RESUMO
A novel heterometallic metal-porphyrinic framework (MPFs) built from Y and K ions as nods and meso-tetra(4-carboxyphenyl)porphyrin as linkers has been successfully synthesized and characterized. The single crystal X-ray diffraction indicated that this complex 1 exhibited a bilayered architecture of the porphyrins, which is seldom seen in MPFs. In addition, in vitro anticancer activity of complex 1 on three human breast cancer cells (BT474, SKBr-3 and ZR-75-30) was further determined.
Assuntos
Humanos , Porfirinas/química , Neoplasias da Mama/tratamento farmacológico , Estruturas Metalorgânicas/farmacologia , Estruturas Metalorgânicas/química , Antineoplásicos/farmacologia , Antineoplásicos/química , Valores de Referência , Sais de Tetrazólio , Reprodutibilidade dos Testes , Cristalografia por Raios X , Linhagem Celular Tumoral , Complexos de Coordenação/farmacologia , Complexos de Coordenação/química , FormazansRESUMO
The intestinal lymph pathway plays an important role in the pathogenesis of organ injury following superior mesenteric artery occlusion (SMAO) shock. We hypothesized that mesenteric lymph reperfusion (MLR) is a major cause of spleen injury after SMAO shock. To test this hypothesis, SMAO shock was induced in Wistar rats by clamping the superior mesenteric artery (SMA) for 1 h, followed by reperfusion for 2 h. Similarly, MLR was performed by clamping the mesenteric lymph duct (MLD) for 1 h, followed by reperfusion for 2 h. In the MLR+SMAO group rats, both the SMA and MLD were clamped and then released for reperfusion for 2 h. SMAO shock alone elicited: 1) splenic structure injury, 2) increased levels of malondialdehyde, nitric oxide (NO), intercellular adhesion molecule-1, endotoxin, lipopolysaccharide receptor (CD14), lipopolysaccharide-binding protein, and tumor necrosis factor-α, 3) enhanced activities of NO synthase and myeloperoxidase, and 4) decreased activities of superoxide dismutase and ATPase. MLR following SMAO shock further aggravated these deleterious effects. We conclude that MLR exacerbates spleen injury caused by SMAO shock, which itself is associated with oxidative stress, excessive release of NO, recruitment of polymorphonuclear neutrophils, endotoxin translocation, and enhanced inflammatory responses.
Assuntos
Animais , Masculino , Linfa/metabolismo , Oclusão Vascular Mesentérica/complicações , Traumatismo por Reperfusão/etiologia , Reperfusão/efeitos adversos , Baço/lesões , Proteínas de Fase Aguda/análise , Adenosina Trifosfatases/análise , /análise , Proteínas de Transporte/análise , Endotoxinas/análise , Molécula 1 de Adesão Intercelular/análise , Intestinos/irrigação sanguínea , Artéria Mesentérica Superior , Malondialdeído/análise , Glicoproteínas de Membrana/análise , Óxido Nítrico Sintase/análise , Óxido Nítrico/análise , Peroxidase/análise , Ratos Wistar , Baço/patologia , Superóxido Dismutase/análise , Fator de Necrose Tumoral alfa/análiseRESUMO
Notch signaling is an evolutionarily ancient, highly conserved pathway important for deciding cell fate, cellular development, differentiation, proliferation, apoptosis, adhesion, and epithelial-to-mesenchymal transition. Notch signaling is also critical in mammalian cardiogenesis, as mutations in this signaling pathway are linked to human congenital heart disease. Furthermore, Notch signaling can repair myocardial injury by promoting myocardial regeneration, protecting ischemic myocardium, inducing angiogenesis, and negatively regulating cardiac fibroblast-myofibroblast transformation. This review provides an update on the known roles of Notch signaling in the mammalian heart. The goal is to assist in developing strategies to influence Notch signaling and optimize myocardial injury repair.