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1.
Exp Ther Med ; 13(5): 2056-2064, 2017 May.
Article in English | MEDLINE | ID: mdl-28565808

ABSTRACT

An increasing number of infants and children undergo surgery and are exposed to anesthesia as a part of medical care each year. Isoflurane is a commonly used anesthetic in the pediatric population. However, previous studies have reported widespread isoflurane-induced neuroapoptosis and cognitive impairments in neonatal animal models, raising concerns over the administration of isoflurane in the pediatric population. The current study investigated the effects of rutin, a flavonoid, on isoflurane-induced neuroapoptosis in a neonatal rodent model. Groups of neonatal rat pups were administered rutin at doses of 10, 20 or 40 mg/kg body weight from postnatal day 1 (P1) to P15. On P7, pups were exposed to 0.75% isoflurane for 6 h. Rat pups in the control groups did not receive rutin, and did not receive anesthesia in one group. Neuroapoptosis following isoflurane exposure was determined by TUNEL assay. The expression levels of cleaved caspase-3, apoptotic pathway proteins [Bcl2-associated agonist of cell death (Bad), phospho-Bad, Bax, B-cell lymphoma 2 (Bcl-2) and Bcl-xL and mitogen-activated protein kinases (MAPK)] signalling pathway proteins [c-Jun N-terminal kinase (JNK), phospho-JNK, extracellular-signal-regulated kinase 1/2 (ERK1/2), phosphoERK1/2, p38, phospho-p38 and phospho-c-Jun], were determined by western blot analysis. The Morris water maze test was used to assess the learning and memory of pups on P30 and P31. The present study found that rutin at the tested doses of 10, 20 and 40 mg significantly reduced (P<0.05) the isoflurane-induced elevation in apoptotic cell count. The expression levels of caspase-3, Bad, Bax and MAPK proteins, which were increased following isoflurane treatment, were rescued by rutin treatment. Furthermore, rutin prevented the increase in Bcl-xL, Bcl-2 and phospho-Bad expression following isoflurane treatment, and enhanced the memory of the rats. Rutin provided neuroprotection against isoflurane-induced neuronal apoptosis and improved the learning and memory of rats by effectively regulating the expression levels of proteins in the MAPK pathway.

2.
Guang Pu Xue Yu Guang Pu Fen Xi ; 34(10): 2732-6, 2014 Oct.
Article in Chinese | MEDLINE | ID: mdl-25739217

ABSTRACT

In the present study, the near infrared spectrum of freshwater fish was used to detect the freshness on line, and the near infrared spectra on-line acquisition device was built to get the fish spectrum. In the process of spectrum acquisition, experiment samples move at a speed of 0.5 m · s(-1), the near-infrared diffuse reflection spectrum (900-2,500 nm) could be got for the next analyzing, and SVM was used to build on-line detection model. Sample set partitioning based on joint X-Y distances algo- rithm (SPXY) was used to divide sample set, there were 111 samples in calibration set (57 fresh samples and 54 bad samples), and 37 samples in test set (19 fresh samples and 18 bad samples). Seven spectral preprocessing methods were utilized to prepro- cess the spectrum, and the influences of different methods were compared. Model results indicated that first derivative (FD) with autoscale was the best preprocessing method, the model recognition rate of calibration set was 97.96%, and the recognition rate of test set was 95.92%. In order to improve the modeling speed, it is necessary to optimize the spectra variables. Therefore genetic algorithm (GA), successive projection algorithm (SPA) and competitive adaptive reweighed sampling (CARS) were adopted to select characteristic variables respectively. Finally CARS was proved to be the optimal variable selection method, 10 characteristic wavelengths were selected to develop SVM model, recognition rate of calibration set reached 100%, and recognition rate of test set was 93.88%. The research provided technical reference for freshwater fish freshness online detection.


Subject(s)
Fishes , Food Analysis/methods , Spectroscopy, Near-Infrared , Algorithms , Animals , Calibration , Fresh Water , Models, Theoretical
3.
Meat Sci ; 88(2): 234-40, 2011 Jun.
Article in English | MEDLINE | ID: mdl-21242036

ABSTRACT

Effects of temperature, pH and ionic strength on the stability of actomyosin (AM) from fish and pork were studied using UV spectra, solubility, turbidity, and sulfhydryl group content measurement for comparison. Pork AM exhibited higher stability to cold storage and heating than fish AM. The unfolding rate of AM increased with increasing temperature. Intense aggregation occurred over 30 °C for fish AM and 40 °C for pork AM. New disulfide bonds mainly formed over 40 °C for fish AM and 60 °C for pork AM. Pork AM exhibited the higher turbidity than fish AM in the range of 50-90 °C, suggesting the higher extent of aggregation of pork AM. Ionic strength mainly influenced solubility of AM, but there was no effect on cleavage and formation of disulfide bond. The lowest solubility of both AM was at pH 5.42. Additionally, fish AM was more sensitive to pH changes than pork AM.


Subject(s)
Actomyosin/chemistry , Fishes , Food Handling/methods , Meat , Swine , Actomyosin/metabolism , Animals , Disulfides/metabolism , Fishes/metabolism , Hydrogen-Ion Concentration , Osmolar Concentration , Protein Folding , Protein Stability , Solubility , Sulfhydryl Compounds/analysis , Swine/metabolism , Temperature , Ultraviolet Rays
4.
Meat Sci ; 80(3): 632-9, 2008 Nov.
Article in English | MEDLINE | ID: mdl-22063575

ABSTRACT

Secondary structures, gelation properties and their relationships in porcine myosin were studied by circular dichroism, dynamic rheological measurement and scanning electron microscopy. Gelling of porcine myosin involved a change in myosin conformation with protein-protein and protein-water interactions. The gelation properties were strongly pH and temperature dependent. Near the pI (pH 5.5 and 6.0), porcine myosin could spontaneously coagulate at 15°C resulting partially from the presence of more ß-sheets. Myosin at pH6.5-9.0 began to form a gel at temperatures greater than 38°C. Heating caused α-helices to partially turn into ß-sheets and random coils. Subsequently, myosin aggregated and formed a gel network. The gel strength decreased and the water-holding capacity (WHC) increased with increasing pH. Correlation analysis indicated that both the unfolding of α-helices and the formation of ß-sheets favored the gelation of porcine myosin. A high ß-sheet fraction prior to heating resulted in a low WHC of resultant gel. A compact and uniform gel was also obtained at pH6.5.

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