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1.
Protein & Cell ; (12): 564-572, 2011.
Artículo en Inglés | WPRIM | ID: wpr-757065

RESUMEN

The responses of macrophages to Bacillus anthracis infection are important for the survival of the host, since macrophages are required for the germination of B. anthracis spores in lymph nodes, and macrophage death exacerbates anthrax lethal toxin (LeTx)-induced organ collapse. To elucidate the mechanism of macrophage cell death induced by LeTx, we performed a genetic screen to search for genes associated with LeTx-induced macrophage cell death. RAW264.7 cells, a macrophage-like cell line sensitive to LeTx-induced death, were randomly mutated and LeTx-resistant mutant clones were selected. AMP deaminase 3 (AMPD3), an enzyme that converts AMP to IMP, was identified to be mutated in one of the resistant clones. The requirement of AMPD3 in LeTx-induced cell death of RAW 264.7 cells was confirmed by the restoration of LeTx sensitivity with ectopic reconstitution of AMPD3 expression. AMPD3 deficiency does not affect LeTx entering cells and the cleavage of mitogen-activated protein kinase kinase (MKK) by lethal factor inside cells, but does impair an unknown downstream event that is linked to cell death. Our data provides new information regarding LeTx-induced macrophage death and suggests that there is a key regulatory site downstream of or parallel to MKK cleavage that controls the cell death in LeTx-treated macrophages.


Asunto(s)
Animales , Ratones , AMP Desaminasa , Genética , Carbunco , Patología , Antígenos Bacterianos , Toxicidad , Toxinas Bacterianas , Toxicidad , Secuencia de Bases , Western Blotting , Muerte Celular , Línea Celular , Supervivencia Celular , Células Cultivadas , Exotoxinas , Toxicidad , Macrófagos , Biología Celular , Datos de Secuencia Molecular , Reacción en Cadena de la Polimerasa
2.
Journal of the Korean Neurological Association ; : 407-409, 2006.
Artículo en Coreano | WPRIM | ID: wpr-191677

RESUMEN

No abstract available.


Asunto(s)
Alelos , AMP Desaminasa , Frecuencia de los Genes
3.
Arq. neuropsiquiatr ; 61(2A): 262-264, Jun. 2003.
Artículo en Inglés | LILACS | ID: lil-339498

RESUMEN

Approximately 1-2 percent of the population has a deficiency of the enzyme myoadenylate deaminase. Early reports suggested that patients with myoadenylate deaminase deficiency had various forms of myalgia, and exercise intolerance. However, a deficiency of the enzyme has been described in many conditions, including myopathies, neuropathies, and motor neuron disease. We report a patient with clinical diagnosis of myotonia congenita and absent myoadenylate deaminase reaction on the muscle biopsy. This is the first description of myoadenilate deaminase deficiency with myotonia congenita. Myoadenylate deaminase deficiency is the most common enzymatic deficit of muscle, and the association with other neuromuscular diseases is coincidental


Asunto(s)
Humanos , Masculino , Niño , AMP Desaminasa , Miotonía Congénita , Biopsia , Músculos , Miotonía Congénita
5.
Korean Journal of Obstetrics and Gynecology ; : 2194-2200, 2001.
Artículo en Coreano | WPRIM | ID: wpr-134917

RESUMEN

OBJECTIVE: This work was demonstrated the induction of apoptosis in response to adriamycin, we checked the cell cycle of adriamycin-induced apoptosis and to investigate whether differential expression is associated with adriamycin-induced genes in human cervical carcinoma HeLa cells. METHODS: Apoptosis was measured by flow cytometry for cell cycle analysis in Hela cells. Differential expression is associated with adriamycin-induced genes in HeLa cells, it was performed to purifiy the RNA, cDNA probe and hybridization. The various different overexpressed genes were determined by gene array analysis (GDA). Analysis were referenced Incyte Genomics Co. (http://www.ncbi.nlm.nih.gov/). RESULTS: We found that adriamycin was induced apoptosis in a dose- and time-dependent manner, as demonstrated by sub-G0/G1 peaks in DNA content histogram of cell cycle. The cells of G2/M phase by treatment of 0.1 microgram/mL adriamycin had been arrested. G2/M peaks in DNA content was decreased in a dose and time-dependent manner. It had been observed 6 group, 16 genes. The group I contained thioredoxin and cytochrome c oxidase subunit IV gene, group II were p53 and excision repair protein (ERCC-1) gene. Group III was metabolic regulated gene, glucosidase, AMP deaminase isoform L (AMPD2), glutamine synthetase, cholesterol 25-hydroxylase, and steryl-sulfatase precursor. Group IV was cell skeleton constructed gene, heparan sulfate proteoglycan (HSPG2), and microfibrillar-associated protein (MFAP2), group V was oncogene group, v-yes-1 Yamaguchi sarcoma viral oncogene homolog-1 (YES1) and tyrosine kinase ELK1. The other group 6 contained NOD1 protein gene interleukine-1 receptor accessory protein (IL1RAP), pregnancy-specific glycoprotein-11 (PSG11), and pregnancy-specific protein-1a (PSG-1a). CONCLUSION: The present findings indicating that adriamycin was revealed apoptosis in Hela cell. Differential gene expression is related in various metabolism by adriamycin.


Asunto(s)
Humanos , AMP Desaminasa , Apoptosis , Ciclo Celular , Colesterol , ADN , Reparación del ADN , ADN Complementario , Doxorrubicina , Complejo IV de Transporte de Electrones , Citometría de Flujo , Expresión Génica , Genómica , Glucosidasas , Glutamato-Amoníaco Ligasa , Células HeLa , Proteoglicanos de Heparán Sulfato , Metabolismo , Oncogenes , Proteínas Tirosina Quinasas , ARN , Sarcoma , Esqueleto , Esteril-Sulfatasa , Tiorredoxinas
6.
Korean Journal of Obstetrics and Gynecology ; : 2194-2200, 2001.
Artículo en Coreano | WPRIM | ID: wpr-134916

RESUMEN

OBJECTIVE: This work was demonstrated the induction of apoptosis in response to adriamycin, we checked the cell cycle of adriamycin-induced apoptosis and to investigate whether differential expression is associated with adriamycin-induced genes in human cervical carcinoma HeLa cells. METHODS: Apoptosis was measured by flow cytometry for cell cycle analysis in Hela cells. Differential expression is associated with adriamycin-induced genes in HeLa cells, it was performed to purifiy the RNA, cDNA probe and hybridization. The various different overexpressed genes were determined by gene array analysis (GDA). Analysis were referenced Incyte Genomics Co. (http://www.ncbi.nlm.nih.gov/). RESULTS: We found that adriamycin was induced apoptosis in a dose- and time-dependent manner, as demonstrated by sub-G0/G1 peaks in DNA content histogram of cell cycle. The cells of G2/M phase by treatment of 0.1 microgram/mL adriamycin had been arrested. G2/M peaks in DNA content was decreased in a dose and time-dependent manner. It had been observed 6 group, 16 genes. The group I contained thioredoxin and cytochrome c oxidase subunit IV gene, group II were p53 and excision repair protein (ERCC-1) gene. Group III was metabolic regulated gene, glucosidase, AMP deaminase isoform L (AMPD2), glutamine synthetase, cholesterol 25-hydroxylase, and steryl-sulfatase precursor. Group IV was cell skeleton constructed gene, heparan sulfate proteoglycan (HSPG2), and microfibrillar-associated protein (MFAP2), group V was oncogene group, v-yes-1 Yamaguchi sarcoma viral oncogene homolog-1 (YES1) and tyrosine kinase ELK1. The other group 6 contained NOD1 protein gene interleukine-1 receptor accessory protein (IL1RAP), pregnancy-specific glycoprotein-11 (PSG11), and pregnancy-specific protein-1a (PSG-1a). CONCLUSION: The present findings indicating that adriamycin was revealed apoptosis in Hela cell. Differential gene expression is related in various metabolism by adriamycin.


Asunto(s)
Humanos , AMP Desaminasa , Apoptosis , Ciclo Celular , Colesterol , ADN , Reparación del ADN , ADN Complementario , Doxorrubicina , Complejo IV de Transporte de Electrones , Citometría de Flujo , Expresión Génica , Genómica , Glucosidasas , Glutamato-Amoníaco Ligasa , Células HeLa , Proteoglicanos de Heparán Sulfato , Metabolismo , Oncogenes , Proteínas Tirosina Quinasas , ARN , Sarcoma , Esqueleto , Esteril-Sulfatasa , Tiorredoxinas
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