Quantum dots (QDs) restrain human cervical carcinoma HeLa cell proliferation through inhibition of the ROCK-c-Myc signaling

2013 ◽  
Vol 5 (3) ◽  
pp. 590 ◽  
Author(s):  
Liqun Chen ◽  
Guangbo Qu ◽  
Changwen Zhang ◽  
Shuping Zhang ◽  
Jiuyang He ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Quantum Dots ◽  
Hela Cell ◽  
Cervical Carcinoma ◽  
Human Cervical Carcinoma

scholarly journals 3-Chloro-2,5-dihydroxybenzyl alcohol activates human cervical carcinoma HeLa cell apoptosis by inducing DNA damage

2007 ◽  
Author(s):  
Yanjun Zhang ◽  
Eun-Young Ahn ◽  
Yahong Jiang ◽  
Dong-Kyoo Kim ◽  
Sung-Goo Kang ◽  
...  
Keyword(s):  
Dna Damage ◽  
Hela Cell ◽  
Cervical Carcinoma ◽  
Cell Apoptosis ◽  
Human Cervical Carcinoma

scholarly journals Synthesis of the 6-Substituted Imidazo[1,2-a]Pyridine-3-yl-2- Phosphonopropionic Acids as Potential Inhibitors of Rab Geranylgeranyl Transferase

2021 ◽  
Vol 8 ◽  
Author(s):  
Damian Kusy ◽  
Aleksandra Marchwicka ◽  
Joanna Małolepsza ◽  
Katarzyna Justyna ◽  
Edyta Gendaszewska-Darmach ◽  
...  
Keyword(s):  
Carboxylic Acid ◽  
Hela Cell ◽  
Cell Line ◽  
Cervical Carcinoma ◽  
Pyridine Ring ◽  
Hela Cell Line ◽  
Human Cervical Carcinoma ◽  
Geranylgeranyl Transferase ◽  
Potential Inhibitors ◽  
Inactive Analog

Twelve phosphonopropionates derived from 2-hydroxy-3-imidazo[1,2-a]pyridin-3-yl-2-phosphonopropionic acid (3-IPEHPC) were synthesized and evaluated for their activity as inhibitors of protein geranylgeranylation. The nature of the substituent in the C6 position of imidazo[1,2-a]pyridine ring was responsible for the compound's activity against Rab geranylgeranyl transferase (RGGT). The most active inhibitors disrupted Rab11A prenylation in the human cervical carcinoma HeLa cell line. The esterification of carboxylic acid in the phosphonopropionate moiety turned the inhibitor into an inactive analog.

Taxol-induced alteration of intracellular amino-acid profile related to human cervical carcinoma HeLa cell death

2011 ◽  
Vol 34 (1) ◽  
pp. 1-7 ◽  
Author(s):  
Xiao-Fei Han ◽  
Yan-Qiu Liu ◽  
Long-Xing Wang ◽  
Qian-Xu Yang ◽  
Hong-Bin Xiao
Keyword(s):  
Cell Death ◽  
Amino Acid ◽  
Hela Cell ◽  
Cervical Carcinoma ◽  
Amino Acid Profile ◽  
Human Cervical Carcinoma ◽  
Intracellular Amino Acid

scholarly journals Quercetin and aconitine synergistically induces the human cervical carcinoma HeLa cell apoptosis via endoplasmic reticulum (ER) stress pathway

PLoS ONE ◽  
2018 ◽  
Vol 13 (1) ◽  
pp. e0191062 ◽  
Author(s):  
Xiu-Mei Li ◽  
Jing Liu ◽  
Fang-Fang Pan ◽  
Dong-Dong Shi ◽  
Zhi-Guo Wen ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Hela Cell ◽  
Er Stress ◽  
Cervical Carcinoma ◽  
Cell Apoptosis ◽  
Human Cervical Carcinoma ◽  
Stress Pathway

scholarly journals The HeLa Cell Glucagon-Like Peptide-2 Receptor Is Coupled to Regulation of Apoptosis and ERK1/2 Activation through Divergent Signaling Pathways

2005 ◽  
Vol 19 (2) ◽  
pp. 459-473 ◽  
Author(s):  
J. A. Koehler ◽  
B. Yusta ◽  
D. J. Drucker
Keyword(s):  
Hela Cell ◽  
Cell Lines ◽  
Cervical Carcinoma ◽  
Hela Cells ◽  
Growth Factor Receptor ◽  
Dominant Negative ◽  
Cdna Libraries ◽  
Independent Manner ◽  
Human Cervical Carcinoma ◽  
Glucagon Like Peptide

Abstract Glucagon-like peptide-2 (GLP-2) regulates proliferative and cytoprotective pathways in the intestine; however GLP-2 receptor (GLP-2R) signal transduction remains poorly understood, and cell lines that express the endogenous GLP-2R have not yet been isolated. We have now identified several expressed sequence tags from human cervical carcinoma cDNA libraries that correspond to GLP-2R nucleotide sequences. GLP-2R mRNA transcripts were detected by RT-PCR in two human cervical carcinoma cell lines, including HeLa cells. GLP-2 increased cAMP accumulation and activated ERK1/2 in HeLa cells transiently expressing the cloned human HeLa cell GLP-2R cDNA. However, the GLP-2R-induced activation of ERK1/2 was not mediated through Gαs, adenylyl cyclase, or transactivation of the epidermal growth factor receptor, but was pertussis toxin sensitive, inhibited by dominant negative Ras, and dependent on βγ-subunits. GLP-2 also induced a significant increase in bromodeoxyuridine incorporation that was blocked by dominant negative Ras. Furthermore, GLP-2 inhibited HeLa cell apoptosis induced by LY294002 in a protein kinase A-dependent, but ERK-independent, manner. These findings demonstrate that the HeLa cell GLP-2R differentially signals through both Gαs/cAMP- and Gi/Go-dependent pathways, illustrating for the first time that the GLP-2R is capable of coupling to multiple heterotrimeric G proteins defining distinct GLP-2R-dependent biological actions.

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