Papers - KOJIMA Takashi

Altered expression of claudin-1, claudin-7, and tricellulin regardless of human papilloma virus infection in human tonsillar squamous cell carcinoma

Atsushi Kondoh, Ken-Ichi Takano, Takashi Kojima, Tsuyoshi Ohkuni, Ryuta Kamekura, Noriko Ogasawara, Mitsuru Go, Norimasa Sawada, Tetsuo Himi

ACTA OTO-LARYNGOLOGICA ( INFORMA HEALTHCARE )  131 ( 8 ) 861 - 868  2011.08  [Refereed]

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Conclusions: Altered expression of claudin-1, claudin-7, and tricellulin in early tonsillar squamous cell carcinoma (SCC) independent of human papilloma virus (HPV) infection may lead to tumor progression. Objectives: Integral tight junction proteins, the claudins and tricellulin, play a crucial role in all tissues. HPV is significantly associated with tonsillar SCC. We sought to determine the expression of claudin-1, claudin-7, and tricellulin in HPV-infected and HPV-free tonsillar SCC. Methods: Twenty-eight tonsillar SCCs were studied by immunohistochemical analysis and real-time reverse transcription polymerase chain reaction with in situ hybridization analysis. Results: Compared with normal tissues, claudin-1 was strongly expressed, whereas claudin-7 and tricellulin were weakly expressed or were absent in primary SCC and metastatic lymph nodes. Claudin-7 and tricellulin were markedly reduced at all stages of tumor development. In situ hybridization analysis showed no correlation between HPV infection and altered expression of the tight junction proteins.

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A nuclear factor-κB signaling pathway via protein kinase C δ regulates replication of respiratory syncytial virus in polarized normal human nasal epithelial cells.

Masaki T, Kojima T, Okabayashi T, Ogasawara N, Ohkuni T, Obata K, Takasawa A, Murata M, Tanaka S, Hirakawa S, Fuchimoto J, Ninomiya T, Fujii N, Tsutsumi H, Himi T, Sawada N

Molecular biology of the cell ( 13 )  22   2144 - 2156  2011.07  [Refereed]

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Transcriptional regulation of claudin-18 via specific protein kinase C signaling pathways and modification of DNA methylation in human pancreatic cancer cells.

Tatsuya Ito, Takashi Kojima, Hiroshi Yamaguchi, Daisuke Kyuno, Yasutoshi Kimura, Masafumi Imamura, Akira Takasawa, Masaki Murata, Satoshi Tanaka, Koichi Hirata, Norimasa Sawada

Journal of cellular biochemistry   112 ( 7 ) 1761 - 72  2011.07  [Refereed]  [International journal]

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Since claudin-18 (Cldn18) is overexpressed in precursor lesion PanIN and pancreatic duct carcinoma, it serves as a diagnostic marker and a target of immunotherapy. The stomach isoform of Cldn18, Cldn18a2 is regulated via a PKC/MAPK/AP-1-dependent pathway in PKC activator 12-O-tetradecanoylphorbol 13-acetate (TPA)-stimulated gastric cancer cells. However, little is known about how Cldn18 is regulated, not only in pancreatic duct carcinoma but also in normal human pancreatic duct epithelial cells (HPDE cells). In the present study, four pancreatic cancer cell lines, HPAF-II, HPAC, PANC-1 and BXPC3, and hTERT-HPDE cells in which the hTERT gene was introduced into HPDE cells in primary culture, were treated with TPA. In all human pancreatic cancer cell lines and hTERT-HPDE cells, Cldn18 mRNA indicated as Cldn18a2 was markedly induced by TPA and in well- or moderately differentiated human pancreatic cancer cells HPAF-II and HPAC and hTERT-HPDE cells, the protein was also strongly increased. The upregulation of Cldn18 by TPA in human pancreatic cancer cell lines was prevented by inhibitors of PKCδ, PKCε, and PKCα, whereas the upregulation of Cldn18 by TPA in hTERT-HPDE cells was prevented by inhibitors of PKCδ, PKCθ, and PKCα. Furthermore, a CpG island was identified within the coding sequence of the Cldn18 gene and treatment with the demethylating agent 5-azadeoxycytidine enhanced upregulation of Cldn18 by TPA in HPAF-II and HPAC, but not hTERT-HPDE cells. Our findings suggest that in human pancreatic cancer cells, Cldn18 is primarily regulated at the transcriptional level via specific PKC signaling pathways and modified by DNA methylation.

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Poly(I:C) reduces expression of JAM-A and induces secretion of IL-8 and TNF-α via distinct NF-κB pathways in human nasal epithelial cells.

Ohkuni T, Kojima T, Ogasawara N, Masaki T, Fuchimoto J, Kamekura R, Koizumi J, Ichimiya S, Murata M, Tanaka S, Himi T, Sawada N

Toxicology and applied pharmacology ( 1 )  250   29 - 38  2011.01  [Refereed]

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Tricellulin Is Expressed in Autotypic Tight Junctions of Peripheral Myelinating Schwann Cells

Shin Kikuchi, Takafumi Ninomiya, Haruyuki Tatsumi, Norimasa Sawada, Takashi Kojima

JOURNAL OF HISTOCHEMISTRY & CYTOCHEMISTRY ( SAGE PUBLICATIONS LTD )  58 ( 12 ) 1067 - 1073  2010.12  [Refereed]

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Autotypic tight junctions are formed by tight junction-like structures in three regions of myelinating Schwann cells, the paranodal loops, Schmidt-Lanterman incisures, and outer/inner mesaxons, and various tight junction molecules, including claudin-19 and junctional adhesion molecule (JAM)-C. Our findings demonstrate the identification and subcellular distribution of a novel tricellular tight junction protein, tricellulin (TRIC), in the autotypic tight junctions of mouse myelinating Schwann cells, compared with the autotypic adherens junction protein E-cadherin and the autotypic tight junction protein JAM-C, which are expressed in the paranodal loops, Schmidt-Lanterman incisures, and mesaxons. In real-time RT-PCR, the expression level of TRIC mRNA was about 10-fold higher in the sciatic nerve than in the spinal cord or cerebrum. In immunostaining, TRIC signals were completely restricted to the peripheral nervous system (PNS) and strongly concentrated at the paranodal loops, Schmidt-Lanterman incisures, and mesaxons of myelinating Schwann cells. In addition, TRIC was expressed in the thin region of the paranode and there was a gap between TRIC and the Na(+) channel. Furthermore, TRIC was more distally located from the node than E-cadherin and was colocalized with JAM-C. It is possible that TRIC may be a component to maintain the integrity for PNS myelin function and morphology. This manuscript contains online supplemental material at http://www.jhc.org. Please visit this article online to view these materials. (J Histochem Cytochem 58:1067-1073, 2010)

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c-Jun N-terminal kinase is largely involved in the regulation of tricellular tight junctions via tricellulin in human pancreatic duct epithelial cells.

Kojima T, Fuchimoto J, Yamaguchi H, Ito T, Takasawa A, Ninomiya T, Kikuchi S, Ogasawara N, Ohkuni T, Masaki T, Hirata K, Himi T, Sawada N

Journal of cellular physiology ( 3 )  225   720 - 733  2010.11  [Refereed]

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Transcriptional control of tight junction proteins via a protein kinase C signal pathway in human telomerase reverse transcriptase-transfected human pancreatic duct epithelial cells.

Yamaguchi H, Kojima T, Ito T, Kimura Y, Imamura M, Son S, Koizumi J, Murata M, Nagayama M, Nobuoka T, Tanaka S, Hirata K, Sawada N

The American journal of pathology ( 2 )  177   698 - 712  2010.08  [Refereed]

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PPARgamma agonists upregulate the barrier function of tight junctions via a PKC pathway in human nasal epithelial cells.

Ogasawara N, Kojima T, Go M, Ohkuni T, Koizumi J, Kamekura R, Masaki T, Murata M, Tanaka S, Fuchimoto J, Himi T, Sawada N

Pharmacological research : the official journal of the Italian Pharmacological Society ( 6 )  61   489 - 498  2010.06  [Refereed]

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Thymic stromal lymphopoietin induces tight junction protein claudin-7 via NF-kappaB in dendritic cells.

Kamekura R, Kojima T, Takashima A, Koizumi J, Ogasawara N, Go M, Takano K, Murata M, Tanaka S, Ichimiya S, Himi T, Sawada N

Histochemistry and cell biology ( 3 )  133   339 - 348  2010.03  [Refereed]

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Expression and localization of tricellulin in human nasal epithelial cells in vivo and in vitro

Tsuyoshi Ohkuni, Takashi Kojima, Noriko Ogasawara, Tomoyuki Masaki, Takafumi Ninomiya, Shin Kikuchi, Mitsuru Go, Ken-ichi Takano, Tetsuo Himi, Norimasa Sawada

MEDICAL MOLECULAR MORPHOLOGY ( SPRINGER TOKYO )  42 ( 4 ) 204 - 211  2009.12  [Refereed]

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Tricellulin was identified as the first marker of the tricellular tight junction, which forms at the meeting points of three cells, and it is required for the maintenance of the transepithelial barrier. Although it is also considered to be important for the mucosal barrier of the upper respiratory tract, little is known about its expression and localization. In the present study, we examined the expression and localization of tricellulin in normal human nasal epithelial cells in vivo and in vitro, especially using primary cultures and telomerase reverse transcriptase (hTERT)-transfected cells. In human nasal epithelial cells in vivo and in vitro, mRNA and protein of tricellulin were detected. It was localized not only at tricellular contacts but also at bicellular borders, and in part colocalized with occludin. In human nasal epithelium, by immunoelectron microscopy analysis, tricellulin-associated gold particles were observed around the junction-like structure of the uppermost region. By treatment with 10% fetal bovine serum (FBS), expression of tricellulin mRNA was weakly increased, whereas that of bicellular tight junction molecules was strongly increased, in real-time PCR. These results suggest that tricellulin is stably expressed in human nasal epithelial cells and may play an important role for the sealing of the corner at tricellular contacts to prevent infiltration by various inhaled viruses and antigens.

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Induction of JAM-A during differentiation of human THP-1 dendritic cells.

Ogasawara N, Kojima T, Go M, Fuchimoto J, Kamekura R, Koizumi J, Ohkuni T, Masaki T, Murata M, Tanaka S, Ichimiya S, Himi T, Sawada N

Biochemical and biophysical research communications ( 3 )  389   543 - 549  2009.11  [Refereed]

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Thymic stromal lymphopoietin enhances tight-junction barrier function of human nasal epithelial cells.

Kamekura R, Kojima T, Koizumi J, Ogasawara N, Kurose M, Go M, Harimaya A, Murata M, Tanaka S, Chiba H, Himi T, Sawada N

Cell and tissue research ( 2 )  338   283 - 293  2009.11  [Refereed]

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Tight junction proteins and signal transduction pathways in hepatocytes.

Kojima T, Murata M, Yamamoto T, Lan M, Imamura M, Son S, Takano K, Yamaguchi H, Ito T, Tanaka S, Chiba H, Hirata K, Sawada N

Histology and histopathology ( 11 )  24   1463 - 1472  2009.11  [Refereed]

PubMed

Knockdown of tight junction protein claudin-2 prevents bile canalicular formation in WIF-B9 cells.

Son S, Kojima T, Decaens C, Yamaguchi H, Ito T, Imamura M, Murata M, Tanaka S, Chiba H, Hirata K, Sawada N

Histochemistry and cell biology ( 3 )  131   411 - 424  2009.03  [Refereed]

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IGF-I regulates tight-junction protein claudin-1 during differentiation of osteoblast-like MC3T3-E1 cells via a MAP-kinase pathway.

Hatakeyama N, Kojima T, Iba K, Murata M, Thi MM, Spray DC, Osanai M, Chiba H, Ishiai S, Yamashita T, Sawada N

Cell and tissue research ( 2 )  334   243 - 254  2008.11  [Refereed]

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Protein kinase C enhances tight junction barrier function of human nasal epithelial cells in primary culture by transcriptional regulation.

Koizumi J, Kojima T, Ogasawara N, Kamekura R, Kurose M, Go M, Harimaya A, Murata M, Osanai M, Chiba H, Himi T, Sawada N

Molecular pharmacology ( 2 )  74   432 - 442  2008.08  [Refereed]

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Expression of tight junction proteins in epithelium including Ck20-positive M-like cells of human adenoids in vivo and in vitro.

Takano K, Kojima T, Ogasawara N, Go M, Kikuchi S, Ninomiya T, Kurose M, Koizumi J, Kamekura R, Murata M, Tanaka S, Chiba H, Himi T, Sawada N

Journal of molecular histology ( 3 )  39   265 - 273  2008.06  [Refereed]

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Transforming growth factor-beta induces epithelial to mesenchymal transition by down-regulation of claudin-1 expression and the fence function in adult rat hepatocytes.

Kojima T, Takano K, Yamamoto T, Murata M, Son S, Imamura M, Yamaguchi H, Osanai M, Chiba H, Himi T, Sawada N

Liver international : official journal of the International Association for the Study of the Liver ( 4 )  28   534 - 545  2008.04  [Refereed]

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Induction of claudins in passaged hTERT-transfected human nasal epithelial cells with an extended life span.

Kurose M, Kojima T, Koizumi J, Kamekura R, Ninomiya T, Murata M, Ichimiya S, Osanai M, Chiba H, Himi T, Sawada N

Cell and tissue research ( 1 )  330   63 - 74  2007.10  [Refereed]

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Changes of gap and tight junctions during differentiation of human nasal epithelial cells using primary human nasal epithelial cells and primary human nasal fibroblast cells in a noncontact coculture system.

Koizumi J, Kojima T, Kamekura R, Kurose M, Harimaya A, Murata M, Osanai M, Chiba H, Himi T, Sawada N

The Journal of membrane biology ( 1-3 )  218   1 - 7  2007.08  [Refereed]

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