Nuclear localization of Formyl-Peptide Receptor 2 in human cancer cells

2016 ◽  
Vol 603 ◽  
pp. 10-19 ◽  
Author(s):  
Fabio Cattaneo ◽  
Melania Parisi ◽  
Tiziana Fioretti ◽  
Daniela Sarnataro ◽  
Gabriella Esposito ◽  
...  
Keyword(s):  
Cancer Cells ◽  
Nuclear Localization ◽  
Human Cancer ◽  
Formyl Peptide Receptor ◽  
Peptide Receptor ◽  
Human Cancer Cells ◽  
Formyl Peptide

scholarly journals Post-transcriptional regulation of cyclins D1, D3 and G1 and proliferation of human cancer cells depend on IMP-3 nuclear localization

Oncogene ◽  
2013 ◽  
Vol 33 (22) ◽  
pp. 2866-2875 ◽  
Author(s):  
T Rivera Vargas ◽  
S Boudoukha ◽  
A Simon ◽  
M Souidi ◽  
S Cuvellier ◽  
...  
Keyword(s):  
Transcriptional Regulation ◽  
Cancer Cells ◽  
Nuclear Localization ◽  
Human Cancer ◽  
Human Cancer Cells ◽  
Post Transcriptional Regulation

scholarly journals Selective Display of a Chemoattractant Agonist on Cancer Cells Activates the Formyl Peptide Receptor 1 on Immune Cells

2021 ◽  
Author(s):  
Eden L. Sikorski ◽  
Janessa Wehr ◽  
Noel J. Ferraro ◽  
Marcos M. Pires ◽  
Damien Thévenin
Keyword(s):  
Immune Response ◽  
Cancer Cells ◽  
Immune Cells ◽  
Formyl Peptide Receptor ◽  
Receptor Ligand ◽  
Patient Response ◽  
Peptide Receptor ◽  
Formyl Peptide ◽  
Tumor Homing

Current immunotherapeutics often work by directing components of the immune system to recognize biomarkers on the surface of cancer cells to generate an immune response. However, variable changes in biomarker distribution and expression can result in uneven patient response. The development of a more universal tumor-homing strategy has the potential to improve selectivity and extend therapy to cancers with decreased expression or absence of specific biomarkers. Here, we designed a bifunctional agent that exploits the inherent acidic microenvironment of most solid tumors to selectively graft the surface of cancer cells with a formyl peptide receptor ligand (FPRL). Our approach is based on the pH(Low) Insertion Peptide (pHLIP), a unique peptide that selectively targets tumors in vivo by anchoring onto cancer cells in a pHdependent manner. We establish that selectively remodeling cancer cells with a pHLIP-based FPRL activates formyl peptide receptors on recruited immune cells, potentially initiating an immune response towards tumors.

Nuclear localization of alkaline phosphatase in cultured human cancer cells

2003 ◽  
Vol 36 (1) ◽  
pp. 47-51 ◽  
Author(s):  
K. Yamamoto ◽  
Takumi Awogi ◽  
Keiji Okuyama ◽  
Nobuo Takahashi
Keyword(s):  
Alkaline Phosphatase ◽  
Cancer Cells ◽  
Nuclear Localization ◽  
Human Cancer ◽  
Human Cancer Cells ◽  
Cultured Human Cancer Cells

scholarly journals Penetration into Cancer Cells via Clathrin-Dependent Mechanism Allows L-Asparaginase from Rhodospirillum rubrum to Inhibit Telomerase

2020 ◽  
Vol 13 (10) ◽  
pp. 286
Author(s):  
Anna A. Plyasova ◽  
Marina V. Pokrovskaya ◽  
Olga M. Lisitsyna ◽  
Vadim S. Pokrovsky ◽  
Svetlana S. Alexandrova ◽  
...  
Keyword(s):  
Cancer Cells ◽  
Nuclear Localization ◽  
Rhodospirillum Rubrum ◽  
Human Cancer ◽  
Fluorescent Microscopy ◽  
Fluorescein Isothiocyanate ◽  
Telomerase Activity ◽  
Human Cancer Cells ◽  
Chromatin Relaxation ◽  
Dual Mechanism

The anticancer effect of L-asparaginases (L-ASNases) is attributable to their ability to hydrolyze L-asparagine in the bloodstream and cancer cell microenvironment. Rhodospirillum rubrum (RrA) has dual mechanism of action and plays a role in the suppression of telomerase activity. The aim of this work was to investigate the possible mechanism of RrA penetration into human cancer cells. Labeling of widely used L-ASNases by fluorescein isothiocyanate followed by flow cytometry and fluorescent microscopy demonstrated that only RrA can interact with cell membranes. The screening of inhibitors of receptor-mediated endocytosis demonstrated the involvement of clathrin receptors in RrA penetration into cells. Confocal microscopy confirmed the cytoplasmic and nuclear localization of RrA in human breast cancer SKBR3 cells. Two predicted nuclear localization motifs allow RrA to penetrate into the cell nucleus and inhibit telomerase. Chromatin relaxation promoted by different agents can increase the ability of RrA to suppress the expression of telomerase main catalytic subunit. Our study demonstrated for the first time the ability of RrA to penetrate into human cancer cells and the involvement of clathrin receptors in this process.

Indirubin derivatives inhibit SFKs/Stat signaling associated with apoptosis in human cancer cells

Planta Medica ◽  
2008 ◽  
Vol 74 (09) ◽  
Author(s):  
S Nam ◽  
R Buettner ◽  
X Liu ◽  
J Turkson ◽  
D Kim ◽  
...  
Keyword(s):  
Cancer Cells ◽  
Human Cancer ◽  
Human Cancer Cells ◽  
Stat Signaling
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