RESUMEN
BACKGROUND: Thirst is a very common symptom in fasted children in intensive care unit (ICU). This study aimed to evaluate the effect of sterile ice water versus menthol spray in ICU fasted children, to provide insights to the clinical care of fasted children. METHODS: The children admitted to the ICU of our hospital from June 1, 2021 to August 31, 2022 and needed to fast were included. Children were randomly assigned to the ice water group or menthol group. We evaluated and compared the thirst distress scale (TDS), oral mucosa wetness scale (OMWS), children medical fear scale (CMFS), numerical rating scale (NRS), unstimulated whole saliva (UWS) flow rate between 2 groups. RESULTS: A total of 139 children were included, involving 69 children in ice water group and 70 children in menthol group. There were no significant differences in the baseline characteristics, TDS, OMWS, OMWS, CMFS, and NRS score, UWS flow rate before intervention between ice water group and menthol group (all P > .05). After intervention, the TDS, OMWS, NRS score of menthol group was statistically less than that of ice water group (all P < .05), the UWS flow rate of menthol group was statistically higher than that of ice water group (P = .034). CONCLUSIONS: Compared with ice water spray, menthol spray may be more beneficial to relieve the thirst and increase the comfort in ICU fasted children. Future studies with larger sample size and rigorous design are needed to evaluate the effects and safety of ice water and menthol spray in the nursing care of children.
Asunto(s)
Mentol , Sed , Humanos , Niño , Estudios Prospectivos , Unidades de Cuidados Intensivos , AguaRESUMEN
Objective: Obesity caused by a high-fat diet (HFD) will expand adipose tissue and cause chronic low-grade systemic inflammation, leading to osteoporosis. Folic acid (FA) is a water-soluble vitamin that plays an essential role in regulating blood lipids and antioxidants. However, the effects and underlying mechanisms of FA in osteoporosis induced by an HFD remain poorly understood. This study aimed to investigate the effect of FA on bone health by using HFD-induced osteoporosis mice. Materials and Methods: Mice were fed a normal diet, HFD or an HFD supplemented with FA (20 µg/ml in drinking water) for 16 weeks. Throughout the 16 weeks study period, the rats were weighed once every week. GTT, ITT and lipid indexes were detected to evaluate the effects of FA on lipid metabolism in the HFD-fed mice. Morphological and structural changes of the femur and tibial bone were observed using micro-CT, HE staining and bone conversion parameters. The expression of MDA, SOD and inflammatory factors were detected to evaluate the effects of FA on oxidative stress and inflammatory response in the HFD-fed mice. Quantitative real-time PCR and Western blot (WB) were used to investigate the AMPK signaling pathway. Results: After the intervention of FA, the body fat rate of obese mice was reduced, and related metabolic disorders such as insulin resistance, hyperlipidemia, and systemic inflammation were alleviated. In correlation with those modifications, FA attenuated bone loss and improved bone microarchitecture, accompanied the number of osteoclasts and adipocytes decreased. Furthermore, FA promoted the phosphorylation of AMPK, thereby promoting the expression of Carnitine palmitoyltransferase 1 (CPT1), nuclear factor erythroid-2 related factor 2 (Nrf2) and antioxidant enzymes. Conclusion: These findings suggest that FA may modulate lipid metabolism and oxidative stress responses activating the AMPK signaling pathway, thereby alleviating HFD-induced osteoporosis. The results from our study provide experimental evidence to prevent HFD-induced osteoporosis.
RESUMEN
Patients with chemotherapy or radiation therapy often generate anemia and low immunity due to the therapy-induced bone marrow (BM) suppression. To enhance hematopoietic regeneration during the therapy-induced BM suppression urgently need to be solved. Fibroblast growth factors (FGFs) play important regulatory roles in hematopoietic stem and progenitor cell (HSPC) expansion in vitro and in vivo by the FGF receptor (FGFR1-4)-mediated signaling pathway. FGFR3 is an important member of the FGFR family, and its regulatory function in hematopoiesis is largely unknown. Using knockout (KO) mice of FGFR3, we found that loss of FGFR3 does not affect HSPC functions or lineage differentiation during steady-state hematopoiesis, but FGFR3 deletion accelerates HSPC expansion and hematopoiesis recovery via a cell-autonomous manner under 5-fluorouracil-induced BM suppression. Our results showed that FGFR3 inactivation accelerates BM suppression-induced HSPC expansion by upregulating FGFR1 and its downstream transcriptional factor, ELK, which regulates the expression of the cyclin D1 gene at the level of transcription. Further studies confirmed that loss of FGFR3 in hematopoietic cells inhibits in vivo leukemogenesis under BM suppression. Our data found a novel hematopoietic regulatory mechanism by which FGFR3 deletion promotes HSPC expansion under BM suppression and also provided a promising approach to enhance antileukemia and hematopoietic regeneration by inhibiting FGFR3 functions in HSPCs combined with leukemic chemotherapy.
Asunto(s)
Médula Ósea , Células Madre Hematopoyéticas/citología , Receptor Tipo 3 de Factor de Crecimiento de Fibroblastos , Animales , Ciclina D1/genética , Ratones , Ratones Noqueados , Receptor Tipo 1 de Factor de Crecimiento de Fibroblastos/genética , Receptor Tipo 3 de Factor de Crecimiento de Fibroblastos/genética , Transducción de Señal , Proteína Elk-1 con Dominio etsRESUMEN
The canine metabolic diseases, such as obesity and diabetes, have become a worldwide problem. Fibroblast growth factor 21 (FGF21) is a potent regulator which has many biological functions relative to metabolism regulation. It suggests that FGF21 plays important roles in regulating canine metabolic diseases. To acquire the recombinant canine FGF21 (rcFGF21) in Escherichia coli, the recombinant bacteria were induced by 0.5 mM IPTG for 16 hours at 16 °C, and the rcFGF21 protein was purified by Ni-NTA. 8 mg rcFGF21 was acquired from one liter bacteria. The rcFGF21 protein has specific immunoblot reactivity against anti-FGF21 and anti-His antibody. The in vivo experimental result showed that rcFGF21 can significantly reduce plasma glucose of STZ-induced diabetic mice.
Asunto(s)
Glucemia/análisis , Diabetes Mellitus Experimental/tratamiento farmacológico , Escherichia coli/genética , Factores de Crecimiento de Fibroblastos/administración & dosificación , Factores de Crecimiento de Fibroblastos/genética , Animales , Diabetes Mellitus Experimental/metabolismo , Enfermedades de los Perros/metabolismo , Perros , Escherichia coli/efectos de los fármacos , Factores de Crecimiento de Fibroblastos/aislamiento & purificación , Factores de Crecimiento de Fibroblastos/metabolismo , Isopropil Tiogalactósido/farmacología , Enfermedades Metabólicas/veterinaria , Ratones , Proteínas Recombinantes/aislamiento & purificación , Proteínas Recombinantes/metabolismo , EstreptozocinaRESUMEN
Background Overexpression or mutated activation of Fibroblast growth factor receptor 3 (FGFR3) is involved in the pathogenesis of many tumors. More and more studies focus on the potential usage of therapeutic antibodies against FGFR3. Results In this study, a novel single-chain Fv (ScFv) against FGFR3 was prepared and characterized. To achieve the soluble expression, ScFv was fused with Sumo (Small ubiquitin-related modifier) by polymerase chain reaction (PCR), and cloned into pET-20b. The recombinant bacteria were induced by 0.5 mM Isopropyl-ß-d-thiogalactopyranoside (IPTG) for 16 h at 20°C, and the supernatant liquid of Sumo-ScFv was harvested and purified by Ni-NTA chromatography. After being cleaved by the Sumo protease, the recombinant ScFv was released from the fusion protein, and further purified by Ni-NTA chromatography. The purity of ScFv was shown to be higher than 95% and their yield reached 4 mg per liter of bacterial culture. In vitro data showed that ScFv can significantly attenuate FGF9-induced phosphorylation of FGFR3. Conclusion We provide a novel method to produce soluble expression and bioactive functions of ScFv in Escherichia coli.