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349 results on '"Hattori, Shunji"'

4. Heart-derived collagen promotes maturation of engineered heart tissue

Author

Tani, Hidenori, Kobayashi, Eiji, Yagi, Shinomi, Tanaka, Keisuke, Kameda-Haga, Kotaro, Shibata, Shinsuke, Moritoki, Nobuko, Takatsuna, Kaworu, Moriwaki, Taijun, Sekine, Otoya, Umei, Tomohiko C, Morita, Yuika, Soma, Yusuke, Kishino, Yoshikazu, Kanazawa, Hideaki, Fujita, Jun, Hattori, Shunji, Fukuda, Keiichi, and Tohyama, Shugo

Published
2023
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16. Gelatin but not type I collagen promotes bacteria phagocytosis in PMA-treated U937 human lymphoma cells.

Author

Meiling, Li, Yiran, Chen, Xiaoli, Sun, Kaihui, Chen, Toshihiko, Hayashi, Kikuji, Itoh, Kazunori, Mizuno, Hattori, Shunji, Fujisaki, Hitomi, Liu, Weiwei, and Ikejima, Takashi

Subjects
PHAGOCYTOSIS, EXTRACELLULAR matrix, GRAM-negative bacteria, BACTERIA, LYMPHOMAS, COLLAGEN, HEART beat, GELATIN
Abstract

Besides comprising scaffolding, extracellular matrix components modulate many biological processes including inflammation and cell differentiation. We previously found precoating cell plates with extracellular matrix collagen I, or its denatured product gelatin, causes aggregation of macrophage-like human lymphoma U937 cells, which are induced to differentiation by phorbol myristate treatment. In the present study, we investigated the influence of gelatin or collagen I precoating on the bacteria phagocytosis in PMA-stimulated U937 cells. Colony forming units of phagocytosed bacteria, Giemsa-staining of cells with phagocytosed bacteria, confocal microscopic and flow cytometric analysis of cells with phagocytosed FITC-labeled bacteria and non-bioactive latex beats were conducted. Gelatin precoating enhances the phagocytosis of both Gram-negative and positive bacteria, as shown by the increased colony forming units of bacteria phagocytosed by cells, and increased intracellular bacteria observed after Giemsa-staining. But collagen I has no marked influence. Confocal microscopy reveals that both live and dead FITC-bacteria were phagocytosed more in the cells with gelatin-coating but not collagen-coating. Of note, both gelatin and collagen I coating had no influence on the phagocytosis of non-bioactive latex beads. Since gelatin-coating increases autophagy but collagen I has no such impact, we are curious about the role of autophagy. Inhibiting autophagy reduced the phagocytosis of bacteria, in cells with gelatin-coating, while stimulating autophagy enhanced phagocytosis. This study finds the bacteria-phagocytosis stimulatory effect of gelatin in PMA-treated U937 cells and reveals the positive regulatory role of autophagy, predicting the potential use of gelatin products in anti-bacterial therapy. [ABSTRACT FROM AUTHOR]

Published
2024
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26. Insights into the catalytic mechanism of Grimontia hollisae collagenase through structural and mutational analyses.

Author

Ueshima, Saori, Yasumoto, Mizuki, Kitagawa, Yuto, Akazawa, Kaho, Takita, Teisuke, Tanaka, Keisuke, Hattori, Shunji, Mizutani, Kimihiko, Mikami, Bunzo, and Yasukawa, Kiyoshi

Subjects
COLLAGENASES, SITE-specific mutagenesis, TYROSINE, ACID catalysts, ZINC ions, CRYSTAL structure
Abstract

Grimontia hollisae collagenase (Ghcol) exhibits high collagen‐degrading activity. To explore its catalytic mechanism, its substrate (Gly‐Pro‐Hyp‐Gly‐Pro‐Hyp, GPOGPO)‐complexed crystal structure was determined at 2.0 Å resolution. A water molecule was observed near the active‐site zinc ion. Since this water was not observed in the product (GPO)‐complexed Ghcol, it was hypothesized that the GPOGPO‐complexed Ghcol structure reflects a Michaelis complex, providing a structural basis for understanding the catalytic mechanism. Analyses of the active‐site geometry and site‐directed mutagenesis of the active‐site tyrosine residues revealed that Glu493 and Tyr564 were essential for catalysis, suggesting that Glu493 functions as an acid and base catalyst while Tyr564 stabilizes the tetrahedral complex in the transition state. These results shed light on the catalytic mechanism of bacterial collagenase. [ABSTRACT FROM AUTHOR]

Published
2023
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31. Phorbol ester (PMA)-treated U937 cells cultured on type I collagen-coated dish express a lower production of pro-inflammatory cytokines through lowered ROS levels in parallel with cell aggregate formation

Author

Zhao, Ye-Li, Liu, Wei-Wei, Liu, Wei, Lu, Zhuo-Yu, Xuan, Di-Hong, Zhang, Xuan, Liu, Xiao-Ling, Hayashi, Toshihiko, Yamato, Masayuki, Ogura, Takaaki, Fujisaki, Hitomi, Hattori, Shunji, Tashiro, Shin-ichi, Onodera, Satoshi, and Ikejima, Takashi

Published
2018
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37. IGF-1R/YAP signaling pathway is involved in collagen V-induced insulin biosynthesis and secretion in rat islet INS-1 cells.

Author

Zhu, Yingying, Chen, Shuaigao, Liu, Weiwei, Xu, Fanxing, Lu, Jingyu, Hayashi, Toshihiko, Mizuno, Kazunori, Hattori, Shunji, Fujisaki, Hitomi, and Ikejima, Takashi

Subjects
HIPPO signaling pathway, BIOSYNTHESIS, INSULIN-like growth factor receptors, SOMATOMEDIN C, ISLANDS of Langerhans, INSULIN, INSULIN receptors, WNT signal transduction
Abstract

Type V collagen (collagen V) is one of the important components of extracellular matrix (ECM) in pancreas. We previously reported that pre-coating collagen V on the culture dishes enhanced insulin production in INS-1 rat pancreatic β cells. In this study, we investigate the underlying mechanism. Insulin biosynthesis and secretion are both increased in INS-1 cells cultured on collagen V-coated dishes, accompanied by the reduced nuclear translocation of Yes-associated protein (YAP), a transcriptional co-activator. YAP, the downstream effector of Hippo signaling pathway, plays an important role in the development and function of pancreas. Inhibition of YAP activation by verteporfin further up-regulates insulin biosynthesis and secretion. Silencing large tumor suppressor (LATS), a core component of Hippo pathway which inhibits activity of YAP by phosphorylation, by siRNA transfection inhibits both insulin biosynthesis and secretion. In the present study, the protein level of insulin-like growth factor 1 receptor (IGF-1 R), detected as the upstream molecule of YAP, is reduced in the INS-1 cells cultured on the dishes coated with collagen V. The silencing of IGF-1 R by siRNA transfection further enhances insulin biosynthesis and secretion. IGF-1 treatment reduces collagen V–induced up-regulation of insulin biosynthesis and secretion, accompanying the increased nuclear YAP. Inhibition of IGF-1 R/YAP signal pathway is involved in collagen V–induced insulin biosynthesis and secretion in INS-1 cells. [ABSTRACT FROM AUTHOR]

Published
2022
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44. Collagens I and V differently regulate the proliferation and adhesion of rat islet INS-1 cells through the integrin β1/E-cadherin/β-catenin pathway.

Author

Zhu, Yingying, Chen, Shuaigao, Liu, Weiwei, Zhang, Luxin, Xu, Fanxing, Hayashi, Toshihiko, Mizuno, Kazunori, Hattori, Shunji, Fujisaki, Hitomi, and Ikejima, Takashi

Subjects
CATENINS, ISLANDS of Langerhans, INTEGRINS, COLLAGEN, TRANSCRIPTION factors
Abstract

Extracellular matrix (ECM) plays an important role in tissue repair, cell proliferation, and differentiation. Our previous study showed that collagen I and collagen V differently regulate the proliferation of rat pancreatic β cells (INS-1 cells) through opposite influences on the nuclear translocation of β-catenin. In this study, we investigated the β-catenin pathway in INS-1 cells on dishes coated with collagen I or V. We found that nuclear translocation of the transcription factor Yes-associated protein (YAP) was enhanced by collagen I and suppressed by collagen V, but had no effect on INS-1 cell proliferation. Morphologically, INS-1 cells on collagen V-coated dishes showed stronger cell-to-cell adhesion, while the cells on collagen I-coated dishes showed weaker cell-to-cell adhesion in comparison with the cells on non-coated dishes. E-cadherin played an inhibitory role in the proliferation of INS-1 cells cultured on collagen I or collagen V coated dishes via regulation of the nuclear translocation of β-catenin. Integrin β1 was enhanced with collagen I, while it was repressed with collagen V. The integrin β1 pathway positively regulated the cell proliferation. Inhibition of integrin β1 pathway restored the protein level of E-cadherin and inhibited the nuclear translocation of β-catenin in the cells on collagen I-coated dishes, but no effect was observed in the cells on collagen V-coated dishes. In conclusion, collagen I enhances the proliferation of INS-1 cells via the integrin β1 and E-cadherin/β-catenin signaling pathway. In INS-1 cells on collagen V-coated dishes, both integrin β1 and E-cadherin/β-catenin signal pathways are involved in the inhibition of proliferation. [ABSTRACT FROM AUTHOR]

Published
2021
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45. Preservation of collagen in the soft tissues of frozen mammoths.

Author

Hattori, Shunji, Kiriyama-Tanaka, Tomomi, Kusubata, Masashi, Taga, Yuki, Ebihara, Testuya, Kumazawa, Yuki, Imai, Katsuyuki, Miura, Mitsutaka, Mezaki, Yoshihiro, Tikhonov, Alexei, and Senoo, Haruki

Subjects
*LIQUID chromatography-mass spectrometry, *MAMMOTHS, *AMINO acid analysis, *TRANSMISSION electron microscopy, *LIVER analysis
Abstract

We investigated the characteristics of extracellular matrix (ECM) in the soft tissue of two frozen baby woolly mammoths (Mammuthus primigenius) that died and were buried in Siberian permafrost approximately 40,000 years ago. Morphological and biochemical analyses of mammoth lung and liver demonstrated that those soft tissues were preserved at the gross anatomical and histological levels. The ultrastructure of ECM components, namely a fibrillar structure with a collagen-characteristic pattern of cross-striation, was clearly visible with transmission and scanning electron microscopy. Type I and type IV collagens were detected by immunohistochemical observation. Quantitative amino acid analysis of liver and lung tissues of the baby mammoths indicated that collagenous protein is selectively preserved in these tissues as a main protein. Type I and type III collagens were detected as major components by means of liquid chromatography–mass spectrometry analysis after digestion with trypsin. These results indicate that the triple helical collagen molecule, which is resistant to proteinase digestion, has been preserved in the soft tissues of these frozen mammoths for 40,000 years. [ABSTRACT FROM AUTHOR]

Published
2021
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