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  1 / 135 MEDLINE  
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[PMID]:27649891
[Au] Autor:Liu J; Shen C; Fan W; Chen Y; Zhang A; Feng Y; Li Z; Kuang Y; Wang Z
[Ad] Endereço:State Key Laboratory of Medical Genomics, Research Center for Experimental Medicine, Ruijin Hospital Affiliated to Shanghai Jiao Tong University School of Medicine (SJTUSM), Shanghai 200025, China.
[Ti] Título:Low levels of PRSS37 protein in sperm are associated with many cases of unexplained male infertility.
[So] Source:Acta Biochim Biophys Sin (Shanghai);48(11):1058-1065, 2016 Nov.
[Is] ISSN:1745-7270
[Cp] País de publicação:China
[La] Idioma:eng
[Ab] Resumo:PRSS37, a putative trypsin-like serine protease, is highly conserved during mammalian evolution as revealed by multiple sequence alignment. Mice deficient for Prss37 gene exhibit male infertility, but their mating behavior, spermatogenesis, sperm morphology, and motility remain unaffected, similar to a situation called unexplained male infertility (UMI) in men (human being). Here, we demonstrated that PRSS37 is restrictively expressed in human testis, where it is mainly located in the elongating and elongated spermatids during spermiogenesis as shown by immunohistochemical analysis of normal human testicular sections. In mature sperm, PRSS37 appears in the acrosome region and diminishes during acrosome reaction. Further examination reveals that PRSS37 contents in sperm from patients with UMI are dramatically lower than those in sperm from men with proven fertility or from sperm donors. Sperm with low PRSS37 contents exhibit abnormal activation of the proacrosin/acrosin system and premature proteolysis of ADAM2, which may impair the functional competence of human sperm in vivo However, the in vitro fertilization outcomes of sperm with low PRSS37 contents are not affected. Together, these data implicate an important role of PRSS37 for male fertility. PRSS37 can be used as a potential molecular biomarker for evaluating sperm fertilization capability in vivo but not in vitro.
[Mh] Termos MeSH primário: Infertilidade Masculina/metabolismo
Serina Proteases/metabolismo
Espermatozoides/metabolismo
[Mh] Termos MeSH secundário: Acrossomo/metabolismo
Reação Acrossômica
Estudos de Casos e Controles
Fertilinas/metabolismo
Fertilização In Vitro
Perfilação da Expressão Gênica
Seres Humanos
Masculino
Proteólise
Serina Proteases/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (PRSS37 protein, human); EC 3.4.- (Serine Proteases); EC 3.4.24.- (ADAM2 protein, human); EC 3.4.24.- (Fertilins)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170214
[Lr] Data última revisão:
170214
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160922
[St] Status:MEDLINE


  2 / 135 MEDLINE  
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[PMID]:27341348
[Au] Autor:Choi H; Jin S; Kwon JT; Kim J; Jeong J; Kim J; Jeon S; Park ZY; Jung KJ; Park K; Cho C
[Ad] Endereço:School of Life Sciences, Gwangju Institute of Science and Technology, Gwangju, Korea.
[Ti] Título:Characterization of Mammalian ADAM2 and Its Absence from Human Sperm.
[So] Source:PLoS One;11(6):e0158321, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The members of the ADAM (a disintegrin and metalloprotease) family are membrane-anchored multi-domain proteins that play prominent roles in male reproduction. ADAM2, which was one of the first identified ADAMs, is the best studied ADAM in reproduction. In the male germ cells of mice, ADAM2 and other ADAMs form complexes that contribute to sperm-sperm adhesion, sperm-egg interactions, and the migration of sperm in the female reproductive tract. Here, we generated specific antibodies against mouse and human ADAM2, and investigated various features of ADAM2 in mice, monkeys and humans. We found that the cytoplasmic domain of ADAM2 might enable the differential association of this protein with other ADAMs in mice. Western blot analysis with the anti-human ADAM2 antibodies showed that ADAM2 is present in the testis and sperm of monkeys. Monkey ADAM2 was found to associate with chaperone proteins in testis. In humans, we identified ADAM2 as a 100-kDa protein in the testis, but failed to detect it in sperm. This is surprising given the results in mice and monkeys, but it is consistent with the failure of ADAM2 identification in the previous proteomic analyses of human sperm. These findings suggest that the reproductive functions of ADAM2 differ between humans and mice. Our protein analysis showed the presence of potential ADAM2 complexes involving yet-unknown proteins in human testis. Taken together, our results provide new information regarding the characteristics of ADAM2 in mammalian species, including humans.
[Mh] Termos MeSH primário: Fertilinas/metabolismo
Mamíferos/metabolismo
Espermatozoides/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Cromatografia Líquida
Fertilinas/química
Fertilinas/genética
Seres Humanos
Macaca fascicularis
Masculino
Camundongos
Domínios e Motivos de Interação entre Proteínas
Espectrometria de Massas em Tandem
Testículo/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.4.24.- (Fertilins)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170724
[Lr] Data última revisão:
170724
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160625
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0158321


  3 / 135 MEDLINE  
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[PMID]:26860122
[Au] Autor:Leahy T; Rickard JP; Aitken RJ; de Graaf SP
[Ad] Endereço:Faculty of Veterinary ScienceThe University of Sydney, Camperdown, New South Wales, Australia tamara.leahy@sydney.edu.au.
[Ti] Título:D-penicillamine prevents ram sperm agglutination by reducing the disulphide bonds of a copper-binding sperm protein.
[So] Source:Reproduction;151(5):491-500, 2016 May.
[Is] ISSN:1741-7899
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Head-to-head agglutination of ram spermatozoa is induced by dilution in the Tyrode's capacitation medium with albumin, lactate and pyruvate (TALP) and ameliorated by the addition of the thiol d-penicillamine (PEN). To better understand the association and disassociation of ram spermatozoa, we investigated the mechanism of action of PEN in perturbing sperm agglutination. PEN acts as a chelator of heavy metals, an antioxidant and a reducing agent. Chelation is not the main mechanism of action, as the broad-spectrum chelator ethylenediaminetetraacetic acid and the copper-specific chelator bathocuproinedisulfonic acid were inferior anti-agglutination agents compared with PEN. Oxidative stress is also an unlikely mechanism of sperm association, as PEN was significantly more effective in ameliorating agglutination than the antioxidants superoxide dismutase, ascorbic acid, α-tocopherol and catalase. Only the reducing agents cysteine and DL-dithiothreitol displayed similar levels of non-agglutinated spermatozoa at 0 h compared with PEN but were less effective after 3 h of incubation (37 °C). The addition of 10 µM Cu(2+) to 250 µM PEN + TALP caused a rapid reversion of the motile sperm population from a non-agglutinated state to an agglutinated state. Other heavy metals (cobalt, iron, manganese and zinc) did not provoke such a strong response. Together, these results indicate that PEN prevents sperm association by the reduction of disulphide bonds on a sperm membrane protein that binds copper. ADAM proteins are possible candidates, as targeted inhibition of the metalloproteinase domain significantly increased the percentage of motile, non-agglutinated spermatozoa (52.0% ± 7.8) compared with TALP alone (10.6% ± 6.1).
[Mh] Termos MeSH primário: Proteínas de Transporte/metabolismo
Quelantes/farmacologia
Cobre/farmacologia
Dissulfetos/química
Penicilamina/farmacologia
Aglutinação Espermática/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Dissulfetos/metabolismo
Fertilinas/metabolismo
Masculino
Ovinos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (Chelating Agents); 0 (Disulfides); 0 (copper-binding protein); 789U1901C5 (Copper); EC 3.4.24.- (Fertilins); GNN1DV99GX (Penicillamine)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160211
[St] Status:MEDLINE
[do] DOI:10.1530/REP-15-0596


  4 / 135 MEDLINE  
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[PMID]:26408501
[Au] Autor:Castilla-Cortázar I; Gago A; Muñoz Ú; Ávila-Gallego E; Guerra-Menéndez L; Sádaba MC; García-Magariño M; Olleros Santos-Ruiz M; Aguirre GA; Puche JE
[Ad] Endereço:Fundación de Investigación HM Hospitales, Madrid, Spain; Escuela Nacional de Medicina, Tecnológico de Monterrey, Nuevo León, Mexico. Electronic address: iccortazar@itesm.mx.
[Ti] Título:Mechanisms Underlying Testicular Damage and Dysfunction in Mice With Partial IGF-1 Deficiency and the Effectiveness of IGF-1 Replacement Therapy.
[So] Source:Urology;86(6):1241.e1-9, 2015 Dec.
[Is] ISSN:1527-9995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: To determine whether insulin-like growth factor (IGF-1) deficiency can cause testicular damage and to examine changes of the testicular morphology and testicular function-related gene expression caused by IGF-1 deficiency. Therefore, this study aims to determine the benefits of low doses of IGF-1 and to explore the mechanisms underlying the IGF-1 replacement therapy. MATERIALS AND METHODS: A murine model of IGF-1 deficiency was used to avoid any factor that could contribute to testicular damage. Testicular weight, score of histopathological damage, and gene expressions were studied in 3 experimental groups of mice: controls (wild-type Igf1(+/+)), heterozygous Igf1(+/-) with partial IGF-1 deficiency, and heterozygous Igf1(+/-) treated with IGF-1. RESULTS: Results show that the partial IGF-1 deficiency induced testicular damage and altered expression of genes involved in IGF-1 and growth hormone signaling and regulation, testicular hormonal function, extracellular matrix establishment and its regulation, angiogenesis, fibrogenesis, inflammation, and cytoprotection. In addition, proteins involved in tight junction expression were found to be reduced. However, low doses of IGF-1 restored the testicular damage and most of these parameters. CONCLUSION: IGF-1 deficiency caused the damage of the blood-testis barrier and testicular structure and induced the abnormal testicular function-related gene expressions. However, low doses of IGF-1 constitute an effective replacement therapy that restores the described testicular damage. Data herein show that (1) cytoprotective activities of IGF-1 seem to be mediated by heat shock proteins and that (2) connective tissue growth factor could play a relevant role together with IGF-1 in the extracellular matrix establishment.
[Mh] Termos MeSH primário: Barreira Hematotesticular/química
Proteínas da Matriz Extracelular/genética
Expressão Gênica/efeitos dos fármacos
Fator de Crescimento Insulin-Like I/deficiência
Fator de Crescimento Insulin-Like I/farmacologia
Proteoglicanas/genética
Testículo/patologia
Testículo/fisiopatologia
[Mh] Termos MeSH secundário: Proteínas ADAM/genética
Animais
Antígenos CD18/genética
Caderinas/análise
Fator de Crescimento do Tecido Conjuntivo/genética
Citocromo P-450 CYP3A/genética
Modelos Animais de Doenças
Fertilinas
Expressão Gênica/genética
Genótipo
Inibinas/genética
Proteínas de Ligação a Fator de Crescimento Semelhante a Insulina/genética
Fator de Crescimento Insulin-Like I/genética
Masculino
Glicoproteínas de Membrana/genética
Metaloproteases/genética
Camundongos
Tamanho do Órgão
Receptor IGF Tipo 1/genética
Receptores do FSH/análise
Receptores da Somatotropina/análise
Receptores da Somatotropina/genética
Transdução de Sinais/efeitos dos fármacos
Transdução de Sinais/genética
Testículo/química
Junções Íntimas/química
Inibidor Tecidual de Metaloproteinase-1/genética
Fator de Crescimento Transformador alfa/genética
Fator de Crescimento Transformador beta/genética
Fator A de Crescimento do Endotélio Vascular/genética
Proteína da Zônula de Oclusão-1/análise
beta Catenina/análise
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (CD18 Antigens); 0 (Cadherins); 0 (Ctgf protein, mouse); 0 (Extracellular Matrix Proteins); 0 (Insulin-Like Growth Factor Binding Proteins); 0 (Membrane Glycoproteins); 0 (Proteoglycans); 0 (Receptors, FSH); 0 (Receptors, Somatotropin); 0 (Timp1 protein, mouse); 0 (Tissue Inhibitor of Metalloproteinase-1); 0 (Transforming Growth Factor alpha); 0 (Transforming Growth Factor beta); 0 (Vascular Endothelial Growth Factor A); 0 (Zonula Occludens-1 Protein); 0 (beta Catenin); 0 (insulin-like growth factor-1, mouse); 139568-91-5 (Connective Tissue Growth Factor); 57285-09-3 (Inhibins); 67763-96-6 (Insulin-Like Growth Factor I); EC 1.14.14.1 (Cyp3a25 protein, mouse); EC 1.14.14.1 (Cytochrome P-450 CYP3A); EC 2.7.10.1 (Receptor, IGF Type 1); EC 3.4.- (Metalloproteases); EC 3.4.24.- (ADAM Proteins); EC 3.4.24.- (Fertilins)
[Em] Mês de entrada:1605
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150927
[St] Status:MEDLINE


  5 / 135 MEDLINE  
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[PMID]:26252478
[Au] Autor:Maheswaran E; Pedersen CB; Ditzel HJ; Gjerstorff MF
[Ad] Endereço:Department of Cancer and Inflammation Research, Institute for Molecular Medicine (IMM), University of Southern Denmark, Odense, Denmark.
[Ti] Título:Lack of ADAM2, CALR3 and SAGE1 Cancer/Testis Antigen Expression in Lung and Breast Cancer.
[So] Source:PLoS One;10(8):e0134967, 2015.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Immunotherapy is emerging as a supplement to conventional cancer treatment, and identifying antigen targets for specific types of cancer is critical to optimizing therapeutic efficacy. Cancer/testis antigens are highly promising targets for immunotherapy due to their cancer-specific expression and antigenic properties, but the expression patterns of most of the more than 200 identified cancer/testis antigens in various cancers remain largely uncharacterized. In this study, we investigated the expression of the cancer/testis antigens ADAM2, CALR3 and SAGE1 in lung and breast cancer, the two most frequent human cancers, with the purpose of providing novel therapeutic targets for these diseases. We used a set of previously uncharacterized antibodies against the cancer/testis antigens ADAM2, CALR3 and SAGE1 to investigate their expression in a large panel of normal tissues as well as breast and lung cancers. Staining for the well-characterized MAGE-A proteins was included for comparison. Immunohistochemical staining confirmed previous mRNA analysis demonstrating that ADAM2, CALR3 and SAGE1 proteins are confined to testis in normal individuals. Negative tissues included plancenta, which express many other CT antigens, such as MAGE-A proteins. Surprisingly, we detected no ADAM2, CALR3 and SAGE1 in the 67 lung cancers (mainly non-small lung cancer) and 189 breast cancers, while MAGE-A proteins were present in 15% and 7-16% of these tumor types, respectively. Treatment with DNA methyltransferase inhibitors has been proposed as an attractive strategy to increase the expression of cancer/testis antigens in tumors before immunotargeting; however, neither ADAM2, CALR3 nor SAGE1 could be significantly induced in lung and breast cancer cell lines using this strategy. Our results suggest that ADAM2, CALR3 and SAGE1 cancer/testis antigens are not promising targets for immunotherapy of breast and lung cancer.
[Mh] Termos MeSH primário: Proteínas ADAM/metabolismo
Antígenos de Neoplasias/metabolismo
Neoplasias da Mama/metabolismo
Calreticulina/metabolismo
Neoplasias Pulmonares/metabolismo
Glicoproteínas de Membrana/metabolismo
[Mh] Termos MeSH secundário: Azacitidina/farmacologia
Azacitidina/uso terapêutico
Neoplasias da Mama/tratamento farmacológico
Neoplasias da Mama/patologia
Linhagem Celular Tumoral
Estudos de Coortes
Feminino
Fertilinas
Seres Humanos
Imuno-Histoquímica
Neoplasias Pulmonares/tratamento farmacológico
Neoplasias Pulmonares/patologia
Antígenos Específicos de Melanoma/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antigens, Neoplasm); 0 (Calreticulin); 0 (MAGEA1 protein, human); 0 (Melanoma-Specific Antigens); 0 (Membrane Glycoproteins); 0 (SAGE protein, human); EC 3.4.24.- (ADAM Proteins); EC 3.4.24.- (ADAM2 protein, human); EC 3.4.24.- (Fertilins); M801H13NRU (Azacitidine)
[Em] Mês de entrada:1605
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150808
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0134967


  6 / 135 MEDLINE  
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[PMID]:26226211
[Au] Autor:Jaiswal MK; Agrawal V; Katara GK; Pamarthy S; Kulshrestha A; Chaouat G; Gilman-Sachs A; Beaman KD
[Ad] Endereço:Department of Microbiology and Immunology, Rosalind Franklin University of Medicine and Science, North Chicago, IL, USA. Electronic address: mukesh.jaiswal@rosalindfranklin.edu.
[Ti] Título:Male fertility and apoptosis in normal spermatogenesis are regulated by vacuolar-ATPase isoform a2.
[So] Source:J Reprod Immunol;112:38-45, 2015 Nov.
[Is] ISSN:1872-7603
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:The a2 isoform of vacuolar-ATPase (ATP6V0A2, referred to as a2V) is required for normal spermatogenesis and maturation of sperm. Treatment of male mice with anti-a2V disturbs the testicular cytokine/chemokine balance and leads to severe deficiencies of spermatogenesis. The aim of the present study was to investigate the role of a2V in male fertility and in the regulation of apoptotic pathways required for normal spermatogenesis in mice. To study the role of a2V single dose of anti-a2V monoclonal antibody or mouse IgG isotype (3µg/animal) was injected i.p. into males on alternate days for 10 days. The expression of sperm maturation-related molecules and pro-apoptotic molecules was measured by real-time PCR or immunohistochemistry in control and anti-a2V-treated testes. The caspase levels and their activity were measured by western blot and fluorometry. We found that the expression of the sperm maturation-related molecules SPAM1, ADAM1, and ADAM2 was significantly decreased in testes from anti-a2V-treated males. The expression of pro-apoptotic molecules (Bax, p53, and p21) and molecules involved in the intrinsic pathway of apoptosis (caspase-9, caspase-3, and PARP), which are crucial for normal spermatogenesis was significantly reduced in testes from anti-a2V-treated males compared with the control. The total ATP level was significantly lower in anti-a2V-treated testes. The data provide novel evidence showing that a2V can regulate the apoptotic pathways, an essential testicular feature, and is necessary for efficient spermatogenesis.
[Mh] Termos MeSH primário: Apoptose/imunologia
Fertilidade/imunologia
ATPases Translocadoras de Prótons/imunologia
Espermatogênese/imunologia
Espermatozoides/imunologia
[Mh] Termos MeSH secundário: Proteínas ADAM/imunologia
Animais
Anticorpos Monoclonais Murinos/imunologia
Anticorpos Monoclonais Murinos/farmacologia
Apoptose/efeitos dos fármacos
Proteínas Reguladoras de Apoptose/imunologia
Caspases/imunologia
Moléculas de Adesão Celular/imunologia
Fertilinas
Fertilidade/efeitos dos fármacos
Hialuronoglucosaminidase/imunologia
Masculino
Glicoproteínas de Membrana/imunologia
Camundongos
Camundongos Endogâmicos BALB C
ATPases Translocadoras de Prótons/antagonistas & inibidores
Espermatogênese/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antibodies, Monoclonal, Murine-Derived); 0 (Apoptosis Regulatory Proteins); 0 (Atp6v0a2 protein, mouse); 0 (Cell Adhesion Molecules); 0 (Membrane Glycoproteins); EC 3.2.1.35 (Hyaluronoglucosaminidase); EC 3.2.1.35 (hyaluronidase PH-20); EC 3.4.22.- (Caspases); EC 3.4.24.- (ADAM Proteins); EC 3.4.24.- (Adam2 protein, mouse); EC 3.4.24.- (Fertilins); EC 3.6.3.14 (Proton-Translocating ATPases)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:161126
[Lr] Data última revisão:
161126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150731
[St] Status:MEDLINE


  7 / 135 MEDLINE  
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[PMID]:23065232
[Au] Autor:Choi H; Lee B; Jin S; Kwon JT; Kim J; Jeong J; Oh S; Cho BN; Park ZY; Cho C
[Ad] Endereço:School of Life Sciences, Gwangju Institute of Science and Technology, Gwangju, 500-712, Korea.
[Ti] Título:Identification and characterization of promoter and regulatory regions for mouse Adam2 gene expression.
[So] Source:Mol Biol Rep;40(2):787-96, 2013 Feb.
[Is] ISSN:1573-4978
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:ADAM2, a member of the 'a disintegrin and metalloprotease' (ADAM) family, is a key protein in mammalian fertilization that is specifically expressed in testicular germ cells. Here, we investigated the transcriptional regulation of the mouse Adam2 gene. An in silico analysis identified two conserved non-coding sequences located upstream of the mouse and human ADAM2 genes. The upstream region of the mouse Adam2 gene was found to lack typical TATA and CAAT boxes, and to have a high GC content. Our in vitro transient transfection-reporter analysis identified a promoter in this region of the mouse Adam2 gene, along with regulatory regions that inhibit the activity of this promoter in somatic cells. Site-directed mutagenesis revealed that the caudal-type homeobox 1 and CCTC-binding factor motifs are responsible for the inhibitory activities of the repressor regions. Finally, electrophoretic mobility shift assays showed putative transcription factor-promoter DNA complexes, and DNA-affinity chromatography and proteomic analyses identified myelin gene regulatory factor as a binding partner of the Adam2 promoter. This provides the first identification and characterization of promoter and repressor regions that regulate the transcription of the mouse Adam2 gene, and offers insights into the regulation of this germ-cell-specific gene.
[Mh] Termos MeSH primário: Proteínas ADAM/genética
Regulação Enzimológica da Expressão Gênica
Glicoproteínas de Membrana/genética
Regiões Promotoras Genéticas
[Mh] Termos MeSH secundário: Proteínas ADAM/metabolismo
Animais
Sequência de Bases
Sítios de Ligação
Ensaio de Desvio de Mobilidade Eletroforética
Fertilinas
Genes Reporter
Células HEK293
Seres Humanos
Luciferases de Renilla/biossíntese
Luciferases de Renilla/genética
Masculino
Glicoproteínas de Membrana/metabolismo
Camundongos
Anotação de Sequência Molecular
Dados de Sequência Molecular
Mutagênese Sítio-Dirigida
Células NIH 3T3
Ligação Proteica
Análise de Sequência de DNA
Testículo/citologia
Fatores de Transcrição/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Membrane Glycoproteins); 0 (Transcription Factors); 0 (myelin gene regulatory factor, mouse); EC 1.13.12.5 (Luciferases, Renilla); EC 3.4.24.- (ADAM Proteins); EC 3.4.24.- (ADAM2 protein, human); EC 3.4.24.- (Adam2 protein, mouse); EC 3.4.24.- (Fertilins)
[Em] Mês de entrada:1306
[Cu] Atualização por classe:171030
[Lr] Data última revisão:
171030
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:121016
[St] Status:MEDLINE
[do] DOI:10.1007/s11033-012-2116-8


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[PMID]:22951102
[Au] Autor:Hwang JY; Mulligan BP; Kim HM; Yang BC; Lee CK
[Ad] Endereço:Department of Agricultural Biotechnology, Animal Biotechnology Major, and Research Institute for Agriculture and Life Science, Seoul National University, Seoul 151-921, Korea.
[Ti] Título:Quantitative analysis of sperm mRNA in the pig: relationship with early embryo development and capacitation.
[So] Source:Reprod Fertil Dev;25(5):807-17, 2013.
[Is] ISSN:1031-3613
[Cp] País de publicação:Australia
[La] Idioma:eng
[Ab] Resumo:Although it is well known that mRNA is present in mammalian spermatozoa, the relevance of mRNA to capacitation and early embryo development in the pig remains unclear. In the present study, we investigated differences in the abundance of selected mRNAs coding for MYC, CYP19, ADAM2, PRM1 and PRM2 in purified porcine spermatozoa depending on embryo cleavage rate and capacitation (n=20 semen samples). Semen samples were used in IVF procedures, with subsequent embryo development classified into one of two groups based on cleavage rate (i.e. high (>75%) and low (<75%) cleavage groups) and mRNA abundance in purified spermatozoa compared between these two groups. In addition, mRNA abundance was compared between capacitated and non-capacitated spermatozoa. Comparison of mRNA levels between porcine spermatozoa revealed that the abundance of MYC, CYP19, ADAM2, PRM1 and PRM2 mRNA was significantly greater in the high cleavage group (n=10 high cleavage group semen samples) than in the low cleavage group (n=10; P<0.05). Significant downregulation of MYC mRNA was observed in capacitated spermatozoa (n=12; P<0.05). The results of the present study suggest that the amount of specific mRNAs could be used for estimating the quality of spermatozoa in the pig.
[Mh] Termos MeSH primário: Regulação da Expressão Gênica/fisiologia
RNA Mensageiro/metabolismo
Capacitação Espermática/fisiologia
Espermatozoides/citologia
Suínos/embriologia
Suínos/genética
[Mh] Termos MeSH secundário: Proteínas ADAM/genética
Animais
Aromatase/genética
Primers do DNA/genética
Fertilinas
Regulação da Expressão Gênica/genética
Genes myc/genética
Modelos Lineares
Masculino
Glicoproteínas de Membrana/genética
Protaminas/genética
RNA Mensageiro/genética
Reação em Cadeia da Polimerase em Tempo Real/veterinária
Reação em Cadeia da Polimerase Via Transcriptase Reversa/veterinária
Espermatozoides/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA Primers); 0 (Membrane Glycoproteins); 0 (Protamines); 0 (RNA, Messenger); EC 1.14.14.1 (Aromatase); EC 3.4.24.- (ADAM Proteins); EC 3.4.24.- (Fertilins)
[Em] Mês de entrada:1401
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120907
[St] Status:MEDLINE
[do] DOI:10.1071/RD12160


  9 / 135 MEDLINE  
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[PMID]:22977858
[Au] Autor:Sukhikh GT; Bourmenskaya OV; Smolnikova VY; Krasnoschoka OE; Trofimov DY; Donnikov AE; Kalinina EA
[Ad] Endereço:V. I. Kulakov Center of Obstetrics, Gynecology, and Perinatology, the Ministry of Health and Social Development of the Russian Federation, Moscow, Russia.
[Ti] Título:Protamine and fertilin mRNA: potential biomarkers of assisted reproductive technology outcomes.
[So] Source:Bull Exp Biol Med;153(4):513-5, 2012 Aug.
[Is] ISSN:1573-8221
[Cp] País de publicação:United States
[La] Idioma:eng; rus
[Ab] Resumo:We studied the relationship between the levels of protamines 1 and 2 (PRM1 and PRM2) and fertilin-ß (ADAM-2) mRNA expression and outcomes of infertility treatment using assisted reproductive technologies was studied. Analysis of the relationships between the outcomes of in vitro fertilization and embryo transfer and profiles of the expression of seminal genes PRM1, PRM2, ADAM-2 mRNA, evaluated by reverse transcription quantitative PCR was carried out in 79 couples. Significant differences in the expression of seminal PRM1, PRM2, ADAM-2 mRNA were detected in couples with different outcomes of in vitro fertilization and embryo transfer. The levels of seminal gene expression are potential predictors of the efficiency of in vitro fertilization and embryo transfer.
[Mh] Termos MeSH primário: Proteínas ADAM/metabolismo
Biomarcadores/metabolismo
Transferência Embrionária
Fertilização In Vitro
Infertilidade/terapia
Glicoproteínas de Membrana/metabolismo
Protaminas/metabolismo
[Mh] Termos MeSH secundário: Proteínas ADAM/genética
Fertilinas
Seres Humanos
Glicoproteínas de Membrana/genética
Protaminas/genética
RNA Mensageiro/metabolismo
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Estatísticas não Paramétricas
Resultado do Tratamento
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Biomarkers); 0 (Membrane Glycoproteins); 0 (PRM1 protein, human); 0 (Protamines); 0 (RNA, Messenger); 0 (protamine 2); EC 3.4.24.- (ADAM Proteins); EC 3.4.24.- (ADAM2 protein, human); EC 3.4.24.- (Fertilins)
[Em] Mês de entrada:1301
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120915
[St] Status:MEDLINE


  10 / 135 MEDLINE  
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[PMID]:22841667
[Au] Autor:Bulstrode H; Jones LM; Siney EJ; Sampson JM; Ludwig A; Gray WP; Willaime-Morawek S
[Ad] Endereço:Clinical Neurosciences, Faculty of Medicine, University of Southampton, Southampton SO16 6YD, UK.
[Ti] Título:A-Disintegrin and Metalloprotease (ADAM) 10 and 17 promote self-renewal of brain tumor sphere forming cells.
[So] Source:Cancer Lett;326(1):79-87, 2012 Dec 29.
[Is] ISSN:1872-7980
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:It has been proposed that gliomas contain a subpopulation of 'Brain Tumor Stem Cells' (BTSCs), which demonstrate resistance to conventional therapies. A potential component of the environment governing the behavior of these BTSCs is a class of transmembrane proteins with structural and signaling functions, the A-Disintegrin And Metalloproteases (ADAMs). In this study we confirm overexpression of ADAM10 and 17 in human glioma tissue compared to human controls, and especially in tumor sphere cultures thought to enrich for BTSCs. Inhibition of ADAM10/17 function impairs the growth of tumor spheres with evidence of depletion of the sphere forming cell population. This results from a combination of reduced proliferation, cell death and a switch of sphere-forming cells away from symmetric self-renewal division towards neuronal differentiation. A developing appreciation of the role of ADAMs in BTSC promises insights into pathophysiology and potential therapeutic avenues in this intractable group of tumors.
[Mh] Termos MeSH primário: Proteínas ADAM/metabolismo
Secretases da Proteína Precursora do Amiloide/metabolismo
Neoplasias Encefálicas/metabolismo
Glioma/metabolismo
Glicoproteínas de Membrana/metabolismo
Proteínas de Membrana/metabolismo
Células-Tronco Neoplásicas/metabolismo
Esferoides Celulares
Células Tumorais Cultivadas
[Mh] Termos MeSH secundário: Proteínas ADAM/antagonistas & inibidores
Proteína ADAM10
Diferenciação Celular
Proliferação Celular
Sobrevivência Celular
Fertilinas
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Membrane Glycoproteins); 0 (Membrane Proteins); EC 3.4.- (Amyloid Precursor Protein Secretases); EC 3.4.24.- (ADAM Proteins); EC 3.4.24.- (Fertilins); EC 3.4.24.81 (ADAM10 Protein); EC 3.4.24.81 (ADAM10 protein, human)
[Em] Mês de entrada:1212
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120731
[St] Status:MEDLINE



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