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Article ; Online: Inhibitory Effects of Eicosapentaenoic Acid on Vascular Endothelial Growth Factor-Induced Monocyte Chemoattractant Protein-1, Interleukin-6, and Interleukin-8 in Human Vascular Endothelial Cells.

Takenoshita, Yoko / Tokito, Akinori / Jougasaki, Michihisa

International journal of molecular sciences

2024 Volume 25, Issue 5

Abstract: Vascular endothelial growth factor (VEGF) induces monocyte chemoattractant protein-1 (MCP-1) and plays an important role in vascular inflammation and atherosclerosis. We investigated the mechanisms of VEGF-induced MCP-1 expression and the effects of ... ...

Abstract	Vascular endothelial growth factor (VEGF) induces monocyte chemoattractant protein-1 (MCP-1) and plays an important role in vascular inflammation and atherosclerosis. We investigated the mechanisms of VEGF-induced MCP-1 expression and the effects of eicosapentaenoic acid (EPA) in human umbilical vein endothelial cells (HUVECs). Real-time reverse transcription polymerase chain reaction (RT-PCR) and enzyme-linked immunosorbent assay (ELISA) demonstrated that VEGF enhanced MCP-1 gene expression and protein secretion in HUVECs. Western immunoblot analysis revealed that VEGF induced the phosphorylation of p38 mitogen-activated protein kinase (MAPK) and inhibitor of nuclear factor (NF)-κB (IκB). Treatment with pharmacological inhibitors of p38 MAPK (SB203580) or NF-κB (BAY11-7085) significantly suppressed VEGF-induced MCP-1 in HUVECs. EPA inhibited VEGF-induced MCP-1 mRNA, protein secretion, phosphorylation of p38 MAPK, and the translocation of phospho-p65 to the nucleus. Additionally, VEGF also stimulated gene expressions of
MeSH term(s)	Humans ; Chemokine CCL2/metabolism ; Interleukin-6/metabolism ; Interleukin-8/metabolism ; NF-kappa B/metabolism ; Vascular Endothelial Growth Factor A/metabolism ; Eicosapentaenoic Acid/pharmacology ; Human Umbilical Vein Endothelial Cells/metabolism ; p38 Mitogen-Activated Protein Kinases/metabolism
Chemical Substances	Chemokine CCL2 ; Interleukin-6 ; Interleukin-8 ; NF-kappa B ; Vascular Endothelial Growth Factor A ; Eicosapentaenoic Acid (AAN7QOV9EA) ; p38 Mitogen-Activated Protein Kinases (EC 2.7.11.24)
Language	English
Publishing date	2024-02-27
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms25052749
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Article ; Online: Left atrial size by planimetry is superior to M-mode diameter: biochemical calibration by atrial and brain natriuretic peptide.

Buchner, Stefan / Muscholl, Michael / Debl, Kurt / Hense, Hans-Werner / Döring, Angela / Stritzke, Jan / Schunkert, Heribert / Jougasaki, Michihisa / Burnett, John C / Riegger, Günter A J / Luchner, Andreas

Journal of the American Society of Echocardiography : official publication of the American Society of Echocardiography

2008 Volume 21, Issue 4, Page(s) 380–385

Abstract: Background: Left atrial (LA) size is routinely assessed by M-mode on echocardiography. Recently ... two-chamber (2C) and four-chamber (4C) views in addition to M-mode echocardiography. ANP and BNP ... present with all measures on LA size. The univariate correlation was lowest with M-mode diameter (r = 0.11 ...

Abstract	Background: Left atrial (LA) size is routinely assessed by M-mode on echocardiography. Recently, a superiority of apical measures of LA size has been suggested, but no biochemical calibration has been attempted yet. The aim of the current study was to compare echocardiographic parameters of LA size through biochemical calibration with the natriuretic peptides atrial natriuretic peptide (ANP) and brain natriuretic peptide (BNP). Methods: A total of 610 middle-aged (50-67 years) subjects from a population-based sample (MONICA Augsburg, Germany) were characterized with respect to LA area and volume from the apical two-chamber (2C) and four-chamber (4C) views in addition to M-mode echocardiography. ANP and BNP concentrations were determined by radioimmunoassay. Results: A significant correlation to ANP and BNP was present with all measures on LA size. The univariate correlation was lowest with M-mode diameter (r = 0.11 with ANP; r = 0.09 with BNP, both P < .03), whereas 2C volume displayed the closest correlation (r = 0.20 with ANP and r = 0.28 with BNP, both P < .001) and even slightly exceeded 2C area, 4C volume, and 4C area. 2C volume further displaced LV systolic function, mass index, and heart rate as statistically significant predictors of ANP (P < .001) and BNP (P < .001) on adjusted regression analysis, whereas M-mode diameter was displaced as a significant predictor of ANP and BNP (P = not significant). Conclusions: The current population-based echocardiographic study allows new insight into the value of different measures of LA size. The closer association between natriuretic peptide concentrations and parameters derived from planimetry and volumetry suggests a superiority of these parameters LA diameter. LA volumetry should be included in routine echocardiography for optimized assessment of LA size.
MeSH term(s)	Aged ; Atrial Natriuretic Factor/blood ; Echocardiography, Three-Dimensional/methods ; Female ; Heart Atria/diagnostic imaging ; Heart Atria/metabolism ; Humans ; Image Enhancement/methods ; Image Interpretation, Computer-Assisted/methods ; Male ; Middle Aged ; Natriuretic Peptide, Brain/blood ; Reproducibility of Results ; Sensitivity and Specificity ; Statistics as Topic ; Ventricular Dysfunction, Left/diagnostic imaging
Chemical Substances	Natriuretic Peptide, Brain (114471-18-0) ; Atrial Natriuretic Factor (85637-73-6)
Language	English
Publishing date	2008-04
Publishing country	United States
Document type	Comparative Study ; Evaluation Studies ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1035622-8
ISSN	1097-6795 ; 0894-7317
ISSN (online)	1097-6795
ISSN	0894-7317
DOI	10.1016/j.echo.2007.06.006
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Article ; Online: Autocrine Regulation of Interleukin-6 via the Activation of STAT3 and Akt in Cardiac Myxoma Cells.

Jougasaki, Michihisa / Takenoshita, Yoko / Umebashi, Katsuyuki / Yamamoto, Masayoshi / Sudou, Ku / Nakashima, Hitoshi / Sonoda, Masahiro / Kinjo, Tamahiro

International journal of molecular sciences

2024 Volume 25, Issue 4

Abstract: Plasma concentrations of a pleiotropic cytokine, interleukin (IL)-6, are increased in patients with cardiac myxoma. We investigated the regulation of IL-6 in cardiac myxoma. Immunohistochemical staining and reverse transcription-polymerase chain reaction ...

Abstract	Plasma concentrations of a pleiotropic cytokine, interleukin (IL)-6, are increased in patients with cardiac myxoma. We investigated the regulation of IL-6 in cardiac myxoma. Immunohistochemical staining and reverse transcription-polymerase chain reaction (RT-PCR) revealed that IL-6 and its receptors, IL-6 receptor (IL-6R) and gp130, co-existed in the myxoma cells. Myxoma cells were cultured, and an antibody array assay showed that a conditioned medium derived from the cultured myxoma cells contained increased amounts of IL-6. Signal transducer and activator of transcription (STAT) 3 and Akt were constitutively phosphorylated in the myxoma cells. An enzyme-linked immunosorbent assay (ELISA) showed that the myxoma cells spontaneously secreted IL-6 into the culture medium. Real-time PCR revealed that stimulation with IL-6 + soluble IL-6R (sIL6R) significantly increased IL-6 mRNA in the myxoma cells. Pharmacological inhibitors of STAT3 and Akt inhibited the IL-6 + sIL-6R-induced gene expression of IL-6 and the spontaneous secretion of IL-6. In addition, IL-6 + sIL-6R-induced translocation of phosphorylated STAT3 to the nucleus was also blocked by STAT3 inhibitors. This study has demonstrated that IL-6 increases its own production via STAT3 and Akt pathways in cardiac myxoma cells. Autocrine regulation of IL-6 may play an important role in the pathophysiology of patients with cardiac myxoma.
MeSH term(s)	Humans ; Cells, Cultured ; Interleukin-6/metabolism ; Myxoma/metabolism ; Proto-Oncogene Proteins c-akt/metabolism ; Receptors, Interleukin-6/metabolism ; Signal Transduction ; STAT3 Transcription Factor/metabolism
Chemical Substances	Interleukin-6 ; Proto-Oncogene Proteins c-akt (EC 2.7.11.1) ; Receptors, Interleukin-6 ; STAT3 protein, human ; STAT3 Transcription Factor
Language	English
Publishing date	2024-02-13
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms25042232
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Article ; Online: Inhibitory Effects of Simvastatin on IL-33-Induced MCP-1 via the Suppression of the JNK Pathway in Human Vascular Endothelial Cells.

Umebashi, Katsuyuki / Yamamoto, Masayoshi / Tokito, Akinori / Sudou, Ku / Takenoshita, Yoko / Jougasaki, Michihisa

International journal of molecular sciences

2023 Volume 24, Issue 16

Abstract: An alarmin, interleukin (IL)-33 is a danger signal that causes inflammation, inducing chemotactic proteins such as monocyte chemoattractant protein (MCP)-1 in various cells. As statins have pleiotropic actions including anti-inflammatory properties, we ... ...

Abstract	An alarmin, interleukin (IL)-33 is a danger signal that causes inflammation, inducing chemotactic proteins such as monocyte chemoattractant protein (MCP)-1 in various cells. As statins have pleiotropic actions including anti-inflammatory properties, we investigated the effects of simvastatin on IL-33-induced MCP-1 expression in human umbilical vein endothelial cells (HUVECs). HUVECs were stimulated with IL-33 in the presence or absence of simvastatin. Gene expression and protein secretion of MCP-1, phosphorylation of mitogen-activated protein kinase (MAPK), nuclear translocation of phosphorylated c-Jun, and human monocyte migration were investigated. Immunocytochemical staining and Western immunoblot analysis revealed that IL-33 augmented MCP-1 protein expression in HUVECs. Real-time reverse transcription-polymerase chain reaction (RT-PCR) and enzyme-linked immunosorbent assay (ELISA) showed that IL-33 significantly increased MCP-1 mRNA and protein secretion, which were suppressed by c-jun N-terminal kinase (JNK) inhibitor SP600125 and p38 MAPK inhibitor SB203580. Simvastatin inhibited IL-33-induced MCP-1 mRNA, protein secretion, phosphorylation of JNK and c-Jun. Additionally, the IL-33-induced nuclear translocation of phosphorylated c-Jun and THP-1 monocyte migration were also blocked by simvastatin. This study demonstrated that IL-33 induces MCP-1 expression via the JNK and p38 MAPK pathways in HUVECs, and that simvastatin inhibits MCP-1 production by selectively suppressing JNK. Simvastatin may inhibit the progression of IL-33-induced inflammation via suppressing JNK to prevent MCP-1 production.
MeSH term(s)	Humans ; Simvastatin/pharmacology ; MAP Kinase Signaling System ; Interleukin-33 ; Human Umbilical Vein Endothelial Cells ; Inflammation
Chemical Substances	Simvastatin (AGG2FN16EV) ; Interleukin-33
Language	English
Publishing date	2023-08-21
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms241613015
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Article ; Online: Respiratory epithelial adenomatoid hamartomas of the sinonasal tract: A histopathological analysis of 50 patients.

Goto, Masamichi / Nishimoto, Kengo / Jougasaki, Yasuyo / Matsuzaki, Tsutomu / Nomoto, Mitsuharu

Pathology international

2022 Volume 72, Issue 11, Page(s) 541–549

Abstract: Respiratory epithelial adenomatoid hamartoma (REAH) is a benign lesion of the nasal cavity and paranasal sinuses. Here, we report the clinicopathological characteristics of REAH identified in 2065 cases with nasal/paranasal polypoid lesions treated with ... ...

Abstract	Respiratory epithelial adenomatoid hamartoma (REAH) is a benign lesion of the nasal cavity and paranasal sinuses. Here, we report the clinicopathological characteristics of REAH identified in 2065 cases with nasal/paranasal polypoid lesions treated with endoscopic sinus surgery (ESS) at our hospital from 2008 to 2021. Cases including the olfactory area were reviewed and 50 patients of REAH were identified pathologically (50/2065, 2.4%). The average age was 58.9 years old and the male/female ratio was 45/5. Grossly, REAH showed a whitish surface and elastic firm consistency. The histopathological characteristics included proliferation of small to medium-sized glands composed of ciliated respiratory epithelium containing goblet cells; thickening of the basement membrane compared to that for inverted papilloma (9.6 ± 2.4 vs. 1.3 ± 1.6 µm, p < 0.001); and no intra-epithelial neutrophilic infiltration. Among the REAH cases, 81% were associated with sinonasal inflammatory polyps. Many olfactory cleft polyps were REAH (38/98, 39%). The rate of REAH found in ESS in the last 7 years was higher than that in the first 7 years (3.17% vs. 1.62%, p = 0.032). Our results in Japanese patients are similar to those found in other countries, including male predominance. REAH is relatively common and that 39% of polyps taken from olfactory clefts are REAH.
MeSH term(s)	Humans ; Male ; Female ; Middle Aged ; Paranasal Sinuses/pathology ; Paranasal Sinuses/surgery ; Hamartoma/pathology ; Endoscopy/methods ; Respiratory Mucosa/pathology ; Adenoma/pathology ; Diagnosis, Differential
Language	English
Publishing date	2022-09-14
Publishing country	Australia
Document type	Journal Article
ZDB-ID	1194850-4
ISSN	1440-1827 ; 1320-5463
ISSN (online)	1440-1827
ISSN	1320-5463
DOI	10.1111/pin.13271
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Article: Cardiotrophin-1 in cardiovascular regulation.

Jougasaki, Michihisa

Advances in clinical chemistry

2011 Volume 52, Page(s) 41–76

Abstract: Cardiotrophin (CT)-1 was discovered by coupling expression cloning with an embryonic stem cell-based model of cardiogenesis. Comparison of similarity in amino acid sequence and conformational structure indicates that CT-1 is a member of the interleukin ( ... ...

Abstract	Cardiotrophin (CT)-1 was discovered by coupling expression cloning with an embryonic stem cell-based model of cardiogenesis. Comparison of similarity in amino acid sequence and conformational structure indicates that CT-1 is a member of the interleukin (IL)-6 type cytokine family that shares the transmembrane signaling protein, glycoprotein (gp) 130 as a receptor. These cytokines mediate overlapping pleiotropic actions on a variety of cell types including cardiac myocytes, hepatocytes, megakaryocytes, osteoclasts, and neuronal cells. CT-lmediates its hypertrophic and cytoprotective properties through the Janus kinase/signal transducers and activators of transcription (JAK/STAT), mitogen-activated protein (MAP) kinase, phosphatidylinositol (PI) 3 kinase, and nuclear factor kappa B (NFkappaB) pathways. CT-1 gene and protein are distributed not only in the heart, but also in the pulmonary, renal, gastrointestinal, cerebral, and muscular tissues. CT-1 could also be synthesized and secreted from vascular endothelial cells and adipocytes. CT-1 has hypertrophic actions on the cardiac myocytes, skeletal muscle cells, and smooth muscle cells as well as cytoprotective actions on the cardiac myocytes, neuronal cells, and hepatocytes. CT-1 is circulating in the body, and its plasma concentration is increased in various cardiovascular and renal diseases such as hypertension, congestive heart failure, myocardial infarction, valvular heart disease, metabolic syndrome, and chronic kidney disease. Treatment with CT-1 is beneficial in experimental animal models of cardiovascular diseases. CT-1 specifically protects the cardiac myocytes from ischemic damage when CT-1 is given not only prior to the ischemia, but also given at the time of reoxygenation. Current evidence suggests that CT-1 plays an important role in the regulation of the cardiovascular system.
MeSH term(s)	Animals ; Cardiovascular Physiological Phenomena ; Cytokines/genetics ; Cytokines/metabolism ; Gene Expression Regulation ; Humans ; Myocytes, Cardiac/metabolism ; Signal Transduction
Chemical Substances	Cytokines ; cardiotrophin 1 (AJ7U77BR8I)
Language	English
Publishing date	2011-01-21
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	210505-6
ISSN	0065-2423
ISSN	0065-2423
DOI	10.1016/s0065-2423(10)52002-x
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Article ; Online: Matrix Metalloproteinases in Non-Neoplastic Disorders.

Tokito, Akinori / Jougasaki, Michihisa

International journal of molecular sciences

2016 Volume 17, Issue 7

Abstract: The matrix metalloproteinases (MMPs) are zinc-dependent endopeptidases belonging to the metzincin superfamily. There are at least 23 members of MMPs ever reported in human, and they and their substrates are widely expressed in many tissues. Recent ... ...

Abstract	The matrix metalloproteinases (MMPs) are zinc-dependent endopeptidases belonging to the metzincin superfamily. There are at least 23 members of MMPs ever reported in human, and they and their substrates are widely expressed in many tissues. Recent growing evidence has established that MMP not only can degrade a variety of components of extracellular matrix, but also can cleave and activate various non-matrix proteins, including cytokines, chemokines and growth factors, contributing to both physiological and pathological processes. In normal conditions, MMP expression and activity are tightly regulated via interactions between their activators and inhibitors. Imbalance among these factors, however, results in dysregulated MMP activity, which causes tissue destruction and functional alteration or local inflammation, leading to the development of diverse diseases, such as cardiovascular disease, arthritis, neurodegenerative disease, as well as cancer. This article focuses on the accumulated evidence supporting a wide range of roles of MMPs in various non-neoplastic diseases and provides an outlook on the therapeutic potential of inhibiting MMP action.
MeSH term(s)	Cardiovascular Diseases/physiopathology ; Digestive System Diseases/physiopathology ; Extracellular Matrix/enzymology ; Humans ; Inflammation/physiopathology ; Kidney Diseases/physiopathology ; Matrix Metalloproteinases/metabolism ; Neurodegenerative Diseases/physiopathology ; Respiration Disorders/physiopathology
Chemical Substances	Matrix Metalloproteinases (EC 3.4.24.-)
Language	English
Publishing date	2016-07-21
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms17071178
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Article ; Online: Interleukin-33 induces interleukin-8 expression via JNK/c-Jun/AP-1 pathway in human umbilical vein endothelial cells.

Umebashi, Katsuyuki / Tokito, Akinori / Yamamoto, Masayoshi / Jougasaki, Michihisa

PloS one

2018 Volume 13, Issue 1, Page(s) e0191659

Abstract: Interleukin (IL)-33 is a member of the IL-1 cytokine family with dual functions as a traditional cytokine and as a transcriptional regulator. We recently reported that IL-33 up-regulated growth regulated oncogene (GRO)-α/CXCL1 expression in human ... ...

Abstract	Interleukin (IL)-33 is a member of the IL-1 cytokine family with dual functions as a traditional cytokine and as a transcriptional regulator. We recently reported that IL-33 up-regulated growth regulated oncogene (GRO)-α/CXCL1 expression in human vascular endothelial cells. The aim of this study was to investigate the effect of IL-33 on the expression of IL-8/CXCL8, another member of the CXC-chemokine family, and to elucidate its signaling pathways in human umbilical vein endothelial cells (HUVECs). Immunocytochemical staining and Western immunoblot analysis revealed that IL-33 augmented IL-8 protein expression in HUVECs. Real time reverse transcription-polymerase chain reaction (RT-PCR) and enzyme-linked immunosorbent assay (ELISA) showed that IL-33 significantly increased IL-8 mRNA and secretion in a dose- and time-dependent manner. IL-33 preferentially stimulated proliferating subconfluent cells, and increased IL-8 secretion to a higher level compared with confluent cells. IL-33 also stimulated phosphorylations of c-Jun N-terminal kinase (JNK) and c-Jun, and enhanced activator protein (AP)-1 DNA-binding activity, all of which were suppressed by SP600125, a JNK inhibitor. Moreover, IL-33-induced IL-8 mRNA and secretion were also suppressed by SP600125. Transfection of c-Jun small interfering RNA into cultured HUVECs significantly reduced the IL-33-induced increase in IL-8 secretion from HUVECs. The present study demonstrates that IL-33 induces IL-8 expression via JNK/c-Jun/AP-1 pathway in human vascular endothelial cells, and provides a new insight into the role of IL-33-induced IL-8 in the pathophysiology of atherosclerosis and vascular inflammation.
MeSH term(s)	Blotting, Western ; Endothelium, Vascular/cytology ; Endothelium, Vascular/metabolism ; Enzyme-Linked Immunosorbent Assay ; Human Umbilical Vein Endothelial Cells ; Humans ; Interleukin-33/physiology ; Interleukin-8/metabolism ; JNK Mitogen-Activated Protein Kinases/metabolism ; Phosphorylation ; Proto-Oncogene Proteins c-jun/metabolism ; Real-Time Polymerase Chain Reaction ; Reverse Transcriptase Polymerase Chain Reaction ; Transcription Factor AP-1/metabolism
Chemical Substances	IL33 protein, human ; Interleukin-33 ; Interleukin-8 ; Proto-Oncogene Proteins c-jun ; Transcription Factor AP-1 ; JNK Mitogen-Activated Protein Kinases (EC 2.7.11.24)
Language	English
Publishing date	2018
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0191659
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Article: [Atherosclerosis and adrenomedullin].

Jougasaki, Michihisa

Nihon rinsho. Japanese journal of clinical medicine

2004 Volume 62 Suppl 9, Page(s) 280–283

MeSH term(s)	Adrenomedullin ; Animals ; Arteriosclerosis/diagnosis ; Arteriosclerosis/etiology ; Arteriosclerosis/physiopathology ; Biomarkers/blood ; Cardiovascular Physiological Phenomena ; Humans ; Neovascularization, Physiologic ; Oxidative Stress ; Peptides/blood ; Peptides/genetics ; Peptides/physiology
Chemical Substances	Biomarkers ; Peptides ; Adrenomedullin (148498-78-6)
Language	Japanese
Publishing date	2004-09
Publishing country	Japan
Document type	Journal Article ; Review
ZDB-ID	390903-7
ISSN	0047-1852
ISSN	0047-1852
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Article ; Online: Interleukin-33 induces growth-regulated oncogene-α expression and secretion in human umbilical vein endothelial cells.

Yamamoto, Masayoshi / Umebashi, Katsuyuki / Tokito, Akinori / Imamura, Junichi / Jougasaki, Michihisa

American journal of physiology. Regulatory, integrative and comparative physiology

2017 Volume 313, Issue 3, Page(s) R272–R279

Abstract: Although interleukin-33 (IL-33), a member of the IL-1 cytokine family, plays proinflammatory roles in immune cells as an "alarmin," little is known regarding the biological actions of IL-33 on vascular endothelial cells. To investigate the effects of IL- ... ...

Abstract	Although interleukin-33 (IL-33), a member of the IL-1 cytokine family, plays proinflammatory roles in immune cells as an "alarmin," little is known regarding the biological actions of IL-33 on vascular endothelial cells. To investigate the effects of IL-33 on vascular endothelial cells, we first screened the IL-33-regulated proteins in human umbilical vein endothelial cells (HUVECs) using a dot blot array and observed that IL-33 markedly increased growth-regulated oncogene-α (GRO-α), a chemokine that is also known as chemokine (C-X-C motif) ligand 1 (CXCL1). Real-time reverse transcription PCR and ELISA demonstrated that IL-33 induced GRO-α expression and secretion in HUVECs in a dose- and a time-dependent manner. Western immunoblot assay revealed that IL-33 activated the phosphorylation of extracellular signal-regulated kinase 1/2 (ERK1/2) and c-Jun NH
MeSH term(s)	Cells, Cultured ; Chemokine CXCL1/genetics ; Chemokine CXCL1/metabolism ; Endothelial Cells/metabolism ; Gene Expression Regulation, Developmental/physiology ; Humans ; Interleukin-33/metabolism ; Umbilical Veins/cytology ; Umbilical Veins/physiology ; Up-Regulation/physiology
Chemical Substances	CXCL1 protein, human ; Chemokine CXCL1 ; IL33 protein, human ; Interleukin-33
Language	English
Publishing date	2017-06-21
Publishing country	United States
Document type	Journal Article
ZDB-ID	603839-6
ISSN	1522-1490 ; 0363-6119
ISSN (online)	1522-1490
ISSN	0363-6119
DOI	10.1152/ajpregu.00435.2016
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