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Pancreatic Neoplasms: HELP
Articles by Shinya Kikuchi
Based on 4 articles published since 2010
(Why 4 articles?)
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Between 2010 and 2020, Shin Kikuchi wrote the following 4 articles about Pancreatic Neoplasms.
 
+ Citations + Abstracts
1 Article Tricellular tight junction protein LSR/angulin-1 contributes to the epithelial barrier and malignancy in human pancreatic cancer cell line. 2020

Kyuno, Takuro / Kyuno, Daisuke / Kohno, Takayuki / Konno, Takumi / Kikuchi, Shin / Arimoto, Chihiro / Yamaguchi, Hiroshi / Imamura, Masafumi / Kimura, Yasutoshi / Kondoh, Masuo / Takemasa, Ichiro / Kojima, Takashi. ·Department of Surgery, Surgical Oncology and Science, Sapporo Medical University School of Medicine, Sapporo, Japan. · Department of Cell Science, Research Institute for Frontier Medicine, Sapporo Medical University School of Medicine, South-1, West-17, Chuo-ku, Sapporo, 060-8556, Japan. · Department of Anatomy, Sapporo Medical University School of Medicine, Sapporo, Japan. · Department of Obstetrics and Gynecology, Sapporo Medical University School of Medicine, Sapporo, Japan. · Drug Discovery Center, Graduate School of Pharmaceutical Sciences, Osaka University, Suita, Japan. · Department of Cell Science, Research Institute for Frontier Medicine, Sapporo Medical University School of Medicine, South-1, West-17, Chuo-ku, Sapporo, 060-8556, Japan. ktakashi@sapmed.ac.jp. ·Histochem Cell Biol · Pubmed #31650247.

ABSTRACT: Lipolysis-stimulated lipoprotein receptor (LSR)/angulin-1 is a crucial molecule of tricellular contacts in the epithelial barrier of normal cells and the malignancy of cancer cells. To investigate whether LSR/angulin-1 affects the epithelial barrier and malignancy in human pancreatic cancer, human pancreatic cancer cell line HPAC was used. Treatment with EGF or TGF-β increased the expression of LSR, but not tricellulin (TRIC), and induced the localization of LSR and TRIC to bicellular tight junctions from tricellular tight junctions. TGF-β receptor type-1 inhibitor EW-7197 prevented changes of the distribution and the barrier function of LSR by TGF-β. Knockdown of LSR increased cell migration, invasion, proliferation and EGF ligand amphiregulin expression and decreased the epithelial barrier. Treatment with amphiregulin induced cell migration and invasion and knockdown of amphiregulin prevented the increases of cell migration, invasion and proliferation caused by knockdown of LSR. Treatment with LSR ligand peptide angubindin-1 decreased the epithelial barrier and the expression of LSR, but not TRIC, and increased cell invasion. Knockdown of TRIC decreased cell migration and the epithelial barrier. In immunohistochemical analysis of human pancreatic cancer tissues, LSR and TRIC were found to be localized at the cell membranes of normal pancreatic ducts and well-differentiated pancreatic ductal adenocarcinomas (PDAC), whereas in poorly differentiated PDAC, LSR was weakly detected in the cytoplasm. Amphiregulin was highly expressed in the cytoplasm of well- and poorly differentiated PDAC. In pancreatic cancer, LSR contributes to the epithelial barrier and malignancy via growth factors and may be a potential targeting molecule in the therapy.

2 Article Diagnostic yield of the plasma free amino acid index for pancreatic cancer in patients with diabetes mellitus. 2019

Mizuno, Suguru / Isayama, Hiroyuki / Nakai, Yousuke / Ishigaki, Kazunaga / Saito, Kei / Sato, Tatsuya / Takeda, Tsuyoshi / Hakuta, Ryunosuke / Saito, Tomotaka / Takahara, Naminatsu / Kogure, Hirofumi / Ijichi, Hideaki / Tateishi, Keisuke / Tada, Minoru / Shikata, Nahoko / Tagami, Tomoyuki / Kikuchi, Shinya / Yamamoto, Hiroshi / Yamakado, Minoru / Koike, Kazuhiko. ·Department of Gastroenterology, Graduate School of Medicine, The University of Tokyo, Tokyo, Japan. · Department of Gastroenterology, Graduate School of Medicine, The University of Tokyo, Tokyo, Japan; Department of Gastroenterology, Graduate School of Medicine, Juntendo University, Tokyo, Japan. Electronic address: isayama-tky@umin.ac.jp. · Research Institute for Bioscience Products & Fine Chemicals, Ajinomoto Co., Inc., Kanagawa, Japan. · Department of Nursing, Ashikaga University, Tochigi, Japan; Center for Multiphasic Health Testing and Services, Mitsui Memorial Hospital, Tokyo, Japan. ·Pancreatology · Pubmed #31320196.

ABSTRACT: OBJECTIVES: A multivariate index calculated using plasma free amino acids (PFAA index) was reported as a diagnostic biomarker for pancreatic cancer (PaC). Although diabetes mellitus (DM) is expected to be an early diagnostic indicator of PaC, identifying the high-risk individuals among patients with DM is warranted. We evaluated the diagnostic yield of the PFAA index for PaC in patients with DM. METHODS: We compared the diagnostic yield of the PFAA index between individuals with and those without DM. Cases and controls were recruited prospectively, and controls were matched to cases at a 1:1 ratio for age, sex, and DM status. RESULTS: A total of 180 case-control pairs were included in the analysis. The prevalence of DM was 53.3%. The sensitivity of the PFAA index was 66.7% in cases with DM and 56.0% in those without DM (P = 0.14), and the specificity was 92.7% in controls with DM and 94.0% in those without DM (P = 0.95). CONCLUSIONS: This matched case-control study revealed a comparable diagnostic yield of the PFAA index for PaC in individuals with and those without DM. The PFAA index can be used as a biomarker for further diagnostic imaging in selected patients with DM.

3 Article A Novel Multivariate Index for Pancreatic Cancer Detection Based On the Plasma Free Amino Acid Profile. 2015

Fukutake, Nobuyasu / Ueno, Makoto / Hiraoka, Nobuyoshi / Shimada, Kazuaki / Shiraishi, Koichi / Saruki, Nobuhiro / Ito, Toshifumi / Yamakado, Minoru / Ono, Nobukazu / Imaizumi, Akira / Kikuchi, Shinya / Yamamoto, Hiroshi / Katayama, Kazuhiro. ·Department of Hepatobiliary and Pancreatic Oncology, Osaka Medical Center of Cancer and Cardiovascular Diseases, Osaka, Japan. · Division of Hepatobiliary and Pancreatic Medical Oncology, Kanagawa Cancer Center, Kanagawa, Japan. · Division of Pathology and Clinical Laboratories, National Cancer Center Hospital, Tokyo, Japan. · Hepatobiliary and Pancreatic Surgery Division, National Cancer Center Hospital, Tokyo, Japan. · Division of Gastroenterology, Department of Internal Medicine, Tokai University Oiso Hospital, Kanagawa, Japan. · Department of Anesthesia, Gunma Prefectural Cancer Center, Gunma, Japan. · Department of Gastroenterology and Hepatology, Japan Community Healthcare Organization (JCHO), Osaka Hospital, Osaka, Japan. · Center for Multiphasic Health Testing and Services, Mitsui Memorial Hospital, Tokyo, Japan. · Institute for Innovation, Ajinomoto Co., Inc., Kanagawa, Japan. ·PLoS One · Pubmed #26133769.

ABSTRACT: BACKGROUND: The incidence of pancreatic cancer (PC) continues to increase in the world, while most patients are diagnosed with advanced stages and survive <12 months. This poor prognosis is attributable to difficulty of early detection. Here we developed and evaluated a multivariate index composed of plasma free amino acids (PFAAs) for early detection of PC. METHODS: We conducted a cross-sectional study in multi-institutions in Japan. Fasting plasma samples from PC patients (n = 360), chronic pancreatitis (CP) patients (n = 28), and healthy control (HC) subjects (n = 8372) without apparent cancers who were undergoing comprehensive medical examinations were collected. Concentrations of 19 PFAAs were measured by liquid chromatography-mass spectrometry. We generated an index consisting of the following six PFAAs: serine, asparagine, isoleucine, alanine, histidine, and tryptophan as variables for discrimination in a training set (120 PC and matching 600 HC) and evaluation in a validation set (240 PC, 28 CP, and 7772 HC). RESULTS: Several amino acid concentrations in plasma were significantly altered in PC. Plasma tryptophan and histidine concentrations in PC were particularly low, while serine was particularly higher than that of HC. The area under curve (AUC) based on receiver operating characteristic (ROC) curve analysis of the resulting index to discriminate PC from HC were 0.89 [95% confidence interval (CI), 0.86-0.93] in the training set. In the validation set, AUCs based on ROC curve analysis of the PFAA index were 0.86 (95% CI, 0.84-0.89) for all PC patients versus HC subjects, 0.81 (95% CI, 0.75-0.86) for PC patients from stage IIA to IIB versus HC subjects, and 0.87 (95% CI, 0.80-0.93) for all PC patients versus CP patients. CONCLUSIONS: These findings suggest that the PFAA profile of PC was significantly different from that of HC. The PFAA index is a promising biomarker for screening and diagnosis of PC.

4 Article c-Jun N-terminal kinase inhibitor SP600125 enhances barrier function and elongation of human pancreatic cancer cell line HPAC in a Ca-switch model. 2015

Konno, Takumi / Ninomiya, Takafumi / Kohno, Takayuki / Kikuchi, Shin / Sawada, Norimasa / Kojima, Takashi. ·Department of Cell Science, Research Institute for Frontier Medicine, Sapporo Medical University School of Medicine, S1. W17., Sapporo, 060-8556, Japan. ·Histochem Cell Biol · Pubmed #25511417.

ABSTRACT: c-Jun N-terminal kinase (JNK), known as a stress-activated protein kinase, regulates normal epithelial biological processes, including assembly of adherens and tight junctions, and it is involved in the development of several cancers. The JNK inhibitor SP600125 enhances epithelial barrier function through modulation of tight junction molecules in normal human pancreatic epithelial cells. Furthermore, this JNK inhibitor suppresses the growth of human pancreatic cancer cells. However, the effects of SP600125 on the epithelial barrier in human pancreatic cancer cells remain unknown. In the present study, the JNK inhibitor SP600125 markedly enhanced the barrier function and cell elongation of well-differentiated human pancreatic cancer cell line HPAC in a Ca-switch model. The epithelial barrier function induced by SP600125 was regulated by phosphorylated β-catenin without changes in the tight junction molecules. The cell elongation induced by SP600125 was closely related to the expression of the F-actin-binding protein DrebrinE. These findings suggest that JNK is involved in the regulation of the epithelial barrier function and cell shape during remodeling of pancreatic cancer cells. The JNK inhibitor SP600125 may have potential as a therapeutic drug for pancreatic cancer via induction of differentiation.