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1.
Biochim Biophys Acta ; 1445(3): 257-70, 1999 Jun 09.
Artigo em Inglês | MEDLINE | ID: mdl-10366710

RESUMO

The human 5T4 oncotrophoblast leucine-rich glycoprotein may contribute to the process of placentation or metastasis by modulating cell adhesion, shape and motility. To understand better the role of 5T4 in development and cancer, the gene structure has been elucidated from both human and mouse genomic clones and mRNA expression has been studied in foetal and adult mouse tissues. The protein coding region is located within the second of two exons, the first exon comprising solely of 5'-untranslated region. Upstream there are no TATA or CAAT boxes, but there are a number of potential Sp1 binding sites. The murine and human proteins show a homologous domain organisation of the leucine rich repeats (LRR) and associated N- and C-terminal flanking regions, although the hydrophilic sequence which intervenes between the two LRR domains contains six additional amino acids in the mouse. The signal peptide, transmembrane region and cytoplasmic tail sequences are identical as are 6 out of the 7 potential N-linked glycosylation sites. Mouse 5T4 transcripts are abundant in placenta and also highly expressed in embryos while in adult tissues transcripts are restricted to brain and ovary. These patterns of expression and the genomic organisation are discussed in relation to possible function and other recently described LRR containing proteins.


Assuntos
Embrião de Mamíferos/metabolismo , Glicoproteínas de Membrana/genética , Placenta/metabolismo , Proteínas da Gravidez/genética , Sequência de Aminoácidos , Animais , Sequência de Bases , DNA Complementar/química , Biblioteca Gênica , Humanos , Glicoproteínas de Membrana/metabolismo , Camundongos , Dados de Sequência Molecular , Reação em Cadeia da Polimerase/métodos , RNA Mensageiro/metabolismo , Homologia de Sequência do Ácido Nucleico
2.
FEMS Microbiol Lett ; 154(2): 283-8, 1997 Sep 15.
Artigo em Inglês | MEDLINE | ID: mdl-9311126

RESUMO

The mechanism by which chlorhexidine kills bacteria is still ill defined. We have investigated the action of chlorhexidine on Escherichia coli JM101/psb311 using a combination of flow cytometry and traditional methods. Chlorhexidine-induced uptake by E. coli cells of bis-(1,3-dibutylbarturic acid) trimethine oxonol and propidium iodide, which monitor membrane potential and membrane integrity respectively, was shown to be concentration dependent for the range 0.003-0.3 mmol-1. In addition, cells in log phase growth were more susceptible to 0.03 mmol-1 chlorhexidine than those in stationary phase. There was, however, no direct correlation between dye uptake and decline in colony forming units.


Assuntos
Anti-Infecciosos Locais/farmacologia , Clorexidina/farmacologia , Escherichia coli/efeitos dos fármacos , Membrana Celular/efeitos dos fármacos , Citometria de Fluxo , Fluorescência , Luz , Espalhamento de Radiação
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