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  1. Article: GLP-1 reduces the migration of hepatocellular carcinoma cells via suppression of the stress-activated protein kinase/c-Jun N-terminal kinase pathway

    Yamada, Noriko / Matsushima-Nishiwaki, Rie / Kobayashi, Kaido / Tachi, Junko / Kozawa, Osamu

    Archives of biochemistry and biophysics. 2021 May 30, v. 703

    2021  

    Abstract: Incretins, glucagon-like peptide-1 (GLP-1) and glucose-dependent insulinotropic polypeptide (GIP), are hormones secreted from small intestine accompanied with oral intake. We previously showed that transforming growth factor (TGF)-α stimulates the ... ...

    Abstract Incretins, glucagon-like peptide-1 (GLP-1) and glucose-dependent insulinotropic polypeptide (GIP), are hormones secreted from small intestine accompanied with oral intake. We previously showed that transforming growth factor (TGF)-α stimulates the migration of hepatocellular carcinoma (HCC) cells via mitogen-activated protein (MAP) kinases, AKT and Rho-kinase. However, it remains to be elucidated whether incretins affect HCC cell functions. In the present study, therefore, we investigated whether incretins affect the migration of HCC cells using human HCC-derived HuH7 cells. GLP-1, but not GIP, reduced both TGF-α- and hepatocyte growth factor (HGF)-induced cell migration. IBMX, an inhibitor of cyclic nucleotide phosphodiesterase, enhanced the suppressive effect of GLP-1. GLP-1 attenuated the phosphorylation of stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK) by TGF-α and HGF. Our results strongly suggest that GLP-1 suppresses TGF-α- and HGF-induced migration of HCC cells through inhibiting the SAPK/JNK signaling pathway, and that the inhibition by GLP-1 is due to cAMP production.
    Keywords biophysics ; cell movement ; gastric inhibitory polypeptide ; glucagon-like peptide 1 ; hepatocyte growth factor ; hepatoma ; humans ; phosphorylation ; small intestine
    Language English
    Dates of publication 2021-0530
    Publishing place Elsevier Inc.
    Document type Article
    Note NAL-AP-2-clean
    ZDB-ID 523-x
    ISSN 1096-0384 ; 0003-9861
    ISSN (online) 1096-0384
    ISSN 0003-9861
    DOI 10.1016/j.abb.2021.108851
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Bonn / Germany

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  2. Article ; Online: GLP-1 reduces the migration of hepatocellular carcinoma cells via suppression of the stress-activated protein kinase/c-Jun N-terminal kinase pathway.

    Yamada, Noriko / Matsushima-Nishiwaki, Rie / Kobayashi, Kaido / Tachi, Junko / Kozawa, Osamu

    Archives of biochemistry and biophysics

    2021  Volume 703, Page(s) 108851

    Abstract: Incretins, glucagon-like peptide-1 (GLP-1) and glucose-dependent insulinotropic polypeptide (GIP), are hormones secreted from small intestine accompanied with oral intake. We previously showed that transforming growth factor (TGF)-α stimulates the ... ...

    Abstract Incretins, glucagon-like peptide-1 (GLP-1) and glucose-dependent insulinotropic polypeptide (GIP), are hormones secreted from small intestine accompanied with oral intake. We previously showed that transforming growth factor (TGF)-α stimulates the migration of hepatocellular carcinoma (HCC) cells via mitogen-activated protein (MAP) kinases, AKT and Rho-kinase. However, it remains to be elucidated whether incretins affect HCC cell functions. In the present study, therefore, we investigated whether incretins affect the migration of HCC cells using human HCC-derived HuH7 cells. GLP-1, but not GIP, reduced both TGF-α- and hepatocyte growth factor (HGF)-induced cell migration. IBMX, an inhibitor of cyclic nucleotide phosphodiesterase, enhanced the suppressive effect of GLP-1. GLP-1 attenuated the phosphorylation of stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK) by TGF-α and HGF. Our results strongly suggest that GLP-1 suppresses TGF-α- and HGF-induced migration of HCC cells through inhibiting the SAPK/JNK signaling pathway, and that the inhibition by GLP-1 is due to cAMP production.
    MeSH term(s) Carcinoma, Hepatocellular/pathology ; Cell Line, Tumor ; Cell Movement/drug effects ; Cyclic AMP/biosynthesis ; Glucagon-Like Peptide 1/pharmacology ; Hepatocyte Growth Factor/pharmacology ; Humans ; JNK Mitogen-Activated Protein Kinases/metabolism ; Liver Neoplasms/pathology ; Mitogen-Activated Protein Kinases/metabolism ; Phosphorylation/drug effects ; Transforming Growth Factor alpha/pharmacology
    Chemical Substances Transforming Growth Factor alpha ; Hepatocyte Growth Factor (67256-21-7) ; Glucagon-Like Peptide 1 (89750-14-1) ; Cyclic AMP (E0399OZS9N) ; JNK Mitogen-Activated Protein Kinases (EC 2.7.11.24) ; Mitogen-Activated Protein Kinases (EC 2.7.11.24)
    Language English
    Publishing date 2021-03-23
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 523-x
    ISSN 1096-0384 ; 0003-9861
    ISSN (online) 1096-0384
    ISSN 0003-9861
    DOI 10.1016/j.abb.2021.108851
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.237: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

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  3. Article ; Online: Cellular Functions of Small Heat Shock Proteins (HSPB) in Hepatocellular Carcinoma.

    Yamada, Noriko / Matsushima-Nishiwaki, Rie / Kobayashi, Kaido / Takahata, Shota / Toyoda, Hidenori / Kumada, Takashi / Kozawa, Osamu

    Current molecular medicine

    2021  Volume 21, Issue 10, Page(s) 872–887

    Abstract: Heat shock proteins (HSPs) play an essential role as molecular chaperones in proteostasis. Small HSPs are a group of low-molecular-weight HSPs in the range of 12- 43 kDa and are classified as HSPB. Within the ten members of the family, HSPB1(HSP27), ... ...

    Abstract Heat shock proteins (HSPs) play an essential role as molecular chaperones in proteostasis. Small HSPs are a group of low-molecular-weight HSPs in the range of 12- 43 kDa and are classified as HSPB. Within the ten members of the family, HSPB1(HSP27), HSPB5 (αB-crystallin), HSPB6 (HSP20), and HSPB8 (HSP22) ubiquitously exist in various tissues, including liver tissue. These small HSPs undergo phosphorylation as a post-translational modification, and their functions are modulated. Hepatocellular carcinoma (HCC) is one of the most frequent cancers and the fourth leading cause of cancer-related death worldwide. HSPs play a cytoprotective role as molecular chaperones. Thus, HSPB has been generally considered to protect HCC cells and help the progression of HCC. On the other hand, recent studies from our laboratories have demonstrated suppressive roles of phospho-HSPB1, HSPB6, and HSPB8 in the progression of HCC. These findings may provide a basis for a novel defense system by HSPB against HCC progression. This review focuses on the cellular functions of HSPB in HCC and summarizes the current research.
    MeSH term(s) Carcinoma, Hepatocellular/genetics ; Carcinoma, Hepatocellular/metabolism ; Heat-Shock Proteins, Small/genetics ; Heat-Shock Proteins, Small/metabolism ; Humans ; Liver Neoplasms/genetics ; Liver Neoplasms/metabolism ; Neoplasm Proteins/genetics ; Neoplasm Proteins/metabolism
    Chemical Substances Heat-Shock Proteins, Small ; Neoplasm Proteins
    Language English
    Publishing date 2021-02-10
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 2064873-X
    ISSN 1875-5666 ; 1566-5240
    ISSN (online) 1875-5666
    ISSN 1566-5240
    DOI 10.2174/1573405617666210204211252
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 5580: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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  4. Article: Heat shock protein 70 positively regulates transforming growth factor-α-induced hepatocellular carcinoma cell migration via the AKT signaling pathway

    Kobayashi, Kaido / Matsushima-Nishiwaki, Rie / Yamada, Noriko / Migita, Saori / Hioki, Tomoyuki / Mizutani, Daisuke / Kozawa, Osamu

    Heliyon. 2020 Sept., v. 6, no. 9

    2020  

    Abstract: Heat shock proteins (HSPs) are induced in response to extracellular stress and manage the quality of proteins as molecular chaperones. HSP70, a highly conserved HSP, has been reported to correlate with the proliferation and migration of human cancer ... ...

    Abstract Heat shock proteins (HSPs) are induced in response to extracellular stress and manage the quality of proteins as molecular chaperones. HSP70, a highly conserved HSP, has been reported to correlate with the proliferation and migration of human cancer cells, such as oral, prostate, lung and liver cancer. Regarding hepatocellular carcinoma (HCC), the HSP70 levels in the tumor tissues from patients are significantly higher than those in the normal liver tissues. HSP70 reportedly upregulates the migration and invasion of HCC. The AKT, p38 mitogen-activated protein kinase (MAPK), c-jun N-terminal kinase (JNK) and Rho-kinase signaling pathways regulate the transforming growth factor (TGF)-α-induced migration of human HCC-derived HuH7 cells. However, the exact mechanism underlying the role of HSP70 in growth factor-induced HCC migration remains unclear. Therefore, in the present study, the mechanism underlying the involvement of HSP70 in TGF-α-induced HCC cell migration was investigated. Treatment with the HSP70 inhibitors VER155008 and YM-08 and the downregulation of HSP70 protein were confirmed to significantly suppress the TGF-α-induced cell migration of HuH7 cells. Both VER155008 and YM-08 reduced the TGF-α-induced phosphorylation of AKT without affecting the phosphorylation of p38 MAPK, JNK or Rho-kinase. These results strongly suggest that HSP70 positively regulates the TGF-α-induced migration of HCC cells via the AKT signaling pathway.
    Keywords cell movement ; heat stress ; heat-shock protein 70 ; hepatoma ; humans ; liver ; lungs ; mitogen-activated protein kinase ; neoplasm cells ; phosphorylation
    Language English
    Dates of publication 2020-09
    Publishing place Elsevier Ltd
    Document type Article
    Note NAL-AP-2-clean
    ZDB-ID 2835763-2
    ISSN 2405-8440
    ISSN 2405-8440
    DOI 10.1016/j.heliyon.2020.e05002
    Database NAL-Catalogue (AGRICOLA)

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  5. Article: Heat shock protein 70 positively regulates transforming growth factor-α-induced hepatocellular carcinoma cell migration via the AKT signaling pathway.

    Kobayashi, Kaido / Matsushima-Nishiwaki, Rie / Yamada, Noriko / Migita, Saori / Hioki, Tomoyuki / Mizutani, Daisuke / Kozawa, Osamu

    Heliyon

    2020  Volume 6, Issue 9, Page(s) e05002

    Abstract: Heat shock proteins (HSPs) are induced in response to extracellular stress and manage the quality of proteins as molecular chaperones. HSP70, a highly conserved HSP, has been reported to correlate with the proliferation and migration of human cancer ... ...

    Abstract Heat shock proteins (HSPs) are induced in response to extracellular stress and manage the quality of proteins as molecular chaperones. HSP70, a highly conserved HSP, has been reported to correlate with the proliferation and migration of human cancer cells, such as oral, prostate, lung and liver cancer. Regarding hepatocellular carcinoma (HCC), the HSP70 levels in the tumor tissues from patients are significantly higher than those in the normal liver tissues. HSP70 reportedly upregulates the migration and invasion of HCC. The AKT, p38 mitogen-activated protein kinase (MAPK), c-
    Language English
    Publishing date 2020-09-23
    Publishing country England
    Document type Journal Article
    ZDB-ID 2835763-2
    ISSN 2405-8440
    ISSN 2405-8440
    DOI 10.1016/j.heliyon.2020.e05002
    Database MEDical Literature Analysis and Retrieval System OnLINE

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