Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 5 de 5
Filtrar
Mais filtros










Base de dados
Intervalo de ano de publicação
1.
J Small Anim Pract ; 60(5): 280-290, 2019 May.
Artigo em Inglês | MEDLINE | ID: mdl-30684356

RESUMO

OBJECTIVES: To report clinical and laboratory features, treatment responses and outcome in dogs diagnosed with sterile steroid-responsive lymphadenitis in the United Kingdom. MATERIALS AND METHODS: Medical records of dogs diagnosed with sterile steroid-responsive lymphadenitis from 2009 to 2016 at six specialist referral centres were evaluated retrospectively. RESULTS: The study included 49 dogs. Springer spaniels appeared to be over-represented (16 of 49 dogs). Young dogs (median age: 3 years and 9 months) and females (31 of 49) were frequently affected. Clinical presentation was variable, with pyrexia (39 of 49), lethargy (35 of 49) and anorexia (21 of 49) the most commonly reported clinical signs. Lymph node cytology or histopathology demonstrated neutrophilic, pyogranulomatous, granulomatous or necrotising lymphadenitis without a detectable underlying cause in all cases. Because a sterile immune-mediated aetiology was suspected, all dogs received prednisolone, which was followed by rapid resolution of clinical signs and lymphadenopathy in most cases. CLINICAL SIGNIFICANCE: Sterile steroid-responsive lymphadenitis should be considered in dogs with pyrexia of unknown origin with inflammatory lymphadenopathy if no underlying cause can be found and often responds well to immunosuppressive corticosteroid therapy.


Assuntos
Doenças do Cão , Linfadenite/veterinária , Animais , Cães , Feminino , Prednisolona , Estudos Retrospectivos , Reino Unido
2.
J Bacteriol ; 152(2): 848-54, 1982 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-6752120

RESUMO

Escherichia coli K-12 strains contain a cytoplasmic activity, peptidase N, capable of hydrolyzing alanine-p-nitroanilide. Mutations in the structural gene for the enzyme, pepN, were mapped, and the properties of mutant strains were examined. The pepN locus lay between ompF and asnS at approximately 20.8 min on the E. coli chromosome. Loss of peptidase N activity through mutation had no apparent effect on the growth rate or nutritional needs of the cell. Enzyme levels in wild-type strains were constant throughout the growth cycle and were constitutive in all of the growth media tested. Starvation for carbon, nitrogen, or phosphate also did not alter enzyme levels. Constitutive expression of peptidase N is consistent with the idea that the enzyme plays a significant role in the degradation of intracellularly generated peptides.


Assuntos
Aminopeptidases/genética , Escherichia coli/enzimologia , Genes , Escherichia coli/efeitos dos fármacos , Escherichia coli/genética , Genes/efeitos dos fármacos , Genótipo , Mutagênicos/farmacologia , Mutação , Especificidade da Espécie , Ésteres do Ácido Sulfúrico/farmacologia
5.
J Bacteriol ; 128(2): 557-72, 1976 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-789357

RESUMO

Two different mutational events generate promoter-active deoxyribonucleic acid sequences within the trp operon of Escherichia coli, probably through single base-pair changes. The mutations, obtained after ethyl methane sulfonate mutagenesis by selecting for elevated lac gene expression in a trp-lac fusion, are cis dominant and trans recessive with respect to their effects on the synthesis of downstream enzymes. One of the mutants (trpD11), obtained repeatedly under the selective conditions employed, prevents the formation of active phosphoribosyltransferase. The second mutation, trp3B, has no effects on any trp enzyme. By deletion mapping, trpD11 was localized near the operator-distal end of trpD, outside the segment of deoxyribonucleic acid that contains the low-efficiency internal promoter trpP2. Reversion to prototrophy of trpD11 was greatly stimulated by 2-aminopurine and ethyl methane sulfonate. Tests with suppressors indicated that trpD11 is a UAA (ochre) nonsense mutation. Under repression conditions, strains harboring either lesion in a normal trp operon synthesize the tryptophan biosynthetic enzymes in a noncoordinate fashion. The products of the operator-distal structural genes trpC, trpB, and trpA are formed at rates approximately 15-fold higher than those of wild type. The enzymes encoded by operator-proximal genes trpE and trpD are low or not detectable. Under derepression conditions, coordinate expression of the operon was observed.


Assuntos
Escherichia coli/metabolismo , Óperon , Transcrição Gênica , Triptofano/biossíntese , Alelos , Antranilato Fosforribosiltransferase/biossíntese , Antranilato Sintase/biossíntese , Mapeamento Cromossômico , Cromossomos Bacterianos , Escherichia coli/enzimologia , Galactosidases/metabolismo , Teste de Complementação Genética , Ligação Genética , Mutação , Recombinação Genética , Transdução Genética , Triptofano/análogos & derivados , Triptofano/farmacologia , Triptofano Sintase/biossíntese
SELEÇÃO DE REFERÊNCIAS
DETALHE DA PESQUISA
...