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2. Expression of Synphilin-1 in Human Vascular Endothelial Cells

Author

Tamo, Wakako, Imaizumi, Tadaatsu, Yoshida, Hidemi, Mori, Fumiaki, Fukuda, Ikuo, Wakabashi, Koichi, Satoh, Kei, Departments of Vascular Biology, Hirosaki University School of Medicine, Departments of Molecular Biology, Institute of Brain Science, Hirosaki University School of Medicine, First Department of Surgery, Hirosaki University School of Medicine, 弘前大学医学部附属脳神経血管病態研究施設脳血管病態部門, 弘前大学医学部附属脳神経血管病態研究施設分子病態部門, 弘前大学医学部外科学第一講座, 田茂, 和歌子, 今泉, 忠淳, 吉田, 秀見, 森, 文秋, 福田, 幾夫, 若林, 孝一, 佐藤, 敬, Tamo, Wakako, Imaizumi, Tadaatsu, Yoshida, Hidemi, Mori, Fumiaki, Fukuda, Ikuo, Wakabashi, Koichi, Satoh, Kei, Departments of Vascular Biology, Hirosaki University School of Medicine, Departments of Molecular Biology, Institute of Brain Science, Hirosaki University School of Medicine, First Department of Surgery, Hirosaki University School of Medicine, 弘前大学医学部附属脳神経血管病態研究施設脳血管病態部門, 弘前大学医学部附属脳神経血管病態研究施設分子病態部門, 弘前大学医学部外科学第一講座, 田茂, 和歌子, 今泉, 忠淳, 吉田, 秀見, 森, 文秋, 福田, 幾夫, 若林, 孝一, and 佐藤, 敬

Abstract

Synphilin-1 was originally identified as a binding protein of α-synuclein, a major component of Lewy bodies in Parkinson's disease. Synphilin-1 localizes mainly in the synaptic terminals and is also found in Lewy bodies. We previously demonstrated the expression of α-synuclein in vascular endothelial cells. The present study was undertaken to address the expression of synphilin-1 in endothelial cells. Synphilin-1 immunoreactivity was detected in the vessel walls, particularly in endothelial cells, in postmortem human brain. Expressions of mRNA and protein for synphilin-1 in human umbilical vein endothelial cells in culture were demonstrated by reverse-transcription polymerase-chain reaction and western blotting. Synphilin-1 is constitutively expressed in endothelial cells and may have some physiological function in the vascular wall.

Published
2007

3. Effect of Sivelestat Sodium Hydrate (Elaspol) for Lung Injury and Acute Respiratory Distress Syndrome after Cardiovascular Surgery

Author

Suzuki, Yasuyuki, Wakayama, Fuminori, Kondo, Norihiko, Tamo, Wakako, Taniguchi, Satoshi, Daitoku, Kazuyuki, Minakawa, Masahito, Fukui, Kozo, Fukuda, Ikuo, First Department Surgery, Hirosaki University School of Medicine, 弘前大学医学部第一外科, 鈴木, 保之, 若山, 文規, 近藤, 慎浩, 田茂, 和歌子, 谷口, 哲, 大徳, 和之, 皆川, 正仁, 福井, 康三, 福田, 幾夫, Suzuki, Yasuyuki, Wakayama, Fuminori, Kondo, Norihiko, Tamo, Wakako, Taniguchi, Satoshi, Daitoku, Kazuyuki, Minakawa, Masahito, Fukui, Kozo, Fukuda, Ikuo, First Department Surgery, Hirosaki University School of Medicine, 弘前大学医学部第一外科, 鈴木, 保之, 若山, 文規, 近藤, 慎浩, 田茂, 和歌子, 谷口, 哲, 大徳, 和之, 皆川, 正仁, 福井, 康三, and 福田, 幾夫

Abstract

Background: Lung injury and acute respiratory distress syndrome after cardiopulmonary bypass were described as severe postoperative complication. Although the incidence of ARDS after cardiopulmonary bypass (CPB) is about 1%, the mortality of ARDS is extremely high. It has been well recognized that CPB is associated with systemic inflammation. This pulmonary dysfunction after CPB is one of those inflammatory responses, activated neutrophil and neurophil elastase play an important role in this injury. Method: ELASPOL (Sivelestat sodium hydrate; Ono Pharmaceutical Co., in Japan) is neutrophil elastase inhibitor that was introduced in 2002 for acute lung injury with SIRS. We hypothesized that this drug would reduce lung dysfunction after CPB especially in the patient who had total arch replacement or cardiac surgery with severe preoperative condition. We compared control group and group treated with ELASPOL[○!R] group retrospectively. The control group were cases of total arch replacement with severe lung dysfunction before 2002, therapeutic group were cases of total arch replacement with ELASPOL that included a case without operation. Arterial PO_2/FiO_2 as indication of lung injury (The P/F ratio is an index of acute lung injury and ARDS, it is defined as acute lung injury when the P/F ratio is under 300, and the P/F ratio of ARDS is under 200.), platelet count, WBC count, CRP, duration of intubation and ICU stay were evaluated. Results: As compared with the control group that had almost same operative procedure with ELASPOL, P/F ratio (arterial PO_2/FiO_2) was increased over 200 at four postoperative days and well maintained after all in therapeutic group. On the other hand it dropped to below 150, and it did not recovered to 200 until 10 days after the operation in the control group (p<0.05). Platelet count in ELASPOL group was relatively higher than control, but there is no significance of differences between groups. The other factors such as WBC count, CRP level

Published
2006

5. Interferon-γ stimulates the expression of galectin-9 in cultured human endothelial cells

Author

Imaizumi, Tadaatsu, primary, Kumagai, Mika, additional, Sasaki, Naoko, additional, Kurotaki, Hidekachi, additional, Mori, Fumiaki, additional, Seki, Masako, additional, Nishi, Nozomu, additional, Fujimoto, Koji, additional, Tanji, Kunikazu, additional, Shibata, Takeo, additional, Tamo, Wakako, additional, Matsumiya, Tomoh, additional, Yoshida, Hidemi, additional, Cui, Xue-Fan, additional, Takanashi, Shingo, additional, Hanada, Katsumi, additional, Okumura, Ken, additional, Yagihashi, Soroku, additional, Wakabayashi, Koichi, additional, Nakamura, Takanori, additional, Hirashima, Mitsuomi, additional, and Satoh, Kei, additional

Published
2002
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7. Effect of MG132, a proteasome inhibitor, on the expression of growth related oncogene protein-alpha in human umbilical vein endothelial cells.

Author

Shibata T, Imaizumi T, Matsumiya T, Tamo W, Hatakeyama M, Yoshida H, Munakata H, Fukuda I, and Satoh K

Subjects
Acetylcysteine pharmacology, Anthracenes pharmacology, Cells, Cultured, Chemokine CXCL1, Chemokines, CXC genetics, Endothelium, Vascular cytology, Enzyme Inhibitors pharmacology, Flavonoids pharmacology, Gene Expression Regulation drug effects, Humans, I-kappa B Proteins drug effects, I-kappa B Proteins metabolism, Imidazoles pharmacology, Intercellular Signaling Peptides and Proteins genetics, JNK Mitogen-Activated Protein Kinases, MAP Kinase Kinase Kinases antagonists & inhibitors, MAP Kinase Kinase Kinases drug effects, MAP Kinase Kinase Kinases metabolism, Mitogen-Activated Protein Kinases antagonists & inhibitors, Mitogen-Activated Protein Kinases drug effects, Mitogen-Activated Protein Kinases metabolism, NF-kappa B drug effects, NF-kappa B metabolism, Phosphorylation, Pyridines pharmacology, Umbilical Veins drug effects, p38 Mitogen-Activated Protein Kinases, Acetylcysteine analogs & derivatives, Chemokines, CXC metabolism, Cysteine Proteinase Inhibitors pharmacology, Endothelium, Vascular drug effects, Intercellular Signaling Peptides and Proteins metabolism, Leupeptins pharmacology, MAP Kinase Kinase Kinase 1, Umbilical Veins cytology
Abstract

Growth related oncogene protein-alpha (GRO-alpha) is a member of C-X-C chemokine and plays an important role in inflammatory responses. Expression of GRO gene family is regulated by a number of factors at both transcriptional and posttranscriptional levels. In the present study, we have addressed the possible regulation of GRO-alpha expression by ubiquitin-proteasome system. Cultures of human umbilical vein endothelial cells were treated with a proteasome inhibitor, MG132, and the levels of GRO-alpha mRNA were analyzed by reverse transcription-polymerase chain reaction or northern blotting. Levels of GRO-alpha protein in the cell-conditioned medium were determined by enzyme-linked immunosorbent assay. MG132 alone increased the levels of GRO-alpha mRNA and protein; however, it did not affect the GRO-alpha mRNA induced by lipopolysaccharide (LPS) and inhibited the LPS-induced decrease in IkappaB levels. Other proteasome inhibitors, MG115 and lactacystin, also induced the expression of GRO-alpha mRNA. MG132 induced the phosphorylation of p38 MAPK, MEK and JNK. Pretreatment of the cells with SB203580, an inhibitor of p38 MAPK, suppressed the MG132-induced GRO-alpha expression, but pretreatment of the cells with U0126, PD98059 or SP600125, inhibitors of MEK1/2 or JNK, did not influence the effect of MG132. We conclude that MG132 upregulates GRO-alpha expression in vascular endothelial cells, at least in part, through the activation of p38 MAPK.

Published
2003
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8. Interferon-gamma stimulates the expression of galectin-9 in cultured human endothelial cells.

Author

Imaizumi T, Kumagai M, Sasaki N, Kurotaki H, Mori F, Seki M, Nishi N, Fujimoto K, Tanji K, Shibata T, Tamo W, Matsumiya T, Yoshida H, Cui XF, Takanashi S, Hanada K, Okumura K, Yagihashi S, Wakabayashi K, Nakamura T, Hirashima M, and Satoh K

Subjects
Autoimmune Diseases metabolism, Autoimmune Diseases pathology, Cell Adhesion drug effects, Cell Membrane metabolism, Cells, Cultured drug effects, Cells, Cultured metabolism, Chemokine CCL11, Chemokines, CC biosynthesis, Chemokines, CC genetics, Cytosol metabolism, Endothelium, Vascular metabolism, Eosinophils cytology, Humans, Hypereosinophilic Syndrome pathology, Interleukin-4 pharmacology, Lactose pharmacology, Lectins genetics, Nasal Polyps chemistry, Recombinant Proteins, Rhinitis, Allergic, Seasonal metabolism, Rhinitis, Allergic, Seasonal pathology, Sjogren's Syndrome metabolism, Sjogren's Syndrome pathology, Tumor Cells, Cultured cytology, Tumor Cells, Cultured drug effects, Umbilical Veins, Endothelium, Vascular drug effects, Galectins, Gene Expression Regulation drug effects, Interferon-gamma pharmacology, Lectins biosynthesis
Abstract

Galectin-9 is a member of the galectin family and has been identified as an eosinophil chemoattractant produced by activated T lymphocytes. Vascular endothelial cells play an important role in the initial step of eosinophil recruitment and activation in immune and inflammatory responses. We have addressed the stimulation of galectin-9 expression in endothelial cells. Galectin-9 was detected in membrane and cytosolic fractions of human umbilical vein endothelial cells stimulated with interferon-gamma (IFN-gamma). IFN-gamma also enhanced the adhesion of human eosinophilic leukemia-1 cells to endothelial monolayers, and it was inhibited by the presence of lactose. Interleukin-4, which induces eotaxin expression, did not affect the expression of galectin-9. The in situ endothelium from patients with inflammatory diseases was found to express galectin-9. IFN-gamma-induced production of galectin-9 by endothelial cells may play an important role in immune responses by regulating interactions between the vascular wall and eosinophils.

Published
2002

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