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Book: Genomic instability and carcinogenesis

Hirohashi, Setsuo

(Extended abstracts for the ... international symposium of the Princess Takamatsu Cancer Research Fund ; 26)

1996

Author's details	ed. by Setsuo Hirohashi
Series title	Extended abstracts for the ... international symposium of the Princess Takamatsu Cancer Research Fund ; 26
Collection
Language	English
Size	V, 117 S. : Ill., graph. Darst.
Publisher	Princess Takamatsu Cancer Research Fund
Publishing place	Tokyo
Publishing country	United States
Document type	Book
HBZ-ID	HT010079203
Database	Catalogue ZB MED Medicine, Health

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Article ; Online: Application of 2D-DIGE in cancer proteomics toward personalized medicine.

Kondo, Tadashi / Hirohashi, Setsuo

Methods in molecular biology (Clifton, N.J.)

2009 Volume 577, Page(s) 135–154

Abstract: Two-dimensional difference gel electrophoresis (2D-DIGE) is an advanced variation of two-dimensional polyacrylamide gel electrophoresis (2D-PAGE); protein samples are labeled with different fluorescent dyes, mixed and separated by 2D-PAGE. 2D-DIGE solves ...

Abstract	Two-dimensional difference gel electrophoresis (2D-DIGE) is an advanced variation of two-dimensional polyacrylamide gel electrophoresis (2D-PAGE); protein samples are labeled with different fluorescent dyes, mixed and separated by 2D-PAGE. 2D-DIGE solves major inherent drawbacks of 2D-PAGE, demonstrating great utility in biomarker studies. Biomarker development requires quantitative, reproducible, highly sensitive and high-throughput experimental platforms, and 2D-DIGE meets these criteria. Here we demonstrate the advantages of 2D-DIGE and discuss the possibilities 2D-DIGE offers for further, more comprehensive proteome studies.
MeSH term(s)	Biomarkers, Tumor/analysis ; Databases, Protein ; Electrophoresis, Gel, Two-Dimensional/methods ; Fluorescent Dyes ; High-Throughput Screening Assays/methods ; Humans ; Molecular Biology/methods ; Neoplasm Proteins/analysis ; Neoplasms/chemistry ; Precision Medicine/methods ; Proteomics/methods ; Proteomics/statistics & numerical data
Chemical Substances	Biomarkers, Tumor ; Fluorescent Dyes ; Neoplasm Proteins
Language	English
Publishing date	2009
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-60761-232-2_11
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Book: Gan no hontai kaimei kara gan kokufuku e

Hirohashi, Setsuo

gan kokufuku shin 10-kanen senryaku purojekuto kenkyū : dai II-ki sōkatsushū

2001

Title translation	Understanding and curing cancer.
Title variant	Gan kokufuku shin 10-kanen senryaku purojekuto kenkyū : dai II-ki sōkatsushū
Author's details	[sōkatsuhan hanchō Hirohashi Setsuo]
MeSH term(s)	Neoplasms ; Medical Oncology
Language	Japanese
Size	240 p. :, ill.
Publisher	Kokuritsu Gan Sentā Kenkyūjo, Kōsei Rōdōshō
Publishing place	Tōkyō
Document type	Book
Note	Sōkatsuhan hanchō: Hirohashi Setsuo, Kokuritsu Gan Sentā Kenkyūjo - colophon
Database	Catalogue of the US National Library of Medicine (NLM)

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Article: [E-cadherin cell adhesion system in human cancer].

Shibata, Tatsuhiro / Hirohashi, Setsuo

Seikagaku. The Journal of Japanese Biochemical Society

2006 Volume 78, Issue 7, Page(s) 647–656

MeSH term(s)	Actinin/physiology ; Cadherins/genetics ; Cadherins/physiology ; Catenins/physiology ; Cell Adhesion/genetics ; Cell Adhesion Molecules/physiology ; Gene Expression Regulation, Neoplastic/genetics ; Humans ; Methylation ; Microfilament Proteins/physiology ; Mutation ; Neoplasm Invasiveness/genetics ; Neoplasms/pathology ; Phosphoproteins/physiology ; Phosphorylation ; Promoter Regions, Genetic/genetics ; Signal Transduction
Chemical Substances	ACTN4 protein, human ; Cadherins ; Catenins ; Cell Adhesion Molecules ; Microfilament Proteins ; Phosphoproteins ; delta catenin ; Actinin (11003-00-2)
Language	Japanese
Publishing date	2006-07
Publishing country	Japan
Document type	Journal Article ; Review
ZDB-ID	282319-6
ISSN	0037-1017
ISSN	0037-1017
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Article ; Online: Alterations of DNA methylation associated with abnormalities of DNA methyltransferases in human cancers during transition from a precancerous to a malignant state.

Kanai, Yae / Hirohashi, Setsuo

Carcinogenesis

2007 Volume 28, Issue 12, Page(s) 2434–2442

Abstract: Alterations of DNA methylation are one of the most consistent epigenetic changes in human cancers. Human cancers generally show global DNA hypomethylation accompanied by region-specific hypermethylation. Alterations of DNA methylation may result in ... ...

Abstract	Alterations of DNA methylation are one of the most consistent epigenetic changes in human cancers. Human cancers generally show global DNA hypomethylation accompanied by region-specific hypermethylation. Alterations of DNA methylation may result in chromosomal instability as a result of changes in chromatin structure. DNA hypermethylation of CpG islands silences various tumor-related genes. Alterations of DNA methylation are frequently observed in cancers associated with chronic inflammation and/or persistent infection with viruses or other pathogenic microorganisms, such as hepatitis B or C viruses, Epstein-Barr virus, human papillomavirus and Helicobacter pylori, or with cigarette smoking. Accumulating evidence suggests that alterations of DNA methylation are involved even in the early and precancerous stages. On the other hand, in patients with cancers, aberrant DNA methylation is significantly associated with poorer tumor differentiation, tumor aggressiveness and poor prognosis. Precancerous conditions showing alterations of DNA methylation may progress rapidly and generate more malignant cancers. DNA methyltransferase (DNMT) 1 over-expression is not a secondary result of increased cell proliferative activity but is significantly correlated with the CpG island methylator phenotype, which is defined as frequent DNA hypermethylation of C-type CpG islands that are usually methylated in a cancer-specific (not age-dependent) manner. Splicing alteration of DNMT3b may result in chromosomal instability through DNA hypomethylation of pericentromeric satellite regions. Alteration of DNA methylation may become an indicator for carcinogenetic risk estimation and early diagnosis of cancers and a biological predictor of poor prognosis in patients with cancers. Correction of DNA methylation status may offer a new strategy for prevention and therapy of cancers.
MeSH term(s)	Alternative Splicing ; Cell Transformation, Neoplastic ; Chromosome Aberrations ; CpG Islands ; DNA (Cytosine-5-)-Methyltransferase 1 ; DNA (Cytosine-5-)-Methyltransferases/genetics ; DNA (Cytosine-5-)-Methyltransferases/physiology ; DNA Methylation ; Humans ; Neoplasms/metabolism ; Neoplasms/pathology ; Precancerous Conditions/metabolism ; Precancerous Conditions/pathology ; DNA Methyltransferase 3B
Chemical Substances	DNA (Cytosine-5-)-Methyltransferase 1 (EC 2.1.1.37) ; DNA (Cytosine-5-)-Methyltransferases (EC 2.1.1.37)
Language	English
Publishing date	2007-09-24
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	603134-1
ISSN	1460-2180 ; 0143-3334
ISSN (online)	1460-2180
ISSN	0143-3334
DOI	10.1093/carcin/bgm206
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Article ; Online: Application of highly sensitive fluorescent dyes (CyDye DIGE Fluor saturation dyes) to laser microdissection and two-dimensional difference gel electrophoresis (2D-DIGE) for cancer proteomics.

Kondo, Tadashi / Hirohashi, Setsuo

Nature protocols

2006 Volume 1, Issue 6, Page(s) 2940–2956

Abstract: Proteome data combined with histopathological information provides important, novel clues for understanding cancer biology and reveals candidates for tumor markers and therapeutic targets. We have established an application of a highly sensitive ... ...

Abstract	Proteome data combined with histopathological information provides important, novel clues for understanding cancer biology and reveals candidates for tumor markers and therapeutic targets. We have established an application of a highly sensitive fluorescent dye (CyDye DIGE Fluor saturation dye), developed for two-dimensional difference gel electrophoresis (2D-DIGE), to the labeling of proteins extracted from laser microdissected tissues. The use of the dye dramatically decreases the protein amount and, in turn, the number of cells required for 2D-DIGE; the cells obtained from a 1 mm2 area of an 8-12 microm thick tissue section generate up to 5,000 protein spots in a large-format 2D gel. This protocol allows the execution of large-scale proteomics in a more efficient, accurate and reproducible way. The protocol can be used to examine a single sample in 5 d or to examine hundreds of samples in large-scale proteomics.
MeSH term(s)	Electrophoresis, Gel, Two-Dimensional/methods ; Fluorescent Dyes ; Humans ; Lasers ; Mass Spectrometry ; Microdissection/methods ; Neoplasms/pathology ; Proteomics/methods ; Staining and Labeling/methods ; Statistics as Topic
Chemical Substances	Fluorescent Dyes
Language	English
Publishing date	2006
Publishing country	England
Document type	Journal Article
ZDB-ID	2244966-8
ISSN	1750-2799 ; 1754-2189
ISSN (online)	1750-2799
ISSN	1754-2189
DOI	10.1038/nprot.2006.421
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Oncogenic mutation of PIK3CA in small cell lung carcinoma: a potential therapeutic target pathway for chemotherapy-resistant lung cancer.

Shibata, Tatsuhiro / Kokubu, Akiko / Tsuta, Koji / Hirohashi, Setsuo

Cancer letters

2009 Volume 283, Issue 2, Page(s) 203–211

Abstract: Lung cancer is one of the most prevalent cancers worldwide. This study focused on small cell lung cancer (SCLC), which has a poor clinical prognosis, and attempted to elucidate potential therapeutic molecular targets. A target-specific mutational search ... ...

Abstract	Lung cancer is one of the most prevalent cancers worldwide. This study focused on small cell lung cancer (SCLC), which has a poor clinical prognosis, and attempted to elucidate potential therapeutic molecular targets. A target-specific mutational search revealed mutation of the PIK3CA gene in three of 13 SCLC cell lines and two of 15 primary SCLCs. By introducing these mutant PIK3CA cDNAs, we established artificial "PIK3CA-addicted" cells and found that Tricribine, a small-molecule inhibitor of AKT signaling that is located downstream from PIK3CA, significantly inhibited the growth and colony formation activity of these cells. Using cancer cell lines, we further showed that PIK3CA-mutated SCLC cells are more sensitive to Tricribine than PIK3CA wild-type cells. Additionally, we found that a cisplatin-resistant subclone of PIK3CA-mutant SCLC cells was equally sensitive to Tricribine. This study for the first time uncovered PIK3CA alterations in SCLC, and our findings suggest that anti-AKT molecular therapy could be effective for a subgroup of SCLC, which shows activation of specific genes, such as PIK3CA mutation, and that genetic stratification of SCLC according to the activation status of individual therapeutic target pathways could be clinically beneficial, especially for chemotherapy-resistant/relapsing tumors.
MeSH term(s)	Antineoplastic Agents/pharmacology ; Base Sequence ; Cell Line, Tumor ; Chlorpropamide/analogs & derivatives ; Chlorpropamide/pharmacology ; Class I Phosphatidylinositol 3-Kinases ; Drug Resistance, Neoplasm/genetics ; Humans ; Lung Neoplasms/drug therapy ; Lung Neoplasms/genetics ; Mutagenesis, Site-Directed ; Mutation ; Phosphatidylinositol 3-Kinases/genetics ; Polymerase Chain Reaction ; Small Cell Lung Carcinoma/drug therapy ; Small Cell Lung Carcinoma/genetics
Chemical Substances	API 2 ; Antineoplastic Agents ; Phosphatidylinositol 3-Kinases (EC 2.7.1.-) ; Class I Phosphatidylinositol 3-Kinases (EC 2.7.1.137) ; PIK3CA protein, human (EC 2.7.1.137) ; Chlorpropamide (WTM2C3IL2X)
Language	English
Publishing date	2009-10-08
Publishing country	Ireland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	195674-7
ISSN	1872-7980 ; 0304-3835
ISSN (online)	1872-7980
ISSN	0304-3835
DOI	10.1016/j.canlet.2009.03.038
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Article: Detection of Allele Loss on Chromosome 16q in DNA Isolated from Fine Needle Aspiration Specimens of Breast Tumors

Tsuda, Hitoshi / Sakamaki, Chinami / Shimamura, Kayako / Hirohashi, Setsuo

Acta Cytologica

2011 Volume 40, Issue 4, Page(s) 625–630

Institution	From the Pathology Division and Department of Clinical Laboratory, National Cancer Center Research Institute and Hospital, Tokyo, Japan
Keywords	breast neoplasms ; fine needle aspiration ; heterozygote ; polymerase chain reaction
Language	English
Publishing date	2011-09-30
Publisher	S. Karger AG
Publishing place	Basel, Switzerland
Document type	Article
Note	Original Articles
ZDB-ID	80003-x
ISSN	1938-2650 ; 0001-5547
ISSN (online)	1938-2650
ISSN	0001-5547
DOI	10.1159/000333849
Database	Karger publisher's database

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Article ; Online: Wnt signaling inside the nucleus.

Shitashige, Miki / Hirohashi, Setsuo / Yamada, Tesshi

Cancer science

2008 Volume 99, Issue 4, Page(s) 631–637

Abstract: Accumulation of the beta-catenin protein and transactivation of a certain set of T-cell factor (TCF)-4 target genes by accumulated beta-catenin have been considered crucial in colorectal carcinogenesis. In the present review, we summarize nuclear ... ...

Abstract	Accumulation of the beta-catenin protein and transactivation of a certain set of T-cell factor (TCF)-4 target genes by accumulated beta-catenin have been considered crucial in colorectal carcinogenesis. In the present review, we summarize nuclear proteins that interact with, and regulate, the beta-catenin and TCF and lymphoid enhancer factor (LEF) transcriptional complexes. Our recent series of proteomic studies has also revealed that various classes of nuclear proteins participate in the beta-catenin-TCF-4 complex and modulate its transcriptional activity. Furthermore, the protein composition of the TCF-4-containing nuclear complex is not fixed, but is regulated dynamically by endogenous programs associated with intestinal epithelial cell differentiation and exogenous stimuli. Restoration of the loss-of-function mutation of the adenomatous polyposis coli (APC) gene in colorectal cancer cells does not seem to be a realistic approach with currently available medical technologies, and only signaling molecules downstream of the APC gene product can be considered as targets of pharmacological intervention. Nuclear proteins associated with the beta-catenin-TCF-4 complex may include feasible targets for molecular therapy against colorectal cancer. Recently, an inhibitor of the interaction between CREB-binding protein and beta-catenin was shown to efficiently shut down the transcriptional activity of TCF-4 and induce apoptosis of colorectal cancer cells. We also summarize current strategies in the development of drugs against Wnt signaling.
MeSH term(s)	Animals ; Antineoplastic Agents/isolation & purification ; Antineoplastic Agents/pharmacology ; Antineoplastic Agents/therapeutic use ; Cell Nucleus/metabolism ; Colorectal Neoplasms/drug therapy ; Colorectal Neoplasms/genetics ; Colorectal Neoplasms/metabolism ; Drug Design ; Female ; Gene Expression Regulation, Neoplastic ; Genes, APC ; Humans ; Male ; Mice ; Nuclear Proteins/drug effects ; Nuclear Proteins/metabolism ; TCF Transcription Factors/antagonists & inhibitors ; TCF Transcription Factors/metabolism ; Transcription Factor 7-Like 2 Protein ; Wnt Proteins/antagonists & inhibitors ; Wnt Proteins/metabolism ; beta Catenin/antagonists & inhibitors ; beta Catenin/metabolism
Chemical Substances	Antineoplastic Agents ; Nuclear Proteins ; TCF Transcription Factors ; TCF7L2 protein, human ; Tcf7l2 protein, mouse ; Transcription Factor 7-Like 2 Protein ; Wnt Proteins ; beta Catenin
Language	English
Publishing date	2008-04
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ISSN	1349-7006
ISSN (online)	1349-7006
DOI	10.1111/j.1349-7006.2007.00716.x
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Dysadherin: a new player in cancer progression.

Nam, Jeong-Seok / Hirohashi, Setsuo / Wakefield, Lalage M

Cancer letters

2007 Volume 255, Issue 2, Page(s) 161–169

Abstract: Dysadherin is a cancer-associated cell membrane glycoprotein that promotes experimental cancer metastasis. Here we review recent work that has provided insights into possible mechanisms of action of this newly recognized player in the cancer progression ... ...

Abstract	Dysadherin is a cancer-associated cell membrane glycoprotein that promotes experimental cancer metastasis. Here we review recent work that has provided insights into possible mechanisms of action of this newly recognized player in the cancer progression process. Dysadherin modulates cell phenotype in a number of ways, including down-regulation of E-cadherin-mediated cell adhesion, and up-regulation of chemokine production. In this way, expression of dysadherin in a tumor can influence both the tumor cell itself and the stromal compartment, so as to create conditions that are more permissive for metastatic spread. Dysadherin expression is also an independent prognostic indicator of metastasis and survival for many different types of human cancer. Thus, dysadherin may represent a new molecular target for the visualization, prevention or treatment of advanced cancer.
MeSH term(s)	Amino Acid Sequence ; Disease Progression ; Humans ; Membrane Glycoproteins/analysis ; Membrane Glycoproteins/drug effects ; Membrane Glycoproteins/metabolism ; Molecular Sequence Data ; Neoplasm Proteins/analysis ; Neoplasm Proteins/drug effects ; Neoplasm Proteins/metabolism ; Neoplasms/metabolism ; Neoplasms/pathology ; Prognosis
Chemical Substances	FXYD5 protein, human ; Membrane Glycoproteins ; Neoplasm Proteins
Language	English
Publishing date	2007-04-17
Publishing country	Ireland
Document type	Journal Article ; Research Support, N.I.H., Intramural ; Review
ZDB-ID	195674-7
ISSN	1872-7980 ; 0304-3835
ISSN (online)	1872-7980
ISSN	0304-3835
DOI	10.1016/j.canlet.2007.02.018
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