DIP can be induced in MCF-7 cells that lack functional p53, suggesting that AB-DIP phosphorylation is independent of p53. Mounting experimental evidence continues to support the role of cell cycle abnormalities in the pathogenesis of Alzheimer's disease, and our results suggest that AB-DIP might provide a mechanistic link between microtubule disruption, mitotic abnormalities, neuronal dysfunction, and death. Therefore, interfering with AB-DIP may have therapeutic applications in conditions such as Alzheimer's disease, in which microtubule disruption and mitotic abnormalities have been suggested to play a pathological role.
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PMID:Amyloid beta protein-related death-inducing protein induces G2/M arrest: Implications for neurodegeneration in Alzheimer's disease. 1751 Sep 77