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  • Open Access

    ARTICLE

    Overloading of differentiated Caco-2 cells during lipid transcytosis induces glycosylation mistakes in the Golgi complex

    GALINA N. DENISOVA1, IVAN D. DIMOV1, ANNA V. ZAITSEVA1,2, LINARD J. ARTIUX3, ALEXANDER A. MIRONOV1,4,*, NATALIA R. KARELINA1

    BIOCELL, Vol.45, No.3, pp. 773-783, 2021, DOI:10.32604/biocell.2021.014233 - 03 March 2021

    Abstract Overloading the intestine enterocytes with lipids induced alteration of the Golgi complex (GC; ) and could cause glycosylation errors. Here, using differentiated Caco-2 cells with the established 0[I] blood group phenotype (no expression of the blood antigens A and B [AgA, AgB] under normal conditions) as a model of human enterocytes we examined whether the overloading of these cells with lipids could cause errors in the Golgi-dependent glycosylation. We demonstrated that under these conditions, there were alterations of the GC and the appearance of lipid droplets in the cytoplasm. Rare cells produced AgA and AgB. More >

  • Open Access

    ARTICLE

    A comparative pattern of lectin-binding in the endometrial glands of the uterus and placenta of healthy buffaloes and bovines at early gestation

    SERGIO GASTÓN CASPE1, JOSÉ LUIS KONRAD2, DADIN PRANDO MOORE3, JUAN MANUEL SALA1, LILIAN LISCHINSKY3, CARLOS MANUEL CAMPERO3, CLAUDIO GUSTAVO BARBEITO4,*

    BIOCELL, Vol.45, No.2, pp. 331-337, 2021, DOI:10.32604/biocell.2021.010701 - 19 February 2021

    Abstract Water buffalo (Bubalus bubalis) and domestic cattle (Bos taurus) are closely related species. However, embryo transfer interspecies has been attempted without any success. The failure in hybrid embryo-implantation is associated with the glycocode in the maternal-fetal interface. Glycosylation patterns have been studied in different species of ruminants; however, in B. bubalis, only the binucleated cells (BNC) have been analyzed. This glycocode is essential for a successful embryo-implantation and can be defined by Lectin-Histochemistry (LHC). The aim of this study is to compare the glycosylation pattern of placenta and uterus in water buffaloes and cattle by LHC. Tissue samples… More >

  • Open Access

    ARTICLE

    20(R)-ginsenoside Rg3, a product of high-efficiency thermal deglycosylation of ginsenoside Rd, exerts protective effects against scrotal heat-induced spermatogenic damage in mice

    WEI LIU1,#, ZI WANG1,2,#, JING LENG1, HENG WEI1, SHEN REN1,2, XIAOJIE GONG3, CHEN CHEN4, YINGPING WANG1,2, RUI ZHANG1,2,*, WEI LI1,2,*

    BIOCELL, Vol.44, No.4, pp. 655-669, 2020, DOI:10.32604/biocell.2020.013202 - 24 December 2020

    Abstract Heat stress (HS) reaction can lead to serious physiological dysfunction associated with cardiovascular and various organ diseases. Ginsenoside Rg3 (G-Rg3) is a representative component of ginseng rare saponin and can protect against multiple organs, also used as functional food to adjust the balance of the human body, but the therapeutic effect and molecular mechanism of G-Rg3 on male diseases under HS are underexplored. The aim of the present study, G-Rg3 was prepared through the efficient conversion of ginsenoside Rd and investigate the contribution of G-Rg3 to testicular injury induced exposure to HS. All mice were… More >

  • Open Access

    ABSTRACT

    Extracellular Matrix Elasticity Gives Integrin a Sweet Change via a p53/miRNA-532/atp2c1 Axis

    Yan Zu1,2, Qiang Li1, Chun Yang2,*

    Molecular & Cellular Biomechanics, Vol.16, Suppl.2, pp. 106-106, 2019, DOI:10.32604/mcb.2019.07132

    Abstract Extracellular matrix (ECM) elasticity affects the function of a variety of cells. Integrins are transmembrane receptors that considered to be a sensor of cellular mechanical stimulation. The activity of integrins is strongly influenced by glycans through glycosylation events and the establishment of glycan-mediated interactions. Our study found that the level of β1 integrin N-linked glycosylation was significantly down-regulated on softer ECM. Further, sialic acid is a common monosaccharide modified at the end of the sugar chain during N-glycosylation. We subjected the enriched sialylated glycoproteins to gel-based proteomic identification by tandem mass spectrometry and found that… More >

  • Open Access

    ARTICLE

    β-1,3-Galactosyl-O-Glycosyl-Glycoprotein β-1,6-N-Acetylglucosaminyltransferase 3 Increases MCAM Stability, Which Enhances S100A8/A9-Mediated Cancer Motility

    I Wayan Sumardika*†, Chen Youyi*, Eisaku Kondo, Yusuke Inoue§, I Made Winarsa Ruma*†, Hitoshi Murata*, Rie Kinoshita*, Ken-Ichi Yamamoto*, Shuta Tomida, Kazuhiko Shien#, Hiroki Sato#, Akira Yamauchi**, Junichiro Futami††, Endy Widya Putranto‡‡, Toshihiko Hibino§§, Shinichi Toyooka¶#¶¶, Masahiro Nishibori##, Masakiyo Sakaguchi*

    Oncology Research, Vol.26, No.3, pp. 431-444, 2018, DOI:10.3727/096504017X15031557924123

    Abstract We previously identified novel S100A8/A9 receptors, extracellular matrix metalloproteinase inducer (EMMPRIN), melanoma cell adhesion molecule (MCAM), activated leukocyte cell adhesion molecule (ALCAM), and neuroplastin (NPTN) β, that are critically involved in S100A8/A9-mediated cancer metastasis and inflammation when expressed at high levels. However, little is known about the presence of any cancerspecific mechanism(s) that modifies these receptors, further inducing upregulation at protein levels without any transcriptional regulation. Expression levels of glycosyltransferase-encoding genes were examined by a PCRbased profiling array followed by confirmation with quantitative real-time PCR. Cell migration and invasion were assessed using a Boyden chamber.… More >

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