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  • Open Access

    ARTICLE

    Light-controlled phosphorylation in the TrkA-Y785 site by photosensitive UAAs activates the MAPK/ERK signaling pathway

    SHU ZHAO1,*, SHIXIN YE2

    BIOCELL, Vol.47, No.6, pp. 1377-1388, 2023, DOI:10.32604/biocell.2023.023874 - 19 May 2023

    Abstract Background: This paper aims to establish a light-controlled phosphorylation detection method at the Y785 site of tropomyosin receptor kinase A (TrkA) receptor in mammalian cells by using genetic code expansion technology and detecting the effects of optical activation of this site on the downstream MAPK/ERK pathway. The study is based on the current situation that the regulatory mechanism of TrkA phosphorylation has not been fully elucidated. Methods: Two photosensitive unnatural amino acids, p-azido-L-phenylalanine (AzF) and photo-caged tyrosine (ONB) were introduced into the TrkA-Y785 site by genetic code expansion technology and site-directed mutagenesis. Western blotting and laser More >

  • Open Access

    ABSTRACT

    Microspheres Modified with the Heparin Increasing the Length of Molecular Linker to Better Capture the Endotoxin

    Qi Dang1, Chun-Gong Li1, Xin-Xin Jin1, Ya-Jin Zhao1, Xiang Wang1,*

    Molecular & Cellular Biomechanics, Vol.16, Suppl.2, pp. 146-146, 2019, DOI:10.32604/mcb.2019.07074

    Abstract Endotoxin is a a very powerful and toxic inflammatory stimulator usually leading to the sepsis occurred. In order to remove endotoxin better through hemoperfusion, it is a pretty choice to increase the length of molecular linker on adsorbents. In this study, we chose the heparin as a molecular linker because of its being anticoagulant linear polysaccharide. Heparin as a linker was covalently immobilized on the chloromethylated polystyrene microspheres (Ps) and then connected with L-phenylalanine (Phe) forming the Ps-Hep-Phe structure to adsorbed endotoxin better. The property of microspheres was characterized by Fourier transform infrared spectroscopy, X-ray More >

  • Open Access

    ARTICLE

    Carcinoembryonic antigen inhibits neutrophil activation by N-formyl-methionyl-leucyl-phenylalanine

    Anna PAŃCZYSZYN1 *, Anna KROP-WATOREK1,2, Maciej WIECZOREK1

    BIOCELL, Vol.39, No.2-3, pp. 1-4, 2015, DOI:10.32604/biocell.2015.39.001

    Abstract Carcinoembryonic antigen (CEA) is a surface glycoprotein expressed in human epithelial cells and is released from their surface, especially during colorectal cancer. Frequently, colorectal cancer is accompanied by inflammation, where tumor-infiltrating neutrophils play an important role. CEA was also found to be a strong chemotactic agent for neutrophils. The purpose of this study was to find out if CEA can enhance neutrophil priming and activation. Primed neutrophils were activated by N-formyl-methionyl-leucyl-phenylalanine (formyl-MLP) and the resulting oxidative burst was measured luminometrically. Unexpectedly, in vitro priming of neutrophils by CEA, alone or preceded by LPS, inhibited subsequent More >

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