MiR-199a-5p suppresses tumorigenesis by targeting clathrin heavy chain in hepatocellular carcinoma

2017 ◽  
Vol 35 (2) ◽  
pp. 98-104 ◽  
Author(s):  
Guo-hao Huang ◽  
Hong Shan ◽  
Dan Li ◽  
Bin Zhou ◽  
Peng-fei Pang
Keyword(s):  
Hepatocellular Carcinoma ◽  
Heavy Chain ◽  
Clathrin Heavy Chain

scholarly journals Identification of novel immunohistochemical tumor markers for primary hepatocellular carcinoma; clathrin heavy chain and formiminotransferase cyclodeaminase

Hepatology ◽  
2008 ◽  
Vol 48 (2) ◽  
pp. 519-530 ◽  
Author(s):  
Masanori Seimiya ◽  
Takeshi Tomonaga ◽  
Kazuyuki Matsushita ◽  
Masahiko Sunaga ◽  
Masamichi Oh-ishi ◽  
...  
Keyword(s):  
Hepatocellular Carcinoma ◽  
Tumor Markers ◽  
Heavy Chain ◽  
Primary Hepatocellular Carcinoma ◽  
Clathrin Heavy Chain ◽  
Formiminotransferase Cyclodeaminase

Diagnostic accuracy of clathrin heavy chain staining in a marker panel for the diagnosis of small hepatocellular carcinoma

Hepatology ◽  
2011 ◽  
Vol 53 (5) ◽  
pp. 1549-1557 ◽  
Author(s):  
Luca Di Tommaso ◽  
Annarita Destro ◽  
Valentina Fabbris ◽  
Gaia Spagnuolo ◽  
Anna Laura Fracanzani ◽  
...  
Keyword(s):  
Hepatocellular Carcinoma ◽  
Diagnostic Accuracy ◽  
Heavy Chain ◽  
Small Hepatocellular Carcinoma ◽  
Marker Panel ◽  
Clathrin Heavy Chain

Structure of clathrin cages and coats in ice

1986 ◽  
Vol 44 ◽  
pp. 94-97
Author(s):  
G.P.A. Vigers ◽  
R.A. Crowther ◽  
B.M.F. Pearse
Keyword(s):  
Electron Microscopy ◽  
Heavy Chain ◽  
Outer Part ◽  
Coated Vesicles ◽  
Eukaryotic Cells ◽  
Coat Proteins ◽  
Terminal Domain ◽  
Clathrin Heavy Chain ◽  
Membrane Components

Clathrin forms the polyhedral cage of coated vesicles, which mediate the transfer of selected membrane components within eukaryotic cells. Clathrin cages and coated vesicles have been extensively studied by electron microscopy of negatively stained preparations and shadowed specimens. From these studies the gross morphology of the outer part of the polyhedral coat has been established and some features of the packing of clathrin trimers into the coat have also been described. However these previous studies have not revealed any internal details about the position of the terminal domain of the clathrin heavy chain, the location of the 100kd-50kd accessory coat proteins or the interactions of the coat with the enclosed membrane.

scholarly journals Characterization of a Temperature-Sensitive Vertebrate Clathrin Heavy Chain Mutant as a Tool to Study Clathrin-Dependent Events In Vivo

PLoS ONE ◽  
2010 ◽  
Vol 5 (8) ◽  
pp. e12017 ◽  
Author(s):  
Petra Neumann-Staubitz ◽  
Stephanie L. Hall ◽  
Joseph Kuo ◽  
Antony P. Jackson
Keyword(s):  
Heavy Chain ◽  
Temperature Sensitive ◽  
Clathrin Heavy Chain

scholarly journals Loss of clathrin heavy chain enhances actin-dependent stiffness of mouse embryonic stem cells

2020 ◽  
Author(s):  
Ridim D Mote ◽  
Jyoti Yadav ◽  
Surya Bansi Singh ◽  
Mahak Tiwari ◽  
Shivprasad Patil ◽  
...  
Keyword(s):  
Mechanical Properties ◽  
Stem Cells ◽  
Embryonic Stem Cells ◽  
Young’S Modulus ◽  
Heavy Chain ◽  
Young's Modulus ◽  
Embryonic Stem ◽  
Mouse Embryonic Stem Cells ◽  
Actin Binding ◽  
Clathrin Heavy Chain

AbstractMouse embryonic stem cells (mESCs) display unique mechanical properties, including low cell stiffness, and specific responses to features of the underlying substratum. Using atomic force microscopy (AFM), we demonstrate that mESCs lacking the clathrin heavy chain (Cltc), display higher Young’s modulus, indicative of greater cellular stiffness, in comparison to WT mESCs. We have previously shown that mESCs lacking Cltc display a loss of pluripotency, and an initiation of differentiation. The increased stiffness observed in these cells was accompanied by the presence of actin stress fibres and accumulation of the inactive, phosphorylated, actin binding protein, Cofilin. Treatment of Cltc knockdown mESCs with actin polymerization inhibitors resulted in a decrease in the Young’s modulus, to values similar to those obtained with WT mESCs. However, the expression profile of pluripotency factors was not rescued. This indicates that a restoration of mechanical properties, through modulation of the actin cytoskeleton, may not always be accompanied by a change in the expression of critical transcription factors that regulate the state of a stem cell, and that this may be dependent on the presence of active endocytosis in a cell.

scholarly journals Clathrin heavy chain phosphorylated at T606 plays a role in proper cell division

Cell Cycle ◽  
2019 ◽  
Vol 18 (16) ◽  
pp. 1976-1994 ◽  
Author(s):  
Yusuke Yabuno ◽  
Toshihiro Uchihashi ◽  
Towa Sasakura ◽  
Hiroyuki Shimizu ◽  
Yoko Naito ◽  
...  
Keyword(s):  
Cell Division ◽  
Heavy Chain ◽  
Clathrin Heavy Chain

Tyrosine phosphorylation of clathrin heavy chain under oxidative stress

2002 ◽  
Vol 297 (2) ◽  
pp. 353-360 ◽  
Author(s):  
Yoshito Ihara ◽  
Chie Yasuoka ◽  
Kan Kageyama ◽  
Yoshinao Wada ◽  
Takahito Kondo
Keyword(s):  
Oxidative Stress ◽  
Tyrosine Phosphorylation ◽  
Heavy Chain ◽  
Clathrin Heavy Chain
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