Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 3 de 3
Filtrar
Mais filtros











Base de dados
Tipo de estudo
Intervalo de ano de publicação
1.
Arch Pediatr ; 31(6): 353-356, 2024 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-39003158

RESUMO

A large proportion of prescriptions for extensively hydrolyzed cow's milk protein (CMP) in newborns are not based on any scientific data justifying the indication. Many of these prescriptions are old habits or are based on incomplete data. The aim of this article is to analyze these practices and propose recommendations. The following points are covered: (a) indications for extensively hydrolyzed formula based on studies demonstrating their benefits in these situations-newborns with a proven allergy to CMP and occasional prescription of supplements to breastfeeding; (b) possible indications not based on a high level of evidence-re-initiation of feeding due to necrotizing enterocolitis, short bowel syndrome, re-initiation of feeding of newborns following intestinal surgery, and laparoschisis if neither the mother's own milk nor milk from a lactarium is available; (c) unjustified indications-newborns at risk of atopy, prematurity, severe neurological pathologies, newborns who are hemodynamically unstable and/or have congenital cardiopathy, neonatal hypoxic-ischemic encephalopathy treated with hypothermia, and newborns with esophageal atresia or diaphragmatic hernia. By following this classification, the prescriber will be guided to use the milk best suited to the pathology, bearing in mind that each situation must be adapted individually and the tolerance and effectiveness of the food reassessed from a nutritional and functional point of view.


Assuntos
Fórmulas Infantis , Hipersensibilidade a Leite , Proteínas do Leite , Animais , Bovinos , Humanos , Recém-Nascido , Enterocolite Necrosante/prevenção & controle , Proteínas do Leite/imunologia , Proteínas do Leite/efeitos adversos , Hidrolisados de Proteína/administração & dosagem
2.
European J Pediatr Surg Rep ; 7(1): e16-e19, 2019 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-31192106

RESUMO

Infantile fibrosarcoma (IFS) is a rare nonrhabdomyosarcoma soft tissue tumor and accounts for less than 1% of childhood cancers. Forty per cent are present at birth and only 10% of IFS occurs in the abdomen. Our case of neonatal fibrosarcoma presented as a distal small bowel stenosis complicated with meconium peritonitis. The diagnosis was by histology of the surgical resection. The diagnosis of IFS is challenging as there are no specific features of IFS on imaging. Any unexpected solid lesion should raise the suspicion of complicated bowel tumoral lesion. If a neoplastic lesion is suspected extensive, surgery may be postponed until the final diagnosis is made.

3.
Artigo em Inglês | MEDLINE | ID: mdl-28069656

RESUMO

The metallo-ß-lactamase NDM-1 is among the most worrisome resistance determinants and is spreading worldwide among Gram-negative bacilli. A bleomycin resistance gene, bleMBL, downstream of the blaNDM-1 gene has been associated with resistance almost systematically. Here, we characterized the corresponding protein, BRPMBL, conferring resistance to bleomycin, an antitumoral glycopeptide molecule. We have determined whether the expression of the blaNDM-1-bleMBL operon is inducible in the presence of carbapenems and/or bleomycin-like molecules using quantitative reverse transcription-PCR (qRT-PCR), determination of imipenem and zeocin MICs, and carbapenemase-specific activity assays. We showed that the blaNDM-1-bleMBL operon is constitutively expressed. Using electrophoretic mobility shift and DNA protection assays performed with purified glutathione S-transferase (GST)-BRPMBL, we demonstrated that BRPMBL is able to bind and sequester bleomycin-like molecules, thus preventing bleomycin-dependent DNA degradation. In silico modeling confirmed that the mechanism of action required the dimerization of the BRPMBL protein in order to sequester bleomycin and prevent DNA damage. BRPMBL acts specifically on bleomycin-like molecules since cloning and expression of bleMBL in Staphyloccoccus aureus did not confer cross-resistance to any other antimicrobial glycopeptides such as vancomycin and teicoplanin.


Assuntos
Antibacterianos/metabolismo , Proteínas de Bactérias/genética , Bleomicina/metabolismo , Farmacorresistência Bacteriana/genética , Escherichia coli/genética , Regulação Bacteriana da Expressão Gênica , Klebsiella pneumoniae/genética , beta-Lactamases/genética , Sequência de Aminoácidos , Antibacterianos/química , Antibacterianos/farmacologia , Proteínas de Bactérias/química , Proteínas de Bactérias/metabolismo , Sítios de Ligação , Bleomicina/química , Bleomicina/farmacologia , Escherichia coli/efeitos dos fármacos , Escherichia coli/crescimento & desenvolvimento , Escherichia coli/metabolismo , Imipenem/farmacologia , Klebsiella pneumoniae/efeitos dos fármacos , Klebsiella pneumoniae/crescimento & desenvolvimento , Klebsiella pneumoniae/metabolismo , Modelos Moleculares , Óperon , Plasmídeos/química , Plasmídeos/metabolismo , Ligação Proteica , Conformação Proteica em alfa-Hélice , Conformação Proteica em Folha beta , Domínios e Motivos de Interação entre Proteínas , Proteínas Recombinantes de Fusão/química , Proteínas Recombinantes de Fusão/genética , Proteínas Recombinantes de Fusão/metabolismo , Alinhamento de Sequência , Especificidade por Substrato , beta-Lactamases/química , beta-Lactamases/metabolismo
SELEÇÃO DE REFERÊNCIAS
DETALHE DA PESQUISA