Asian Science Citation Index is committed to provide an authoritative, trusted and significant information by the coverage of the most important and influential journals to meet the needs of the global scientific community.  
ASCI Database
308-Lasani Town,
Sargodha Road,
Faisalabad, Pakistan
Fax: +92-41-8815544
Contact Via Web
Suggest a Journal
 
Articles by Zhuo Wang
Total Records ( 2 ) for Zhuo Wang
  Weili Sun , Guangyu Li , Hanlu Liu , Wei Zhong , Haihua Zhang , Kun Bao , Chao Xu , Yahan Yang and Zhuo Wang
  The study was to develop a Polymerase Chain Reaction (PCR) assay for specific detection of mink meat using designed pairs of primers based on mitochondrial D-loop. Mink meat is used as fraud ingredients of false mutton or dog meat in meat markets. This study was conducted to establish Polymerase Chain Reaction (PCR) method for the sensitive and specific detection of mink (Mustela vison) DNA in meat products. Six pairs of primers were designed from tandem repeat region of D-loop in mitochondria after alignment of the available sequences in the GenBank database. The specific pair of primers chosen from the six designed pairs by PCR generated specific fragments of 343 bp in length for mink. The specificity of detection was conducted with DNA samples of mink, blue fox, dog, raccoon dog, swine, sheep. Then amplification of positive reaction was observed only in mink species. In this study, no adverse effects of cooking and autoclaving were found on amplification of mink DNA fragments. Then the detection limit was found to be less than 1% in mixed meat products. The PCR method described in this study proved to be very sensitive and reliable in mink DNA identification. Thus, it could be considered as a further improvement method for the detection of mink DNA in meat products processed under different manufacturing conditions.
  Dilek Telci , Zhuo Wang , Xiaoling Li , Elisabetta A. M. Verderio , Martin J. Humphries , Manuela Baccarini , Huveyda Basaga and Martin Griffin
  Heterotropic association of tissue transglutaminase (TG2) with extracellular matrix-associated fibronectin (FN) can restore the adhesion of fibroblasts when the integrin-mediated direct binding to FN is impaired using RGD-containing peptide. We demonstrate that the compensatory effect of the TG-FN complex in the presence of RGD-containing peptides is mediated by TG2 binding to the heparan sulfate chains of the syndecan-4 cell surface receptor. This binding mediates activation of protein kinase Cα (PKCα) and its subsequent interaction with β1 integrin since disruption of PKCα binding to β1 integrins with a cell-permeant competitive peptide inhibits cell adhesion and the associated actin stress fiber formation. Cell signaling by this process leads to the activation of focal adhesion kinase and ERK1/2 mitogen-activated protein kinases. Fibroblasts deficient in Raf-1 do not respond fully to the TG-FN complex unless either the full-length kinase competent Raf-1 or the kinase-inactive domain of Raf-1 is reintroduced, indicating the involvement of the Raf-1 protein in the signaling mechanism. We propose a model for a novel RGD-independent cell adhesion process that could be important during tissue injury and/or remodeling whereby TG-FN binding to syndecan-4 activates PKCα leading to its association with β1 integrin, reinforcement of actin-stress fiber organization, and MAPK pathway activation.
 
 
 
Copyright   |   Desclaimer   |    Privacy Policy   |   Browsers   |   Accessibility