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Articles by Lili Zhang
Total Records ( 2 ) for Lili Zhang
  Farman Ali Siyal , Mohamed Ezzat Abd El-Hack , Mahmoud Alagawany , Chao Wang , Xioli Wan , Jintian He , Mingfa Wang , Lili Zhang , Xiang Zhong , Tian Wang and Kuldeep Dhama
  Background and Objective: Lecithin is a feed supplement and dietary source of several active compounds; therefore, this study evaluated the Soybean Lecithin (SL) in broiler diets by measuring performance, nutrient utilization, serum parameters and hepatic antioxidant status. Methodology: About 216 days old Arbor Acre broiler chicks were allotted into three groups as follow: the first group was fed a Basal Diet (BD) without emulsifier; the second and third groups were fed basal diet supplemented with 0.05 (SL0.05) and 0.1% (SL0.10) of SL, respectively. Results: During starter, grower and overall period, chicken fed with SL has better daily gain and feed intake compared with control, while feed conversion was improved in SL0.10 throughout the experiment compared to SL0.05 and control. At 21 and 42 days old, SL0.10 showed highest relative liver weight compared to SL0.05 and control (p<0.05). On day 21, digestibility of dry matter, ether extract and protein in chickens fed diet with SL0.10 was significantly improved in comparison with those fed SL0.05 and control. Cholesterol, triglyceride and low density lipoprotein concentrations were decreased in SL0.10 group in comparison with control. Serum glucose was higher in SL0.10 group compared to SL0.05 and control. Feeding SL0.10 resulted in the decreased hepatic malondialdehyde content and remarkably increased catalase, total superoxide dismutase and total antioxidant capacity enzyme activities. Conclusion: Feeding soy lecithin at 0.10% improved performance, reduced cholesterol and triglyceride, LDL-cholesterol concentrations in serum broilers. In addition, soy lecithin is suitable for improving antioxidant status and has ability to protect against oxidative stress.
  Lili Zhang , Zeljka Smit-McBride , Xiaoyu Pan , Jeanette Rheinhardt and John W. B. Hershey
  Dysregulation of protein synthesis has been implicated in oncogenesis through a mechanism whereby "weak" mRNAs encoding proteins involved in cell proliferation are strongly translated when the protein synthesis apparatus is activated. Previous work has determined that many cancer cells contain high levels of eIF3h, a protein subunit of translation initiation factor eIF3, and overexpression of eIF3h malignantly transforms immortal NIH-3T3 cells. This is a general feature of eIF3h, as high levels also affect translation, proliferation, and a number of malignant phenotypes of CHO-K1 and HeLa cells and, most significantly, of a primary prostate cell line. Furthermore, overexpressed eIF3h inhibits Myc-dependent induction of apoptosis of primary prostate cells. eIF3h appears to function through translation, as the initial appearance of overexpressed eIF3h in rapidly induced NIH-3T3 cells correlates tightly with the stimulation of protein synthesis and the generation of malignant phenotypes. This oncogenic potential of eIF3h is enhanced by phosphorylation at Ser183. Finally, reduction of eIF3h levels in breast and prostate cancer cell lines by short interfering RNA methods reduces their rates of proliferation and anchorage-independent growth in soft agar. The results provide compelling evidence that high eIF3h levels directly stimulate protein synthesis, resulting in the establishment and maintenance of the malignant state in cells.
 
 
 
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