Quantitative proteomic analysis of MDCK cell adhesion

2021 ◽  
Author(s):  
Xuanqing Ye ◽  
Jiamin Wang ◽  
Zilin Qiao ◽  
Di Yang ◽  
Jiao Wang ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Genetic Engineering ◽  
Cell Line ◽  
Mdck Cell ◽  
Proteomic Analysis ◽  
Quantitative Proteomics ◽  
Mdck Cells ◽  
Vaccine Production ◽  
Quantitative Proteomic Analysis ◽  
Suspension Cell Line

Establishing a stable MDCK suspension cell line by genetic engineering has significant potential to aid industrialization of vaccine production. In this study, quantitative proteomics was used to explore adhesion proteins in MDCK cells.

scholarly journals Quantitative proteomic analysis of cervical cancer based on TMT-labeled quantitative proteomics

2021 ◽  
pp. 104453
Author(s):  
Dianqin Xu ◽  
Xiaoyu Zhu ◽  
Ji Ren ◽  
Shan Huang ◽  
Ziwen Xiao ◽  
...  
Keyword(s):  
Cervical Cancer ◽  
Proteomic Analysis ◽  
Quantitative Proteomics ◽  
Quantitative Proteomic Analysis

scholarly journals Quantitative proteomic analysis for radiation-induced cell cycle suspension in 92-1 melanoma cell line

2013 ◽  
Vol 54 (4) ◽  
pp. 649-662 ◽  
Author(s):  
Fengling Wang ◽  
Zhitong Bing ◽  
Yanan Zhang ◽  
Bin Ao ◽  
Sheng Zhang ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Cell Line ◽  
Melanoma Cell ◽  
Proteomic Analysis ◽  
Melanoma Cell Line ◽  
Quantitative Proteomic Analysis ◽  
Radiation Induced

scholarly journals Quantitative proteomic analysis of HeLa cells in response to biocompatible Fe2C@C nanoparticles: 16O/18O-labelling & HPLC-ESI-orbit-trap profiling approach

2018 ◽  
Vol 7 (1) ◽  
pp. 84-92 ◽  
Author(s):  
Murtaza Hasan ◽  
Ghazala Mustafa ◽  
Javed Iqbal ◽  
Muhammad Ashfaq ◽  
Nasir Mahmood
Keyword(s):  
Cell Culture ◽  
Hela Cells ◽  
Proteomic Analysis ◽  
Quantitative Proteomics ◽  
Molecular Response ◽  
Isotopic Labelling ◽  
Proteomics Analysis ◽  
Quantitative Proteomic Analysis

Here, we have investigated the comparative quantitative proteomics analysis of the molecular response of HeLa cells to biocompatible Fe2C@C nanoparticles (NPs) using 16O/18O isotopic labelling of the cell culture.

Assessment of aspects of the toxicity of Clostridium perfringens E-toxin using the MDCK cell line

1996 ◽  
Vol 15 (11) ◽  
pp. 904-908 ◽  
Author(s):  
Christopher D Lindsay
Keyword(s):  
Cell Line ◽  
Clostridium Perfringens ◽  
Mechanism Of Action ◽  
Sodium Azide ◽  
Mdck Cell ◽  
Mdck Cells ◽  
Neutral Red ◽  
Temperature Sensitive ◽  
Mdck Cell Line ◽  
Neutral Red Assay

1 The epithelial Madin Darby Canine Kidney (MDCK) cell line was used to study the toxicity of ∈-toxin from Clostridium perfringens. The epithelial MDCK cell line is known to be sensitive to ∈-toxin of Clostridium perfringens and to investigate its mechanism of action, the neutral red assay has been used to determine the viability of cultures of this cell line. 2 Comparison of the LC 50s obtained at 34°C and 0°C showed that the lethality of ∈-toxin was reduced by 18- fold at the lower temperature. The effect of tempera ture on ∈-toxin lethality is unlikely to be due to reductions in membrane fluidity for the addition of Ca2+ or Mg2+ (2 mM) to buffer containing toxin was without effect. Varying the pH of the toxin-containing buffer from 6.9 to 8.7 did not increase the lethality of the toxin, though the most acidic pH used (5.8) was found to potentiate its action on MDCK cells. 3 The effect of inhibiting endocytosis on the lethality ofe toxin was also investigated by incubating cultures of MDCK cells with and without sodium azide over a range of concentrations of toxin. The co-administra tion of sodium azide did not reduce the toxicity of ∈ toxin, suggesting that energy-dependent uptake pro cesses such as endocytosis were unlikely to be involved in its mechanism of action. The results are, however, consistent with known receptor-based me chanisms of uptake and with other mechanisms of internalisation across the plasma membrane. ∈-toxin thus interacts with cell surfaces by a temperature sensitive mechanism potentiated by low pH.

C-Met signalling in an HGF/SF-insensitive variant MDCK cell line with constitutive motile/invasive behaviour

1996 ◽  
Vol 109 (9) ◽  
pp. 2371-2381
Author(s):  
C.P. Webb ◽  
K. Lane ◽  
A.P. Dawson ◽  
G.F. Vande Woude ◽  
R.M. Warn
Keyword(s):  
Growth Factor ◽  
Tyrosine Kinase ◽  
Cell Line ◽  
Tyrosine Phosphorylation ◽  
Mdck Cell ◽  
Mdck Cells ◽  
Cell Surface Expression ◽  
Cell Phenotype ◽  
Mdck Cell Line

The Met protein is a receptor tyrosine kinase for hepatocyte growth factor/scatter factor (HGF/SF), a multifunctional growth factor with mitogenic, motogenic and morphogenic properties. A morphologically altered variant of the MDCK cell line, MDCK-1, spontaneously exhibits a number of features associated with a partial HGF/SF-Met induced phenotype (less adhesive colonies in culture, enhanced invasion and motility, nascent tubule formation), but paradoxically does not respond to HGF/SF treatment. Although the overall cell surface expression and distribution of Met were found to be similar in parental MDCK cells and the MDCK-1 cell line, p145met autophosphorylation (+/ HGF/SF) was significantly reduced in MDCK-1 cells in vitro and in vivo when compared with parental MDCK cells. In contrast, EGF induced cell proliferation and EGF receptor autophosphorylation to similar levels in both cell lines. The basal levels of protein tyrosine phosphorylation were higher in MDCK-1 cells when compared with parental MDCK cells, including that of two prominent proteins with molecular masses of approximately 185 kDa and 220 kDa. Moreover, both p185 and p220 are present and tyrosine phosphorylated in Met immunoprecipitates from MDCK-1 cells (+/-HGF/SF), but not parental MDCK cells. In addition, Met immunocomplexes from MDCK-1 cells exhibited an approximately 3-fold increased tyrosine kinase activity in vitro when compared with MDCK cells, correlating with the higher basal levels of total phosphotyrosine. Treatment of MDCK-1 cells with the tyrosine kinase inhibitor herbimycin A reverted the cell phenotype to a more MDCK-like morphology in culture, with a concomitant reduction in the tyrosine phosphorylation predominantly of p220. Taken together these data suggest that aberrations in Met activity and associated signalling render MDCK-1 cells insensitive to HGF/SF, and may also mediate alterations in MDCK-1 cell behaviour.

Presence of a novel influx pathway for Mg2+ in MDCK cells

1990 ◽  
Vol 259 (3) ◽  
pp. C521-C525 ◽  
Author(s):  
G. A. Quamme ◽  
L. J. Dai
Keyword(s):  
Cell Line ◽  
Mdck Cell ◽  
Mdck Cells ◽  
Cell Types ◽  
Madin Darby Canine Kidney ◽  
Entry Pathway ◽  
Electrical Gradient ◽  
Free Media ◽  
Darby Canine Kidney ◽  
Canine Kidney

Basal free Mg2+ concentration was 0.49 +/- 0.03 mM in normal single Madin-Darby canine kidney (MDCK) cells as measured by fluorescence with the aid of mag-fura-2. Accordingly, Mg2+ may enter the cell down a transmembrane electrical gradient. The present study describes some aspects of Mg2+ entry into the established MDCK cell line. MDCK cells were Mg2(+)-depleted (0.26 +/- 0.01 mM) by culturing in Mg2(+)-free media for 16-20 h. Cells were subsequently exposed to 5 mM MgCl2, and intracellular Mg2+ concentration ([Mg2+]i) was monitored with fluorescence. [Mg2+]i returned to normal basal levels, 0.56 +/- 0.05 mM, with a refill rate of 272 +/- 39 nM/s, n = 4. Mg2+ entry was not changed by 5.0 mM external Ca2+ but was completely inhibited with 5.0 mM La3+. Intracellular Ca2+ concentration was not altered by Mg2+ depletion or during Mg2+ repletion. Mg2+ uptake was inhibited by verapamil (0 +/- 27 nM/s, n = 3), was inhibited less so by diltiazem (141 +/- 34 nM/s, n = 3), and was not affected by nifedipine (300 +/- 53 nM/s, n = 6). These inhibitors were fully reversible on removal, and [Mg2+]i returned to normal levels. These data indicate the presence of a unique Mg2+ entry pathway in MDCK cells that may be important in Mg2+ homeostasis. The model of Mg2+ refill into Mg2(+)-depleted cells may be useful in other cell types.

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