scholarly journals cAMP signaling induces rapid loss of histone H3 phosphorylation in mammary adenocarcinoma-derived cell lines

2008 ◽  
Vol 314 (1) ◽  
pp. 1-10 ◽  
Author(s):  
Pedro Rodriguez-Collazo ◽  
Sara K. Snyder ◽  
Rebecca C. Chiffer ◽  
Jordanka Zlatanova ◽  
Sanford H. Leuba ◽  
...  
Keyword(s):  
Cell Lines ◽  
Histone H3 ◽  
Mammary Adenocarcinoma ◽  
Camp Signaling ◽  
Rapid Loss ◽  
H3 Phosphorylation ◽  
Histone H3 Phosphorylation

scholarly journals Sangivamycin and its derivatives inhibit Haspin-Histone H3-survivin signaling and induce pancreatic cancer cell death

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Ligia I. Bastea ◽  
Laeticia M. A. Hollant ◽  
Heike R. Döppler ◽  
Elizabeth M. Reid ◽  
Peter Storz
Keyword(s):  
Pancreatic Cancer ◽  
Cell Death ◽  
Cell Lines ◽  
Apoptotic Cell ◽  
Treatment Options ◽  
Histone H3 ◽  
Current Treatment ◽  
Cancer Cell Death ◽  
H3 Phosphorylation ◽  
Histone H3 Phosphorylation

Abstract Current treatment options for patients with pancreatic cancer are suboptimal, resulting in a five year survival rate of about 9%. Difficulties with treatment are due to an immunosuppressive, fibrotic tumor microenvironment that prevents drugs from reaching tumor cells, but also to the limited efficacy of existing FDA-approved chemotherapeutic compounds. We here show that the nucleoside analog Sangivamycin and its closely-related compound Toyocamycin target PDA cell lines, and are significantly more efficient than Gemcitabine. Using KINOMEscan screening, we identified the kinase Haspin, which is overexpressed in PDA cell lines and human PDA samples, as a main target for both compounds. Inhibition of Haspin leads to a decrease in Histone H3 phosphorylation and prevents Histone H3 binding to survivin, thus providing mechanistic insight of how Sangivamycin targets cell proliferation, mitosis and induces apoptotic cell death. In orthotopically implanted tumors in mice, Sangivamycin was efficient in decreasing the growth of established tumors. In summary, we show that Sangivamycin and derivatives can be an efficient new option for treatment of PDA.

scholarly journals cAMP signaling regulates histone H3 phosphorylation and mitotic entry through a disruption of G2 progression

2008 ◽  
Vol 314 (15) ◽  
pp. 2855-2869 ◽  
Author(s):  
Pedro Rodriguez-Collazo ◽  
Sara K. Snyder ◽  
Rebecca C. Chiffer ◽  
Erin A. Bressler ◽  
Ty C. Voss ◽  
...  
Keyword(s):  
Histone H3 ◽  
Camp Signaling ◽  
Mitotic Entry ◽  
H3 Phosphorylation ◽  
Histone H3 Phosphorylation

scholarly journals Glutamate induces histone H3 phosphorylation but not acetylation in striatal neurons: role of mitogen- and stress-activated kinase-1

2006 ◽  
Vol 101 (3) ◽  
pp. 697-708 ◽  
Author(s):  
Karen Brami-Cherrier ◽  
Jeremie Lavaur ◽  
Christiane Pagès ◽  
J. Simon C. Arthur ◽  
Jocelyne Caboche
Keyword(s):  
Histone H3 ◽  
Striatal Neurons ◽  
H3 Phosphorylation ◽  
Histone H3 Phosphorylation

scholarly journals Squamocin modulates histone H3 phosphorylation levels and induces G1 phase arrest and apoptosis in cancer cells

BMC Cancer ◽  
2011 ◽  
Vol 11 (1) ◽  
Author(s):  
Chien-Chih Lee ◽  
Yi-Hsiung Lin ◽  
Wen-Hsin Chang ◽  
Pei-Chin Lin ◽  
Yang-Chang Wu ◽  
...  
Keyword(s):  
Cancer Cells ◽  
Histone H3 ◽  
G1 Phase ◽  
Phase Arrest ◽  
H3 Phosphorylation ◽  
G1 Phase Arrest ◽  
Histone H3 Phosphorylation ◽  
Apoptosis In Cancer Cells

scholarly journals NIK Is Involved in Nucleosomal Regulation by Enhancing Histone H3 Phosphorylation by IKKα

2006 ◽  
Vol 281 (27) ◽  
pp. 18684-18690 ◽  
Author(s):  
Gye Young Park ◽  
Xuerong Wang ◽  
Ningning Hu ◽  
Tetyana V. Pedchenko ◽  
Timothy S. Blackwell ◽  
...  
Keyword(s):  
Histone H3 ◽  
H3 Phosphorylation ◽  
Histone H3 Phosphorylation
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