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Article ; Online: Hemin as a novel candidate for treating COVID-19 via heme oxygenase-1 induction.

Kim, Dong-Hwi / Ahn, Hee-Seop / Go, Hyeon-Jeong / Kim, Da-Yoon / Kim, Jae-Hyeong / Lee, Joong-Bok / Park, Seung-Yong / Song, Chang-Seon / Lee, Sang-Won / Ha, Sang-Do / Choi, Changsun / Choi, In-Soo

Scientific reports

2021 Volume 11, Issue 1, Page(s) 21462

Abstract: ... To confirm whether HO-1 suppresses SARS-CoV-2 infection, we assessed the antiviral activity of hemin ... an effective and safe HO-1 inducer, in SARS-CoV-2 infection. We found that treatment with hemin efficiently ... hemin indirectly increased the expression of interferon-stimulated proteins known to restrict SARS-CoV-2 ...

Abstract	Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the causative agent of the coronavirus disease-19 (COVID-19). More than 143 million cases of COVID-19 have been reported to date, with the global death rate at 2.13%. Currently, there are no licensed therapeutics for controlling SARS-CoV-2 infection. The antiviral effects of heme oxygenase-1 (HO-1), a cytoprotective enzyme that inhibits the inflammatory response and reduces oxidative stress, have been investigated in several viral infections. To confirm whether HO-1 suppresses SARS-CoV-2 infection, we assessed the antiviral activity of hemin, an effective and safe HO-1 inducer, in SARS-CoV-2 infection. We found that treatment with hemin efficiently suppressed SARS-CoV-2 replication (selectivity index: 249.7012). Besides, the transient expression of HO-1 using an expression vector also suppressed the growth of the virus in cells. Free iron and biliverdin, which are metabolic byproducts of heme catalysis by HO-1, also suppressed the viral infection. Additionally, hemin indirectly increased the expression of interferon-stimulated proteins known to restrict SARS-CoV-2 replication. Overall, the findings suggested that HO-1, induced by hemin, effectively suppressed SARS-CoV-2 in vitro. Therefore, HO-1 could be potential therapeutic candidate for COVID-19.
MeSH term(s)	Animals ; Antiviral Agents/chemistry ; Antiviral Agents/pharmacology ; Antiviral Agents/therapeutic use ; COVID-19/virology ; Cell Survival/drug effects ; Chlorocebus aethiops ; Heme Oxygenase-1/antagonists & inhibitors ; Heme Oxygenase-1/genetics ; Heme Oxygenase-1/metabolism ; Hemin/chemistry ; Hemin/pharmacology ; Hemin/therapeutic use ; Humans ; RNA Interference ; RNA, Small Interfering/metabolism ; RNA, Viral/metabolism ; SARS-CoV-2/genetics ; SARS-CoV-2/isolation & purification ; SARS-CoV-2/physiology ; Up-Regulation/drug effects ; Vero Cells ; Virus Replication/drug effects ; COVID-19 Drug Treatment
Chemical Substances	Antiviral Agents ; RNA, Small Interfering ; RNA, Viral ; Hemin (743LRP9S7N) ; Heme Oxygenase-1 (EC 1.14.14.18)
Language	English
Publishing date	2021-11-02
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-021-01054-3
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Microprocessor depends on hemin to recognize the apical loop of primary microRNA.

Nguyen, Tuan Anh / Park, Joha / Dang, Thi Lieu / Choi, Yeon-Gil / Kim, V Narry

Nucleic acids research

2018 Volume 46, Issue 11, Page(s) 5726–5736

Abstract: ... remains unknown. In this study, we find that hemin, a ferric ion-containing porphyrin, enhances ... mutant cell line and carrying out rescue experiments, we discover that hemin preferentially stimulates ... Our findings reveal the molecular action mechanism of hemin in pri-miRNA processing and establish a novel ...

Abstract	Microprocessor, which consists of a ribonuclease III DROSHA and its cofactor DGCR8, initiates microRNA (miRNA) maturation by cleaving primary miRNA transcripts (pri-miRNAs). We recently demonstrated that the DGCR8 dimer recognizes the apical elements of pri-miRNAs, including the UGU motif, to accurately locate and orient Microprocessor on pri-miRNAs. However, the mechanism underlying the selective RNA binding remains unknown. In this study, we find that hemin, a ferric ion-containing porphyrin, enhances the specific interaction between the apical UGU motif and the DGCR8 dimer, allowing Microprocessor to achieve high efficiency and fidelity of pri-miRNA processing in vitro. Furthermore, by generating a DGCR8 mutant cell line and carrying out rescue experiments, we discover that hemin preferentially stimulates the expression of miRNAs possessing the UGU motif, thereby conferring differential regulation of miRNA maturation. Our findings reveal the molecular action mechanism of hemin in pri-miRNA processing and establish a novel function of hemin in inducing specific RNA-protein interaction.
MeSH term(s)	Cell Line ; Gene Knockout Techniques ; Hemin/physiology ; Humans ; MicroRNAs/chemistry ; MicroRNAs/metabolism ; RNA Precursors/chemistry ; RNA Precursors/metabolism ; RNA-Binding Proteins/genetics ; RNA-Binding Proteins/metabolism ; Ribonuclease III/metabolism
Chemical Substances	DGCR8 protein, human ; MicroRNAs ; RNA Precursors ; RNA-Binding Proteins ; Hemin (743LRP9S7N) ; DROSHA protein, human (EC 3.1.26.3) ; Ribonuclease III (EC 3.1.26.3)
Language	English
Publishing date	2018-05-03
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	186809-3
ISSN	1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
ISSN (online)	1362-4962 ; 1362-4954
ISSN	0301-5610 ; 0305-1048
DOI	10.1093/nar/gky248
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Article ; Online: Hemin as a novel candidate for treating COVID-19 via heme oxygenase-1 induction

Dong-Hwi Kim / Hee-Seop Ahn / Hyeon-Jeong Go / Da-Yoon Kim / Jae-Hyeong Kim / Joong-Bok Lee / Seung-Yong Park / Chang-Seon Song / Sang-Won Lee / Sang-Do Ha / Changsun Choi / In-Soo Choi

Scientific Reports, Vol 11, Iss 1, Pp 1-

2021 Volume 9

Abstract	Abstract Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the causative agent of the coronavirus disease-19 (COVID-19). More than 143 million cases of COVID-19 have been reported to date, with the global death rate at 2.13%. Currently, there are no licensed therapeutics for controlling SARS-CoV-2 infection. The antiviral effects of heme oxygenase-1 (HO-1), a cytoprotective enzyme that inhibits the inflammatory response and reduces oxidative stress, have been investigated in several viral infections. To confirm whether HO-1 suppresses SARS-CoV-2 infection, we assessed the antiviral activity of hemin, an effective and safe HO-1 inducer, in SARS-CoV-2 infection. We found that treatment with hemin efficiently suppressed SARS-CoV-2 replication (selectivity index: 249.7012). Besides, the transient expression of HO-1 using an expression vector also suppressed the growth of the virus in cells. Free iron and biliverdin, which are metabolic byproducts of heme catalysis by HO-1, also suppressed the viral infection. Additionally, hemin indirectly increased the expression of interferon-stimulated proteins known to restrict SARS-CoV-2 replication. Overall, the findings suggested that HO-1, induced by hemin, effectively suppressed SARS-CoV-2 in vitro. Therefore, HO-1 could be potential therapeutic candidate for COVID-19.
Keywords	Medicine ; R ; Science ; Q
Subject code	570
Language	English
Publishing date	2021-11-01T00:00:00Z
Publisher	Nature Portfolio
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Effects of hemin on heme oxygenase-1, gastric emptying, and symptoms in diabetic gastroparesis.

Bharucha, A E / Daley, S L / Low, P A / Gibbons, S J / Choi, K M / Camilleri, M / Saw, J J / Farrugia, G / Zinsmeister, A R

Neurogastroenterology and motility : the official journal of the European Gastrointestinal Motility Society

2016 Volume 28, Issue 11, Page(s) 1731–1740

Abstract: ... gastric emptying (GE) in non-obese diabetic mice. Our hypothesis was that hemin upregulation of HO1 would restore ... normal GE in humans with gastroparesis.: Aims: To compare effects of hemin and placebo infusions ... we compared intravenous hemin, prepared in albumin, or albumin alone (placebo) in 20 patients, aged 41 ± 5 ...

Abstract	Background: Therapeutic options for management of diabetic gastroparesis are limited. Failure to maintain upregulation of heme oxygenase (HO1) leads to loss of interstitial cells of Cajal and delayed gastric emptying (GE) in non-obese diabetic mice. Our hypothesis was that hemin upregulation of HO1 would restore normal GE in humans with gastroparesis. Aims: To compare effects of hemin and placebo infusions on HO1 activity and protein, GE, autonomic function, and gastrointestinal symptoms in diabetic gastroparesis. Methods: In a single-center, double-blind, placebo-controlled, randomized clinical trial, we compared intravenous hemin, prepared in albumin, or albumin alone (placebo) in 20 patients, aged 41 ± 5 (SEM) years with diabetic gastroparesis. After infusions on days 1, 3, and 7, weekly infusions were administered for 7 additional weeks. Assessments included blood tests for HO1 protein and enzyme activity levels, GE with Key results: Nine of 11 patients randomized to hemin completed all study procedures. Compared to placebo, hemin increased HO1 protein on days 3 (p = 0.0002) and 7 (p = 0.008) and HO1 activity on day 3 (p = 0.0003) but not after. Gastric emptying, autonomic functions, and symptoms did not differ significantly in the hemin group relative to placebo. Conclusions & inferences: Hemin failed to sustain increased HO1 levels beyond a week and did not improve GE or symptoms in diabetic gastroparesis. Further studies are necessary to ascertain whether more frequent hemin infusions or other drugs would have a more sustained effect on HO1 and improve GE.
MeSH term(s)	Adult ; Aged ; Diabetes Mellitus/blood ; Diabetes Mellitus/drug therapy ; Double-Blind Method ; Female ; Gastric Emptying/drug effects ; Gastric Emptying/physiology ; Gastroparesis/blood ; Gastroparesis/drug therapy ; Heme Oxygenase-1/blood ; Hemin/administration & dosage ; Humans ; Infusions, Intravenous ; Male ; Middle Aged ; Treatment Outcome ; Young Adult
Chemical Substances	Hemin (743LRP9S7N) ; Heme Oxygenase-1 (EC 1.14.14.18)
Language	English
Publishing date	2016-06-09
Publishing country	England
Document type	Journal Article ; Randomized Controlled Trial
ZDB-ID	1186328-6
ISSN	1365-2982 ; 1350-1925
ISSN (online)	1365-2982
ISSN	1350-1925
DOI	10.1111/nmo.12874
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Zs.A 2979: Show issues

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Article ; Online: Voltage-Gated K+ Channel, Kv3.3 Is Involved in Hemin-Induced K562 Differentiation.

Song, Min Seok / Choi, Seon Young / Ryu, Pan Dong / Lee, So Yeong

PloS one

2016 Volume 11, Issue 2, Page(s) e0148633

Abstract: ... differentiation. Down-regulation of Kv3.3 using siRNA-Kv3.3 increased hemin-induced K562 erythroid differentiation ...

Abstract	Voltage-gated K+ (Kv) channels are well known to be involved in cell proliferation. However, even though cell proliferation is closely related to cell differentiation, the relationship between Kv channels and cell differentiation remains poorly investigated. This study demonstrates that Kv3.3 is involved in K562 cell erythroid differentiation. Down-regulation of Kv3.3 using siRNA-Kv3.3 increased hemin-induced K562 erythroid differentiation through decreased activation of signal molecules such as p38, cAMP response element-binding protein, and c-fos. Down-regulation of Kv3.3 also enhanced cell adhesion by increasing integrin β3 and this effect was amplified when the cells were cultured with fibronectin. The Kv channels, or at least Kv3.3, appear to be associated with cell differentiation; therefore, understanding the mechanisms of Kv channel regulation of cell differentiation would provide important information regarding vital cellular processes.
MeSH term(s)	Cell Adhesion/drug effects ; Cell Adhesion/genetics ; Cell Differentiation/drug effects ; Cell Differentiation/genetics ; Down-Regulation/drug effects ; Down-Regulation/genetics ; Fibronectins/pharmacology ; Hemin/pharmacology ; Humans ; Integrin beta3/biosynthesis ; K562 Cells ; Response Elements/physiology ; Shaw Potassium Channels/biosynthesis ; Shaw Potassium Channels/genetics
Chemical Substances	Fibronectins ; ITGB3 protein, human ; Integrin beta3 ; KCNC3 protein, human ; Shaw Potassium Channels ; Hemin (743LRP9S7N)
Language	English
Publishing date	2016-02-05
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.0148633
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Induction of heme oxygenase-1 with hemin reduces obesity-induced adipose tissue inflammation via adipose macrophage phenotype switching.

Tu, Thai Hien / Joe, Yeonsoo / Choi, Hye-Seon / Chung, Hun Taeg / Yu, Rina

Mediators of inflammation

2014 Volume 2014, Page(s) 290708

Abstract: ... we demonstrate that the HO-1 inducer, hemin, protects against obesity-induced adipose inflammation by inducing ... macrophages to switch to the M2 phenotype. HO-1 induction by hemin reduced the production of proinflammatory ... of inflammatory signaling molecules (JNK and NF-κB) in both cell types. Hemin enhanced transcript levels of M2 ...

Abstract	Adipose macrophages with the anti-inflammatory M2 phenotype protect against obesity-induced inflammation and insulin resistance. Heme oxygenase-1 (HO-1), which elicits antioxidant and anti-inflammatory activity, modulates macrophage phenotypes and thus is implicated in various inflammatory diseases. Here, we demonstrate that the HO-1 inducer, hemin, protects against obesity-induced adipose inflammation by inducing macrophages to switch to the M2 phenotype. HO-1 induction by hemin reduced the production of proinflammatory cytokines (TNF-α and IL-6) from cocultured adipocytes and macrophages by inhibiting the activation of inflammatory signaling molecules (JNK and NF-κB) in both cell types. Hemin enhanced transcript levels of M2 macrophage marker genes (IL-4, Mrc1, and Clec10a) in the cocultures, while reducing transcripts of M1 macrophage markers (CD274 and TNF-α). The protective effects of hemin on adipose inflammation and macrophage phenotype switching were confirmed in mice fed a high-fat diet, and these were associated with PPARγ upregulation and STAT6 activation. These findings suggest that induction of HO-1 with hemin protects against obesity-induced adipose inflammation through M2 macrophage phenotype switching, which is induced by the PPARγ and STAT6 pathway. HO-1 inducers such as hemin may be useful for preventing obesity-induced adipose inflammation.
MeSH term(s)	3T3-L1 Cells ; Adipocytes/drug effects ; Adipocytes/metabolism ; Adipocytes/pathology ; Adipose Tissue/drug effects ; Adipose Tissue/metabolism ; Adipose Tissue/pathology ; Animals ; Cell Line ; Coculture Techniques ; Cytokines/metabolism ; Enzyme Induction/drug effects ; Heme Oxygenase-1/biosynthesis ; Hemin/pharmacology ; Inflammation/metabolism ; Inflammation/pathology ; Inflammation/prevention & control ; Inflammation Mediators/metabolism ; Macrophages/drug effects ; Macrophages/metabolism ; Macrophages/pathology ; Male ; Mice ; Mice, Inbred C57BL ; Obesity/drug therapy ; Obesity/metabolism ; Obesity/pathology ; Phenotype ; Signal Transduction/drug effects
Chemical Substances	Cytokines ; Inflammation Mediators ; Hemin (743LRP9S7N) ; Heme Oxygenase-1 (EC 1.14.14.18)
Language	English
Publishing date	2014
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1137605-3
ISSN	1466-1861 ; 0962-9351
ISSN (online)	1466-1861
ISSN	0962-9351
DOI	10.1155/2014/290708
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Article ; Online: Voltage-Gated K+ Channel, Kv3.3 Is Involved in Hemin-Induced K562 Differentiation.

Min Seok Song / Seon Young Choi / Pan Dong Ryu / So Yeong Lee

PLoS ONE, Vol 11, Iss 2, p e

2016 Volume 0148633

Abstract: ... differentiation. Down-regulation of Kv3.3 using siRNA-Kv3.3 increased hemin-induced K562 erythroid differentiation ...

Abstract	Voltage-gated K+ (Kv) channels are well known to be involved in cell proliferation. However, even though cell proliferation is closely related to cell differentiation, the relationship between Kv channels and cell differentiation remains poorly investigated. This study demonstrates that Kv3.3 is involved in K562 cell erythroid differentiation. Down-regulation of Kv3.3 using siRNA-Kv3.3 increased hemin-induced K562 erythroid differentiation through decreased activation of signal molecules such as p38, cAMP response element-binding protein, and c-fos. Down-regulation of Kv3.3 also enhanced cell adhesion by increasing integrin β3 and this effect was amplified when the cells were cultured with fibronectin. The Kv channels, or at least Kv3.3, appear to be associated with cell differentiation; therefore, understanding the mechanisms of Kv channel regulation of cell differentiation would provide important information regarding vital cellular processes.
Keywords	Medicine ; R ; Science ; Q
Subject code	571
Language	English
Publishing date	2016-01-01T00:00:00Z
Publisher	Public Library of Science (PLoS)
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Induction of Heme Oxygenase-1 with Hemin Reduces Obesity-Induced Adipose Tissue Inflammation via Adipose Macrophage Phenotype Switching

Thai Hien Tu / Yeonsoo Joe / Hye-Seon Choi / Hun Taeg Chung / Rina Yu

Mediators of Inflammation, Vol

2014 Volume 2014

Keywords	Pathology ; RB1-214 ; Medicine ; R
Language	English
Publishing date	2014-01-01T00:00:00Z
Publisher	Hindawi Publishing Corporation
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Induction of Heme Oxygenase-1 with Hemin Reduces Obesity-Induced Adipose Tissue Inflammation via Adipose Macrophage Phenotype Switching

Thai Hien Tu / Yeonsoo Joe / Hye-Seon Choi / Hun Taeg Chung / Rina Yu

Mediators of Inflammation, Vol

2014 Volume 2014

Keywords	Pathology ; RB1-214 ; Medicine ; R
Language	English
Publishing date	2014-01-01T00:00:00Z
Publisher	Hindawi Publishing Corporation
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Induction of Heme Oxygenase-1 with Hemin Reduces Obesity-Induced Adipose Tissue Inflammation via Adipose Macrophage Phenotype Switching

Thai Hien Tu / Yeonsoo Joe / Hye-Seon Choi / Hun Taeg Chung / Rina Yu

Mediators of Inflammation, Vol

2014 Volume 2014

Keywords	Pathology ; RB1-214 ; Medicine ; R
Language	English
Publishing date	2014-01-01T00:00:00Z
Publisher	Hindawi Publishing Corporation
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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