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Article: Editorial: HTLV-1: addressing unmet research needs, volume II.

Cunha, Marcela S / Zhang, Wei / Mansky, Louis M / Mendonça, Luiza M

2023 Volume 14, Page(s) 1306416

Language	English
Publishing date	2023-10-26
Publishing country	Switzerland
Document type	Editorial
ZDB-ID	2587354-4
ISSN	1664-302X
ISSN	1664-302X
DOI	10.3389/fmicb.2023.1306416
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Article ; Online: Tucum-do-cerrado (Bactris setosa Mart.) modulates oxidative stress, inflammation, and apoptosis-related proteins in rats treated with azoxymethane.

Campos, Natália A / da Cunha, Marcela S B / Arruda, Sandra F

PloS one

2018 Volume 13, Issue 11, Page(s) e0206670

Abstract: Oxidative and inflammatory responses play an important role in the development and prevention of cancer, with both responses being modulated by phytochemical compounds. This study investigated the chemopreventive effect of tucum-do-cerrado fruit in rats ... ...

Abstract	Oxidative and inflammatory responses play an important role in the development and prevention of cancer, with both responses being modulated by phytochemical compounds. This study investigated the chemopreventive effect of tucum-do-cerrado fruit in rats treated with azoxymethane. Wistar rats were treated for 12 weeks with: a control diet (CT); a control diet + AOM (CT/DR); a control diet + 15% tucum-do-cerrado (TU); or a control diet + 15% tucum-do-cerrado + AOM (TU/DR). The association of tucum-do-cerrado and AOM (TU/DR) increased glutathione-S-transferase activity, decreased MDA levels, increased levels of COX2, TNFα and BAX, and decreased Bcl2/Bax ratio, compared to the CT/DR group. Carbonyl levels, IL-1β and IL-6 mRNA levels, and aberrant crypt foci showed no difference between the treatments. In conclusion, tucum-do-cerrado reduced lipid oxidative damage, induced a pro-inflammatory effect, and promoted a pro-apoptotic "environment" in rats treated with AOM; however no changes in aberrant crypts were observed.
MeSH term(s)	Animals ; Apoptosis/drug effects ; Apoptosis/physiology ; Arecaceae ; Azoxymethane ; Colon/metabolism ; Colon/pathology ; Colonic Neoplasms/metabolism ; Colonic Neoplasms/pathology ; Colonic Neoplasms/therapy ; Disease Models, Animal ; Fruit ; Inflammation/metabolism ; Inflammation/pathology ; Inflammation/therapy ; Liver/metabolism ; Male ; Oxidative Stress/physiology ; Phytotherapy ; Rats, Wistar
Chemical Substances	Azoxymethane (MO0N1J0SEN)
Language	English
Publishing date	2018-11-14
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.0206670
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Article: Chikungunya Virus: An Emergent Arbovirus to the South American Continent and a Continuous Threat to the World.

Cunha, Marcela S / Costa, Pedro A G / Correa, Isadora Alonso / de Souza, Marcos R M / Calil, Pedro Teles / da Silva, Gustavo P Duarte / Costa, Sara Mesquita / Fonseca, Vinícius Wakoff P / da Costa, Luciana J

Frontiers in microbiology

2020 Volume 11, Page(s) 1297

Abstract: Chikungunya virus (CHIKV) is an arthropod-borne virus (arbovirus) of epidemic concern, transmitted ... ...

Abstract	Chikungunya virus (CHIKV) is an arthropod-borne virus (arbovirus) of epidemic concern, transmitted by
Language	English
Publishing date	2020-06-26
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2587354-4
ISSN	1664-302X
ISSN	1664-302X
DOI	10.3389/fmicb.2020.01297
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Article ; Online: Vitamin A deficiency modulates iron metabolism via ineffective erythropoiesis.

da Cunha, Marcela S B / Siqueira, Egle M A / Trindade, Luciano S / Arruda, Sandra F

The Journal of nutritional biochemistry

2014 Volume 25, Issue 10, Page(s) 1035–1044

Abstract: Vitamin A modulates inflammatory status, iron metabolism and erythropoiesis. Given that these factors modulate the expression of the hormone hepcidin (Hamp), we investigated the effect of vitamin A deficiency on molecular biomarkers of iron metabolism, ... ...

Abstract	Vitamin A modulates inflammatory status, iron metabolism and erythropoiesis. Given that these factors modulate the expression of the hormone hepcidin (Hamp), we investigated the effect of vitamin A deficiency on molecular biomarkers of iron metabolism, the inflammatory response and the erythropoietic system. Five groups of male Wistar rats were treated: control (AIN-93G), the vitamin A-deficient (VAD) diet, the iron-deficient (FeD) diet, the vitamin A- and iron-deficient (VAFeD) diet or the diet with 12 mg atRA/kg diet replacing all-trans-retinyl palmitate by all-trans retinoic acid (atRA). Vitamin A deficiency reduced serum iron and transferrin saturation levels, increased spleen iron concentrations, reduced hepatic Hamp and kidney erythropoietin messenger RNA (mRNA) levels and up-regulated hepatic and spleen heme oxygenase-1 gene expression while reducing the liver HO-1 specific activity compared with the control. The FeD and VAFeD rats exhibited lower levels of serum iron and transferrin saturation, lower iron concentrations in tissues and lower hepatic Hamp mRNA levels compared with the control. The treatment with atRA resulted in lower serum iron and transferrin concentrations, an increased iron concentration in the liver, a decreased iron concentration in the spleen and in the gut, and decreased hepatic Hamp mRNA levels. In summary, these findings suggest that vitamin A deficiency leads to ineffective erythropoiesis by the down-regulation of renal erythropoietin expression in the kidney, resulting in erythrocyte malformation and the consequent accumulation of the heme group in the spleen. Vitamin A deficiency indirectly modulates systemic iron homeostasis by enhancing erythrophagocytosis of undifferentiated erythrocytes.
MeSH term(s)	Animals ; Biomarkers/blood ; Cation Transport Proteins/genetics ; Cation Transport Proteins/metabolism ; Down-Regulation ; Erythrocytes/metabolism ; Erythropoiesis ; Erythropoietin/blood ; Erythropoietin/genetics ; Genetic Markers ; Heme Oxygenase (Decyclizing)/genetics ; Heme Oxygenase (Decyclizing)/metabolism ; Hepcidins/blood ; Hepcidins/genetics ; Homeostasis ; Interleukin-1beta/blood ; Interleukin-1beta/genetics ; Interleukin-6/blood ; Interleukin-6/genetics ; Iron/blood ; Iron/deficiency ; Kidney/metabolism ; Liver/metabolism ; Male ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; Rats ; Rats, Wistar ; Spleen/metabolism ; Suppressor of Cytokine Signaling 3 Protein ; Suppressor of Cytokine Signaling Proteins/genetics ; Suppressor of Cytokine Signaling Proteins/metabolism ; Transferrin/metabolism ; Up-Regulation ; Vitamin A/administration & dosage ; Vitamin A/blood ; Vitamin A Deficiency/blood
Chemical Substances	Biomarkers ; Cation Transport Proteins ; Genetic Markers ; Hamp protein, rat ; Hepcidins ; Interleukin-1beta ; Interleukin-6 ; RNA, Messenger ; Socs3 protein, rat ; Suppressor of Cytokine Signaling 3 Protein ; Suppressor of Cytokine Signaling Proteins ; Transferrin ; metal transporting protein 1 ; Erythropoietin (11096-26-7) ; Vitamin A (11103-57-4) ; Iron (E1UOL152H7) ; Heme Oxygenase (Decyclizing) (EC 1.14.14.18) ; Hmox1 protein, rat (EC 1.14.14.18)
Language	English
Publishing date	2014-10
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1014929-6
ISSN	1873-4847 ; 0955-2863
ISSN (online)	1873-4847
ISSN	0955-2863
DOI	10.1016/j.jnutbio.2014.05.005
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Article ; Online: Tucum-Do-Cerrado (Bactris setosa Mart.) Consumption Modulates Iron Homeostasis and Prevents Iron-Induced Oxidative Stress in the Rat Liver.

Fustinoni-Reis, Adriana M / Arruda, Sandra F / Dourado, Lívia P S / da Cunha, Marcela S B / Siqueira, Egle M A

Nutrients

2016 Volume 8, Issue 2, Page(s) 38

Abstract: This study investigated the effect of tucum-do-cerrado consumption in the oxidative status of iron-supplemented rats. Four groups of rats were treated: Control (AIN-93G), Tuc (AIN-93G added of tucum-do-cerrado), Fe (AIN-93G iron-enriched), or TucFe (AIN- ... ...

Abstract	This study investigated the effect of tucum-do-cerrado consumption in the oxidative status of iron-supplemented rats. Four groups of rats were treated: Control (AIN-93G), Tuc (AIN-93G added of tucum-do-cerrado), Fe (AIN-93G iron-enriched), or TucFe (AIN-93G with tucum-do-cerrado and iron-enriched) diet, for 30 days. Iron-enriched diet increased serum, liver, spleen, and intestine iron levels; transferrin saturation; liver lipid oxidation; mRNA levels of hepatic Hamp and Bmp6, and Nrf2 in the intestine. Tucum-do-cerrado consumption reduced spleen lipid and protein oxidation; mRNA levels of hepatic Hamp and Ftl, and increased serum antioxidant capacity and hepatic mRNA levels of Bmp6, Hmox1, Nqo1, and Nrf2. TucFe diet consumption abrogated the liver Hamp iron-induced up-regulation, prevented intestinal iron accumulation; hepatic lipid peroxidation; splenic protein damage, and the increase of catalase, glutathione reductase, and glutathione peroxidase activity in some tissues. These results suggest that tucum-do-cerrado protects tissues against oxidative damage, by reducing iron availability in liver and consequently inhibiting liver Hamp expression.
MeSH term(s)	Animals ; Antioxidants/metabolism ; Antioxidants/pharmacology ; Arecaceae ; Catalase/metabolism ; Diet ; Food, Fortified ; Glutathione/metabolism ; Hepcidins/genetics ; Hepcidins/metabolism ; Homeostasis ; Intestines/drug effects ; Intestines/metabolism ; Iron/blood ; Iron/metabolism ; Lipid Peroxidation/drug effects ; Liver/drug effects ; Liver/metabolism ; Male ; Oxidative Stress/drug effects ; Plant Extracts/pharmacology ; Protein Carbonylation/drug effects ; RNA, Messenger/metabolism ; Rats, Wistar ; Spleen/drug effects ; Spleen/metabolism ; Up-Regulation
Chemical Substances	Antioxidants ; Hamp protein, rat ; Hepcidins ; Plant Extracts ; RNA, Messenger ; Iron (E1UOL152H7) ; Catalase (EC 1.11.1.6) ; Glutathione (GAN16C9B8O)
Language	English
Publishing date	2016-02-17
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2518386-2
ISSN	2072-6643 ; 2072-6643
ISSN (online)	2072-6643
ISSN	2072-6643
DOI	10.3390/nu8020038
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Article: Vitamin A deficiency modulates iron metabolism via ineffective erythropoiesis

da Cunha, Marcela S.B / Egle M.A. Siqueira / Luciano S. Trindade / Sandra F. Arruda

Journal of nutritional biochemistry. 2014 Oct., v. 25

2014

Abstract	Vitamin A modulates inflammatory status, iron metabolism and erythropoiesis. Given that these factors modulate the expression of the hormone hepcidin (Hamp), we investigated the effect of vitamin A deficiency on molecular biomarkers of iron metabolism, the inflammatory response and the erythropoietic system. Five groups of male Wistar rats were treated: control (AIN-93G), the vitamin A-deficient (VAD) diet, the iron-deficient (FeD) diet, the vitamin A- and iron-deficient (VAFeD) diet or the diet with 12 mg atRA/kg diet replacing all-trans-retinyl palmitate by all-trans retinoic acid (atRA). Vitamin A deficiency reduced serum iron and transferrin saturation levels, increased spleen iron concentrations, reduced hepatic Hamp and kidney erythropoietin messenger RNA (mRNA) levels and up-regulated hepatic and spleen heme oxygenase-1 gene expression while reducing the liver HO-1 specific activity compared with the control. The FeD and VAFeD rats exhibited lower levels of serum iron and transferrin saturation, lower iron concentrations in tissues and lower hepatic Hamp mRNA levels compared with the control. The treatment with atRA resulted in lower serum iron and transferrin concentrations, an increased iron concentration in the liver, a decreased iron concentration in the spleen and in the gut, and decreased hepatic Hamp mRNA levels. In summary, these findings suggest that vitamin A deficiency leads to ineffective erythropoiesis by the down-regulation of renal erythropoietin expression in the kidney, resulting in erythrocyte malformation and the consequent accumulation of the heme group in the spleen. Vitamin A deficiency indirectly modulates systemic iron homeostasis by enhancing erythrophagocytosis of undifferentiated erythrocytes.
Keywords	abnormal development ; biomarkers ; blood serum ; diet ; erythrocytes ; erythropoiesis ; erythropoietin ; gene expression ; gene expression regulation ; heme ; heme oxygenase (biliverdin-producing) ; hepcidin ; homeostasis ; inflammation ; iron ; iron absorption ; kidneys ; liver ; males ; messenger RNA ; palmitates ; rats ; retinoic acid ; spleen ; transferrin ; vitamin A ; vitamin A deficiency
Language	English
Dates of publication	2014-10
Size	p. 1035-1044.
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	1014929-6
ISSN	1873-4847 ; 0955-2863
ISSN (online)	1873-4847
ISSN	0955-2863
DOI	10.1016/j.jnutbio.2014.05.005
Database	NAL-Catalogue (AGRICOLA)

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Article: Tucum-Do-Cerrado (<i>Bactris setosa</i> Mart.) Consumption Modulates Iron Homeostasis and Prevents Iron-Induced Oxidative Stress in the Rat Liver

Fustinoni-Reis, Adriana M / Arruda, Sandra F / Dourado, Lívia P. S / da Cunha, Marcela S. B / Siqueira, Egle M. A

Nutrients. 2016 Feb. 17, v. 8, no. 2

2016

Abstract	This study investigated the effect of tucum-do-cerrado consumption in the oxidative status of iron-supplemented rats. Four groups of rats were treated: Control (AIN-93G), Tuc (AIN-93G added of tucum-do-cerrado), Fe (AIN-93G iron-enriched), or TucFe (AIN-93G with tucum-do-cerrado and iron-enriched) diet, for 30 days. Iron-enriched diet increased serum, liver, spleen, and intestine iron levels; transferrin saturation; liver lipid oxidation; mRNA levels of hepatic Hamp and Bmp6, and Nrf2 in the intestine. Tucum-do-cerrado consumption reduced spleen lipid and protein oxidation; mRNA levels of hepatic Hamp and Ftl, and increased serum antioxidant capacity and hepatic mRNA levels of Bmp6, Hmox1, Nqo1, and Nrf2. TucFe diet consumption abrogated the liver Hamp iron-induced up-regulation, prevented intestinal iron accumulation; hepatic lipid peroxidation; splenic protein damage, and the increase of catalase, glutathione reductase, and glutathione peroxidase activity in some tissues. These results suggest that tucum-do-cerrado protects tissues against oxidative damage, by reducing iron availability in liver and consequently inhibiting liver Hamp expression.
Keywords	Bactris setosa ; antioxidant activity ; blood serum ; catalase ; diet ; enzyme activity ; glutathione peroxidase ; glutathione-disulfide reductase ; homeostasis ; intestines ; iron ; lipid peroxidation ; lipids ; liver ; messenger RNA ; oxidation ; oxidative stress ; rats ; spleen ; tissues ; transferrin
Language	English
Dates of publication	2016-0217
Publishing place	Multidisciplinary Digital Publishing Institute
Document type	Article
ZDB-ID	2518386-2
ISSN	2072-6643
ISSN	2072-6643
DOI	10.3390/nu8020038
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Autochthonous Transmission of East/Central/South African Genotype Chikungunya Virus, Brazil.

Cunha, Marcela S / Cruz, Nádia V G / Schnellrath, Laila C / Medaglia, Maria Luiza Gomes / Casotto, Michele E / Albano, Rodolpho M / Costa, Luciana J / Damaso, Clarissa R

Emerging infectious diseases

2017 Volume 23, Issue 10, Page(s) 1737–1739

Abstract: We isolated East/Central/South African genotype chikungunya virus during the 2016 epidemic in Rio de Janeiro, Brazil. Genome sequencing revealed unique mutations in the nonstructural protein 4 (NSP4-A481D) and envelope protein 1 (E1-K211T). Moreover, all ...

Abstract	We isolated East/Central/South African genotype chikungunya virus during the 2016 epidemic in Rio de Janeiro, Brazil. Genome sequencing revealed unique mutations in the nonstructural protein 4 (NSP4-A481D) and envelope protein 1 (E1-K211T). Moreover, all Brazil East/Central/South isolates shared the exclusive mutations E1-M407L and E2-A103T.
Language	English
Publishing date	2017
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1380686-5
ISSN	1080-6059 ; 1080-6040
ISSN (online)	1080-6059
ISSN	1080-6040
DOI	10.3201/eid2310.161855
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Article: Co-occurrence of sporadic parkinsonism and late-onset Alzheimer's disease in a Brazilian male with the LRRK2 p.G2019S mutation.

Santos-Rebouças, Cíntia B / Abdalla, Cláudia B / Baldi, Fábio José R / Martins, Paloma A / Corrêa, Juliana C / Gonçalves, Andressa P / Cunha, Marcela S / Borges, Margarete B / Pereira, João S / Laks, Jerson / Pimentel, Márcia M G

Genetic testing

2008 Volume 12, Issue 4, Page(s) 471–473

Abstract: Mutations in the leucine-rich repeat kinase 2 (LRRK2) gene represent the most common known genetic cause of inherited and idiopathic Parkinson's disease (PD) in different populations. The predicted multifunctionality of LRRK2 product and the pleomorphic ... ...

Abstract	Mutations in the leucine-rich repeat kinase 2 (LRRK2) gene represent the most common known genetic cause of inherited and idiopathic Parkinson's disease (PD) in different populations. The predicted multifunctionality of LRRK2 product and the pleomorphic pathology associated with LRRK2 mutations place this gene as a potential candidate for other neurodegenerative disorders, mainly Alzheimer's disease (AD). We report a Brazilian male expressing both late-onset AD and slowly progressive parkinsonism signs, and who presented the most frequent LRRK2 mutation (p.G2019S). Although the co-occurrence of PD and AD would be expected occasionally, the shared mechanisms between the two complex disorders are still unclear and are discussed herein. In light of recent findings about the wide role of LRRK2 under normal and pathological conditions, it is tempting to speculate that LRRK2 mutations might play an upstream influence on the etiology of not just PD but also several alpha-synuclein and tau pathologies, including AD.
MeSH term(s)	Aged ; Aged, 80 and over ; Alzheimer Disease/complications ; Alzheimer Disease/genetics ; Brazil ; Humans ; Leucine-Rich Repeat Serine-Threonine Protein Kinase-2 ; Male ; Parkinsonian Disorders/complications ; Parkinsonian Disorders/genetics ; Point Mutation ; Protein-Serine-Threonine Kinases/genetics
Chemical Substances	LRRK2 protein, human (EC 2.7.11.1) ; Leucine-Rich Repeat Serine-Threonine Protein Kinase-2 (EC 2.7.11.1) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1)
Language	English
Publishing date	2008-12
Publishing country	United States
Document type	Case Reports ; Letter ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1345729-9
ISSN	1557-7473 ; 1090-6576
ISSN (online)	1557-7473
ISSN	1090-6576
DOI	10.1089/gte.2008.0042
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