Base de dados : MEDLINE
Pesquisa : D12.776.124.790.106.740 [Categoria DeCS]
Referências encontradas : 80 [refinar]
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[PMID]:19105413
[Au] Autor:Novikova MS; Kalinchenko SIu; Borisov VV
[Ti] Título:[Metabolic syndrome and chronic disease of the kidneys: the role of age-related androgenic deficiency. New approaches to treatment (review)].
[So] Source:Ter Arkh;80(10):41-6, 2008.
[Is] ISSN:0040-3660
[Cp] País de publicação:Russia (Federation)
[La] Idioma:rus
[Mh] Termos MeSH primário: Androgênios/deficiência
Hipolipemiantes/uso terapêutico
Falência Renal Crônica/tratamento farmacológico
Falência Renal Crônica/epidemiologia
Lactonas/uso terapêutico
Síndrome Metabólica/tratamento farmacológico
Síndrome Metabólica/epidemiologia
Testosterona/análogos & derivados
[Mh] Termos MeSH secundário: Fatores Etários
Dislipidemias/epidemiologia
Seres Humanos
Hipertensão/epidemiologia
Resistência à Insulina
Síndrome Metabólica/metabolismo
Globulina de Ligação a Progesterona/deficiência
Testosterona/deficiência
Testosterona/uso terapêutico
Fator de Necrose Tumoral alfa/metabolismo
Túnica Íntima/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Androgens); 0 (Hypolipidemic Agents); 0 (Lactones); 0 (Progesterone-Binding Globulin); 0 (Tumor Necrosis Factor-alpha); 3XMK78S47O (Testosterone); 95M8R751W8 (orlistat); H16A5VCT9C (testosterone undecanoate)
[Em] Mês de entrada:0902
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:081225
[St] Status:MEDLINE


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[PMID]:15702432
[Au] Autor:Lösel R; Breiter S; Seyfert M; Wehling M; Falkenstein E
[Ad] Endereço:Department of Clinical Pharmacology, Faculty for Clinical Medicine Mannheim, University of Heidelberg, Theodor-Kutzer-Ufer, 68167 Mannheim, Germany. ralf.loesel@kpha.ma.uni-heidelberg.de
[Ti] Título:Classic and non-classic progesterone receptors are both expressed in human spermatozoa.
[So] Source:Horm Metab Res;37(1):10-4, 2005 Jan.
[Is] ISSN:0018-5043
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Progesterone is one of the physiological inducers of the acrosome reaction in mammalian spermatozoa. The receptor that responds to progesterone is not yet identified, and its properties differ in many aspects from the properties of the classic nuclear progesterone receptor, suggesting the participation of a novel or non-classic receptor. In this study, we investigated the expression of a novel progesterone-binding protein (hmPR1/PGMRC1) and its ortholog (hmPR2/PGMRC2), which have previously been identified in liver microsomes and are considered receptor candidates, along with the nuclear progesterone receptor. The purification procedure was optimized with special emphasis on the control of leukocyte contamination in single donor samples. The results indicate that all three proteins are expressed in human sperm, as transcripts have been detected in 46 %, 42 % and 37.5 % of individual samples, respectively (n = 24).
[Mh] Termos MeSH primário: Proteínas de Membrana/metabolismo
Globulina de Ligação a Progesterona/metabolismo
Receptores de Progesterona/classificação
Receptores de Progesterona/metabolismo
Espermatozoides/metabolismo
[Mh] Termos MeSH secundário: Separação Celular/métodos
Perfilação da Expressão Gênica/métodos
Seres Humanos
Técnicas In Vitro
Masculino
Proteínas de Membrana/genética
Globulina de Ligação a Progesterona/genética
RNA Mensageiro/análise
Receptores de Progesterona/genética
Valores de Referência
Reação em Cadeia da Polimerase Via Transcriptase Reversa
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Membrane Proteins); 0 (PGRMC1 protein, human); 0 (PGRMC2 protein, human); 0 (Progesterone-Binding Globulin); 0 (RNA, Messenger); 0 (Receptors, Progesterone)
[Em] Mês de entrada:0507
[Cu] Atualização por classe:141120
[Lr] Data última revisão:
141120
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:050211
[St] Status:MEDLINE


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[PMID]:15207350
[Au] Autor:Sakamoto H; Ukena K; Takemori H; Okamoto M; Kawata M; Tsutsui K
[Ad] Endereço:Laboratory of Brain Science, Faculty of Integrated Arts and Sciences, Hiroshima University, Japan.
[Ti] Título:Expression and localization of 25-Dx, a membrane-associated putative progesterone-binding protein, in the developing Purkinje cell.
[So] Source:Neuroscience;126(2):325-34, 2004.
[Is] ISSN:0306-4522
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Neurosteroids are synthesized de novo in the brain and the cerebellar Purkinje cell is a major site for neurosteroid formation. We have demonstrated that the rat Purkinje cell actively produces progesterone de novo from cholesterol only during neonatal life and progesterone promotes dendritic growth, spinogenesis and synaptogenesis via its nuclear receptor in this neuron. On the other hand, 25-Dx, a putative membrane progesterone receptor, has been identified in the rat liver. In this study, we therefore investigated the expression and localization of 25-Dx in the Purkinje cell to understand the mode of progesterone actions in this neuron. Reverse transcription-PCR and Western immunoblot analyses revealed the expressions of 25-Dx mRNA and 25-Dx-like protein in the rat cerebellum, which increased during neonatal life. By immunocytochemistry, the expression of 25-Dx-like protein was localized in the Purkinje cell and external granule cell layer. At the ultrastructural level, we further found that 25-Dx-like immunoreactivity was associated with membrane structures of the endoplasmic reticulum and Golgi apparatus in the Purkinje cell. These results indicate that the Purkinje cell expresses the putative membrane progesterone receptor, 25-Dx during neonatal life. Progesterone may promote dendritic growth, spinogenesis and synaptogenesis via 25-Dx as well as its nuclear receptor in the Purkinje cell in the neonate.
[Mh] Termos MeSH primário: Proteínas de Transporte/biossíntese
Cerebelo/metabolismo
Células de Purkinje/metabolismo
[Mh] Termos MeSH secundário: Animais
Animais Recém-Nascidos
Proteínas de Transporte/genética
Cerebelo/crescimento & desenvolvimento
Cerebelo/ultraestrutura
Feminino
Regulação da Expressão Gênica no Desenvolvimento/fisiologia
Imuno-Histoquímica
Masculino
Proteínas de Membrana
Globulina de Ligação a Progesterona/biossíntese
Globulina de Ligação a Progesterona/genética
Células de Purkinje/ultraestrutura
RNA Mensageiro/biossíntese
RNA Mensageiro/genética
Ratos
Ratos Endogâmicos F344
Receptores de Progesterona
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (Membrane Proteins); 0 (Pgrmc1 protein, rat); 0 (Progesterone-Binding Globulin); 0 (RNA, Messenger); 0 (Receptors, Progesterone)
[Em] Mês de entrada:0408
[Cu] Atualização por classe:111117
[Lr] Data última revisão:
111117
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:040623
[St] Status:MEDLINE


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[PMID]:15033482
[Au] Autor:Leel V; Elrick LJ; Solares J; Ingram N; Charlton KA; Porter AJ; Wright MC
[Ad] Endereço:Department of Molecular and Cell Biology, Institute of Medical Sciences, University of Aberdeen, Aberdeen, UK.
[Ti] Título:Identification of a truncated ratp28-related protein expressed in kidney.
[So] Source:Biochem Biophys Res Commun;316(3):872-7, 2004 Apr 09.
[Is] ISSN:0006-291X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:An RT-PCR based strategy to clone the membrane-associated steroid binding protein ratp28 additionally amplified a novel sequence-related PCR product termed HC5. The HC5 PCR product was cloned and sequenced and showed 94% nucleotide sequence similarity to ratp28. The HC5 cDNA sequence open reading frame encodes a predicted 75 amino acid (8.0kDa) protein, and is therefore truncated compared to ratp28 (195 amino acids, 21.6kDa). In vitro transcription and translation of the HC5 cDNA resulted in the production of 2 proteins of approximately 8 and 6kDa. Restriction digests from various tissues demonstrated that liver and heart expressed primarily ratp28 mRNA whereas kidney and blood contained both ratp28 and HC5 transcripts. Phage display was employed to generate an antibody fragment to a peptide sequence conserved in ratp28 and HC5. Western blotting identified a 10kDa protein in cytosolic fractions of rat kidney. The function of HC5 remains to be determined.
[Mh] Termos MeSH primário: Proteínas de Transporte/química
Rim/metabolismo
Proteínas de Membrana/biossíntese
Proteínas de Membrana/química
Globulina de Ligação a Progesterona/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Sequência de Bases
Western Blotting
Proteínas de Transporte/biossíntese
Clonagem Molecular
Sequência Conservada
Citosol/metabolismo
DNA Complementar/metabolismo
Ensaio de Imunoadsorção Enzimática
Masculino
Microssomos/metabolismo
Dados de Sequência Molecular
Fases de Leitura Aberta
Biblioteca de Peptídeos
Peptídeos/química
Perfusão
Plasmídeos/metabolismo
Ligação Proteica
Biossíntese de Proteínas
RNA Mensageiro/metabolismo
Ratos
Ratos Sprague-Dawley
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Homologia de Sequência de Aminoácidos
Homologia de Sequência do Ácido Nucleico
Distribuição Tecidual
Transcrição Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (DNA, Complementary); 0 (HC5 protein, rat); 0 (Membrane Proteins); 0 (Peptide Library); 0 (Peptides); 0 (Progesterone-Binding Globulin); 0 (RNA, Messenger); 0 (Ratp28 protein, rat)
[Em] Mês de entrada:0405
[Cu] Atualização por classe:061115
[Lr] Data última revisão:
061115
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:040323
[St] Status:MEDLINE


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[PMID]:12493703
[Au] Autor:Peluso JJ; Bremner T; Fernandez G; Pappalardo A; White BA
[Ad] Endereço:Department of Physiology, University of Connecticut Health Center, Farmington, Connecticut 06030, USA. peluso@nso2.uchc.edu
[Ti] Título:Expression pattern and role of a 60-kilodalton progesterone binding protein in regulating granulosa cell apoptosis: involvement of the mitogen-activated protein kinase cascade.
[So] Source:Biol Reprod;68(1):122-8, 2003 Jan.
[Is] ISSN:0006-3363
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Progesterone (P4) inhibits both granulosa cells and spontaneously immortalized granulosa cells (SIGCs) from undergoing apoptosis. P4 does so through a plasma membrane-initiated event. It appears that P4's membrane-initiated actions are mediated by a 60-kDa P4 binding protein (P4BP), which is detected by an antibody directed against the ligand binding domain of the nuclear P4 receptor (i.e., C-262). Immunohistochemical analysis revealed that a C-262-detectable protein was first observed in the periphery of a few granulosa cells within early antral-stage follicles. In nonatretic antral follicles, this protein was detected at the periphery of virtually all granulosa cells. In contrast, granulosa cells of atretic follicles lost the distinct peripheral localization of this C-262-detectable protein. This reduction in the membrane localization was also observed by Western blot analysis. To assess the temporal changes in this 60-kDa P4BP during apoptosis, studies were conducted using SIGCs. That this 60-kDa protein is important in mediating P4's action was confirmed by the observation that C-262 but not IgG attenuated P4's antiapoptotic action. Interestingly, the membrane localization of this 60-kDa P4BP was maintained but the ability of P4 to prevent apoptosis was lost within 20 min of initiating the apoptotic cascade. In addition, Erk-1 and -2 phosphorylation (i.e., activity) increased within 20 min of P4 withdrawal. Further, P4 suppressed the increase in the Erk-1 phosphorylation if administered within 5 but not 20 min of initiating the apoptotic cascade. Moreover, the mitogen-activated protein kinase kinase (MEK) inhibitor, PD98059, reduced the percentage of SIGCs undergoing apoptosis in the absence of P4. Because MEK phosphorylates Erk, these observations suggests that 1) the increase in Erk-1 activity is an important part of the apoptotic cascade, 2) P4 promotes granulosa cell viability by modulating the activity of Erk-1, and 3) P4 becomes "uncoupled" from its antiapoptotic signal transduction mechanism within 20 min of initiating apoptosis, even though the membrane localization of the 60-kDa P4BP is maintained.
[Mh] Termos MeSH primário: Apoptose/fisiologia
Células da Granulosa/citologia
Células da Granulosa/metabolismo
Sistema de Sinalização das MAP Quinases
Globulina de Ligação a Progesterona/metabolismo
[Mh] Termos MeSH secundário: Animais
Apoptose/efeitos dos fármacos
Inibidores Enzimáticos/farmacologia
Feminino
Flavonoides/farmacologia
Células da Granulosa/efeitos dos fármacos
MAP Quinase Quinase 1
MAP Quinase Quinase 2
Sistema de Sinalização das MAP Quinases/efeitos dos fármacos
Proteína Quinase 1 Ativada por Mitógeno/antagonistas & inibidores
Proteína Quinase 1 Ativada por Mitógeno/metabolismo
Proteína Quinase 3 Ativada por Mitógeno
Quinases de Proteína Quinase Ativadas por Mitógeno/antagonistas & inibidores
Quinases de Proteína Quinase Ativadas por Mitógeno/metabolismo
Proteínas Quinases Ativadas por Mitógeno/antagonistas & inibidores
Proteínas Quinases Ativadas por Mitógeno/metabolismo
Peso Molecular
Progesterona/metabolismo
Progesterona/farmacologia
Globulina de Ligação a Progesterona/química
Proteínas Serina-Treonina Quinases/antagonistas & inibidores
Proteínas Serina-Treonina Quinases/metabolismo
Proteínas Tirosina Quinases/antagonistas & inibidores
Proteínas Tirosina Quinases/metabolismo
Ratos
Ratos Wistar
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, P.H.S.
[Nm] Nome de substância:
0 (2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one); 0 (Enzyme Inhibitors); 0 (Flavonoids); 0 (Progesterone-Binding Globulin); 4G7DS2Q64Y (Progesterone); EC 2.7.10.1 (Protein-Tyrosine Kinases); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 2.7.11.24 (Mitogen-Activated Protein Kinase 1); EC 2.7.11.24 (Mitogen-Activated Protein Kinase 3); EC 2.7.11.24 (Mitogen-Activated Protein Kinases); EC 2.7.12.2 (MAP Kinase Kinase 1); EC 2.7.12.2 (MAP Kinase Kinase 2); EC 2.7.12.2 (Mitogen-Activated Protein Kinase Kinases)
[Em] Mês de entrada:0308
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:021221
[St] Status:MEDLINE


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[PMID]:10630418
[Au] Autor:Buddhikot M; Falkenstein E; Wehling M; Meizel S
[Ad] Endereço:Department of Cell Biology and Human Anatomy, University of California, School of Medicine, Davis 95616-8643, USA.
[Ti] Título:Recognition of a human sperm surface protein involved in the progesterone-initiated acrosome reaction by antisera against an endomembrane progesterone binding protein from porcine liver.
[So] Source:Mol Cell Endocrinol;158(1-2):187-93, 1999 Dec 20.
[Is] ISSN:0303-7207
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:Antisera against a porcine liver endomembrane progesterone (P4)-binding protein inhibited the P4-initiated acrosome reaction (AR) but not the ionomycin-initiated AR of human sperm. Indirect immunofluorescence studies detected antigen in the sperm head that moved during capacitation from a posterior head region to a midhead region. Moreover, the antisera detected a 44.6 kDa protein in western blots of sperm digitonin extracts. These results suggest that a sperm protein with at least partial homology to the liver endomembrane P4-binding protein, is a putative P4-receptor on the sperm plasma membrane involved in the P4-initiated AR.
[Mh] Termos MeSH primário: Proteínas de Membrana/metabolismo
Globulina de Ligação a Progesterona/metabolismo
Progesterona/metabolismo
Cabeça do Espermatozoide/metabolismo
Espermatozoides/metabolismo
[Mh] Termos MeSH secundário: Reação Acrossômica/fisiologia
Animais
Western Blotting
Imunofluorescência
Seres Humanos
Soros Imunes
Fígado/metabolismo
Masculino
Proteínas de Membrana/imunologia
Globulina de Ligação a Progesterona/imunologia
Capacitação Espermática/fisiologia
Suínos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, P.H.S.
[Nm] Nome de substância:
0 (Immune Sera); 0 (Membrane Proteins); 0 (Progesterone-Binding Globulin); 4G7DS2Q64Y (Progesterone)
[Em] Mês de entrada:0002
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:000112
[St] Status:MEDLINE


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[PMID]:10359327
[Au] Autor:Cenedella RJ; Sexton PS; Zhu XL
[Ad] Endereço:Department of Biochemistry, Kirksville College of Osteopathic Medicine, Missouri 63501, USA.
[Ti] Título:Lens epithelia contain a high-affinity, membrane steroid hormone-binding protein.
[So] Source:Invest Ophthalmol Vis Sci;40(7):1452-9, 1999 Jun.
[Is] ISSN:0146-0404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:PURPOSE: To describe the serendipitous discovery of a high-affinity, membrane steroid-binding protein (MSBP) in lens epithelial cells and to examine the binding of progesterone to epithelial cell membranes. METHODS: Bovine lens epithelial cells (BLECs) were cultured in media containing 3H-mevalonolactone to examine protein prenylation by mevalonate-derived isoprenes. Cell proteins were divided into insoluble and soluble fractions, separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and label detected by fluorography. Insoluble proteins were then fractionated on a C18 reversed-phase column. A high-performance liquid chromatography fraction containing a 28kDa 3H-labeled hydrophobic protein was collected, lyophilized, and subjected to SDS-PAGE and the separated proteins transferred to membrane. Protein in the recovered 28-kDa band was submitted for identification by N-terminal sequence analysis. Microsomal membranes prepared from fresh epithelia of intact bovine, rat, and human lens and cultured BLECs were tested for the presence of MSBP by western blot analysis using an antiserum to porcine liver microsomal MSBP. Radiolabeling of MSBP from 3H-mevalonate was confirmed by immunoprecipitation using the same antiserum. 3H-Progesterone was incubated with microsomal membrane from bovine lens epithelia to measure high-affinity binding. Radiolabeled progesterone-protein complexes were trapped on glass filters and radioactivity measured and the binding data subjected to Scatchard analysis. RESULTS: Membrane recovered from BLECs incubated with 3H-mevalonolactone contained a 3H-labeled 28-kDa protein fraction. The N-terminal sequence of the principal protein in this fraction was very similar to that of the recently discovered MSBP. Western blot analysis with antiserum to MSBP indicated the presence of the 28-kDa protein in the microsomal fraction from BLECs and epithelia of bovine, rat, and young human lenses but not in lens fiber cell membrane. Microsomal membrane from intact bovine lens epithelium bound progesterone with high affinity, with disso ciation constant (Kd) at approximately 75 nM and a receptor concentration of approximately 3 picomoles/mg protein. CONCLUSIONS: The lens epithelium contains a 28-kDa membrane protein that can bind progesterone and perhaps other steroid hormones with high affinity. The protein appears to be microsomal and prenylated. The MBSP may mediate rapid nongenomic steroid effects that contribute to steroid-induced cataracts.
[Mh] Termos MeSH primário: Células Epiteliais/metabolismo
Cristalino/metabolismo
Globulina de Ligação a Progesterona/metabolismo
[Mh] Termos MeSH secundário: Adolescente
Animais
Western Blotting
Bovinos
Membrana Celular/metabolismo
Células Cultivadas
Eletroforese em Gel de Poliacrilamida
Células Epiteliais/efeitos dos fármacos
Seres Humanos
Cristalino/efeitos dos fármacos
Ácido Mevalônico/análogos & derivados
Ácido Mevalônico/farmacologia
Microssomos/metabolismo
Microssomos Hepáticos/metabolismo
Peso Molecular
Progesterona/metabolismo
Prenilação de Proteína
Ratos
Ratos Sprague-Dawley
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, P.H.S.
[Nm] Nome de substância:
0 (Progesterone-Binding Globulin); 4G7DS2Q64Y (Progesterone); 661X270Z3L (mevalonolactone); S5UOB36OCZ (Mevalonic Acid)
[Em] Mês de entrada:9906
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:990608
[St] Status:MEDLINE


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[PMID]:10323684
[Au] Autor:Blackmore PF
[Ad] Endereço:Eastern Virginia Medical School, Department of Physiological Sciences, Norfolk 23507, USA. blackmore@evms.edu
[Ti] Título:Extragenomic actions of progesterone in human sperm and progesterone metabolites in human platelets.
[So] Source:Steroids;64(1-2):149-56, 1999 Jan-Feb.
[Is] ISSN:0039-128X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Progesterone rapidly increased intracellular free calcium ([Ca2+]i) in human sperm, removal of extracellular Ca2+ prevented the increase in [Ca2+]i. The Ca2+ influx was not blocked by the T-type Ca2+ channel blocker mibefradil. However T-type calcium channels do appear to be present in human sperm because the neoglycoprotein mannose-albumin, an inducer of the acrosome reaction, was able to promote Ca2+ influx, which was blocked by mibefradil and more potently inhibited by Ni2+ than Cd2+. The receptor for progesterone that promotes the Ca2+ influx was located on the plasma membrane using FITC-progesterone-albumin. It is concluded that progesterone stimulates Ca2+ influx in human sperm via a unique Ca2+ channel possibly similar to a store-operated channel (SOC) or a receptor-operated channel (ROC). We have found that progesterone metabolites, such as pregnanolone and pregnanediol, promote a rapid rise in [Ca2+]i and aggregation in human platelets, similar to that observed with thrombin. The increase in [Ca2+]i was prevented when extracellular Ca2+ was removed or by the SOC inhibitor SKF-96365. The phospholipase C inhibitor U-73122 also prevented the increase in [Ca2+]i, suggesting that these metabolites interact with a cell surface receptor on the platelet to activate phospholipase C to produce inositol-P3, which mobilizes intracellular Ca2+, thereby activating the SOC in the plasma membrane. Progesterone and estradiol conjugated to albumin, also produced a rapid increase in [Ca2+]i, which was prevented by Ca2+ removal from the medium or when SKF-96365 or U-73122 were added. It is proposed that human platelets possess cell surface receptors for steroids.
[Mh] Termos MeSH primário: Plaquetas/metabolismo
Progesterona/fisiologia
Espermatozoides/fisiologia
[Mh] Termos MeSH secundário: Cálcio/sangue
Canais de Cálcio/metabolismo
Estrogênios/metabolismo
Seres Humanos
Masculino
Progesterona/metabolismo
Globulina de Ligação a Progesterona/metabolismo
Ligação Proteica
Albumina Sérica/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Calcium Channels); 0 (Estrogens); 0 (Progesterone-Binding Globulin); 0 (Serum Albumin); 4G7DS2Q64Y (Progesterone); SY7Q814VUP (Calcium)
[Em] Mês de entrada:9906
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:990514
[St] Status:MEDLINE


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[PMID]:9836376
[Au] Autor:Müller B; Gimsa U; Mitchison NA; Radbruch A; Sieper J; Yin Z
[Ad] Endereço:Deutsches Rheuma Forschungs Zentrum, Berlin, Germany.
[Ti] Título:Modulating the Th1/Th2 balance in inflammatory arthritis.
[So] Source:Springer Semin Immunopathol;20(1-2):181-96, 1998.
[Is] ISSN:0344-4325
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:The balance between Th1 and Th2 cells regulates the choice between inflammatory and antibody-mediated immune responses. To an increasing extent this balance is thought to involve the participation of antigen-presenting cells, rather than the entirely autonomous activity of T cells and their cytokines. Here we survey current opinion concerning the working of this balance, and its condition in rheumatoid arthritis and the other inflammatory arthritides. The contrast between Lyme arthritis and reactive arthritis is particularly illuminating, since one is triggered by extracellular and the other by intracellular infection. We describe current approaches to the modulation of this balance. Guided by the principles that genetic polymorphism is likely to identify relevant genes, that any cytokine gene picked up by a virus must matter and that natural immunosuppressive activity at mucosal surfaces should be worth exploiting, we identify as particularly worthy of attention: (i) IL-10, (ii) inhibitors of IL-12 production, (iii) inhibitors of CD40 ligand expression and (iv) oral and nasal tolerance. Other protective T cell subsets are touched on, and the impact of oligonucleotide arrays mentioned.
[Mh] Termos MeSH primário: Artrite/imunologia
Células Th1/fisiologia
Células Th2/fisiologia
[Mh] Termos MeSH secundário: Animais
Artrite/prevenção & controle
Artrite Infecciosa/imunologia
Artrite Reativa/imunologia
Artrite Reumatoide/imunologia
Biomarcadores
Antígenos CD40/imunologia
Feminino
Seres Humanos
Tolerância Imunológica
Interleucina-10/imunologia
Interleucina-12/imunologia
Interleucina-12/farmacologia
Doença de Lyme/imunologia
Camundongos
Mucosa Bucal/imunologia
Mucosa Nasal/imunologia
Gravidez
Globulina de Ligação a Progesterona/imunologia
Globulina de Ligação a Hormônio Sexual/imunologia
Células Th1/efeitos dos fármacos
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, P.H.S.; REVIEW
[Nm] Nome de substância:
0 (Biomarkers); 0 (CD40 Antigens); 0 (Progesterone-Binding Globulin); 0 (Sex Hormone-Binding Globulin); 130068-27-8 (Interleukin-10); 187348-17-0 (Interleukin-12)
[Em] Mês de entrada:9902
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM; X
[Da] Data de entrada para processamento:981204
[St] Status:MEDLINE


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Fotocópia
[PMID]:9678891
[Au] Autor:Falkenstein E; Schmieding K; Lange A; Meyer C; Gerdes D; Welsch U; Wehling M
[Ad] Endereço:Institute of Clinical Pharmacology, Faculty for Clinical Medicine at Mannheim, University of Heidelberg, Germany.
[Ti] Título:Localization of a putative progesterone membrane binding protein in porcine hepatocytes.
[So] Source:Cell Mol Biol (Noisy-le-grand);44(4):571-8, 1998 Jun.
[Is] ISSN:0145-5680
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:A putative membrane bound steroid receptor was localized using a peptide specific antibody. Surprisingly, the distribution of immunocytochemical staining in porcine hepatocytes cells provides evidence for the localization to endomembranes (endoplasmic reticulum, Golgi apparatus). Immunofluorescence experiments with HEK cells, which were transfected with a pcDNA3.1 vector containing the coding sequence of the putative progesterone binding protein shows staining within the cells supporting these results. Additionally, 3H-progesterone binding and glucose-6-phosphatase activity as marker enzyme for endoplasmic reticulum were closely correlated in subcellular fractions of porcine liver cells.
[Mh] Termos MeSH primário: Fígado/metabolismo
Proteínas de Membrana/metabolismo
Globulina de Ligação a Progesterona/metabolismo
[Mh] Termos MeSH secundário: Animais
Western Blotting
Eletroforese em Gel de Poliacrilamida
Retículo Endoplasmático/metabolismo
Técnica Indireta de Fluorescência para Anticorpo
Glucose-6-Fosfatase/metabolismo
Seres Humanos
Imuno-Histoquímica
Progesterona/metabolismo
Globulina de Ligação a Progesterona/genética
Frações Subcelulares
Suínos
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Membrane Proteins); 0 (Progesterone-Binding Globulin); 4G7DS2Q64Y (Progesterone); EC 3.1.3.9 (Glucose-6-Phosphatase)
[Em] Mês de entrada:9810
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:980725
[St] Status:MEDLINE



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