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Article ; Online: Identification of iodotyrosines as novel substrates for the thyroid hormone transporter MCT8.

Groeneweg, Stefan / Zevenbergen, Chantal / Lima de Souza, Elaine C / van Geest, Ferdy S / Kloeckener-Gruissem, Barbara / Laczko, Endre / Camargo, Simone M R / Meima, Marcel E / Peeters, Robin P / Visser, W Edward

Thyroid : official journal of the American Thyroid Association

2024

Abstract: ... analysis identified 21 m/z ratios, corresponding to 87 candidate metabolites, with a 2.0-times differential ...

Abstract	Background Monocarboxylate transporter 8 (MCT8) is the most specific thyroid hormone transporter identified to date, deficiency of which has been associated with severe intellectual and motor disability and abnormal serum thyroid function tests. However, it is currently unknown if MCT8, like other thyroid hormone transporters, also accepts additional substrates, and if disruption of their transport may contribute to the observed phenotype. Methods In this study, we aimed to identify such substrates by applying LC-MS-based metabolome analysis in lysates of control and MCT8-overexpressing Xenopus oocytes. A subset of identified candidate substrates was validated by direct transport studies in transiently transfected COS-1 cells and human fibroblasts which endogenously express MCT8. Moreover, transport characteristics were determined, including transport saturation and cis-inhibition potency of thyroid hormone transport. Results Metabolome analysis identified 21 m/z ratios, corresponding to 87 candidate metabolites, with a 2.0-times differential abundance in MCT8-injected oocytes compared to controls. These metabolites included 3,5-diiodotyrosine (DIT) and several amino acids, including glutamate and glutamine. In accordance, MCT8-expressing COS-1 cells had 2.2-times lower intracellular accumulation of [125I]-DIT compared to control cells. This effect was largely blocked in the presence of T3 (IC50: 2.5±1.5 µM) or T4 (IC50: 5.8±1.3 µM). Conversely, increasing concentrations of DIT enhanced the accumulation of T3 and T4. The MCT8-specific inhibitor silychristin increased the intracellular accumulation of DIT in human fibroblasts. COS-1 cells expressing MCT8 also exhibited a 50%-reduction in intracellular accumulation of [125I]-3-monoiodotyrosine (MIT). In contrast, COS-1 cells expressing MCT8 did not alter the intracellular accumulation of [3H]-glutamate or [3H]-glutamine in. However, studies in human fibroblasts showed a 1.5-1.9-times higher glutamate uptake in control fibroblasts compared to fibroblasts derived from patients with MCT8 deficiency, which was not affected in the presence of silychristin. Conclusions Taken together, our results suggest that the iodotyrosines DIT and MIT can be exported by MCT8. MIT and DIT interfere with MCT8-mediated transport of thyroid hormone in vitro, and vice versa. Future studies should elucidate if MCT8, being highly expressed in thyroidal follicular cells, also transports iodotyrosines in vivo.
Language	English
Publishing date	2024-04-25
Publishing country	United States
Document type	Journal Article
ZDB-ID	1086044-7
ISSN	1557-9077 ; 1050-7256
ISSN (online)	1557-9077
ISSN	1050-7256
DOI	10.1089/thy.2023.0551
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Article ; Online: ACE2 and gut amino acid transport.

Camargo, Simone M R / Vuille-Dit-Bille, Raphael N / Meier, Chantal F / Verrey, François

Clinical science (London, England : 1979)

2020 Volume 134, Issue 21, Page(s) 2823–2833

Abstract: ACE2 is a type I membrane protein with extracellular carboxypeptidase activity displaying a broad tissue distribution with highest expression levels at the brush border membrane (BBM) of small intestine enterocytes and a lower expression in stomach and ... ...

Abstract	ACE2 is a type I membrane protein with extracellular carboxypeptidase activity displaying a broad tissue distribution with highest expression levels at the brush border membrane (BBM) of small intestine enterocytes and a lower expression in stomach and colon. In small intestinal mucosa, ACE2 mRNA expression appears to increase with age and to display higher levels in patients taking ACE-inhibitors (ACE-I). There, ACE2 protein heterodimerizes with the neutral amino acid transporter Broad neutral Amino acid Transporter 1 (B0AT1) (SLC6A19) or the imino acid transporter Sodium-dependent Imino Transporter 1 (SIT1) (SLC6A20), associations that are required for the surface expression of these transport proteins. These heterodimers can form quaternary structures able to function as binding sites for SARS-CoV-2 spike glycoproteins. The heterodimerization of the carboxypeptidase ACE2 with B0AT1 is suggested to favor the direct supply of substrate amino acids to the transporter, but whether this association impacts the ability of ACE2 to mediate viral infection is not known. B0AT1 mutations cause Hartnup disorder, a condition characterized by neutral aminoaciduria and, in some cases, pellagra-like symptoms, such as photosensitive rash, diarrhea, and cerebellar ataxia. Correspondingly, the lack of ACE2 and the concurrent absence of B0AT1 expression in small intestine causes a decrease in l-tryptophan absorption, niacin deficiency, decreased intestinal antimicrobial peptide production, and increased susceptibility to inflammatory bowel disease (IBD) in mice. Thus, the abundant expression of ACE2 in small intestine and its association with amino acid transporters appears to play a crucial role for the digestion of peptides and the absorption of amino acids and, thereby, for the maintenance of structural and functional gut integrity.
MeSH term(s)	Amino Acid Transport Systems, Neutral/metabolism ; Angiotensin-Converting Enzyme 2 ; Animals ; Betacoronavirus/pathogenicity ; COVID-19 ; Coronavirus Infections/enzymology ; Coronavirus Infections/virology ; Host-Pathogen Interactions ; Humans ; Inflammatory Bowel Diseases/genetics ; Inflammatory Bowel Diseases/metabolism ; Intestinal Absorption ; Intestinal Mucosa/enzymology ; Membrane Transport Proteins/metabolism ; Pandemics ; Peptidyl-Dipeptidase A/genetics ; Peptidyl-Dipeptidase A/metabolism ; Pneumonia, Viral/enzymology ; Pneumonia, Viral/virology ; Protein Multimerization ; SARS-CoV-2 ; Virus Internalization
Chemical Substances	Amino Acid Transport Systems, Neutral ; Membrane Transport Proteins ; SLC6A19 protein, human ; SLC6A20 protein, human ; Peptidyl-Dipeptidase A (EC 3.4.15.1) ; ACE2 protein, human (EC 3.4.17.23) ; Ace2 protein, mouse (EC 3.4.17.23) ; Angiotensin-Converting Enzyme 2 (EC 3.4.17.23)
Keywords	covid19
Language	English
Publishing date	2020-11-03
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	206835-7
ISSN	1470-8736 ; 0301-0538 ; 0009-0360 ; 0143-5221
ISSN (online)	1470-8736
ISSN	0301-0538 ; 0009-0360 ; 0143-5221
DOI	10.1042/CS20200477
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Article ; Online: Phosphorylation of mouse intestinal basolateral amino acid uniporter LAT4 is controlled by food-entrained diurnal rhythm and dietary proteins.

Oparija-Rogenmozere, Lalita / Rajendran, Anuradha / Poncet, Nadège / Camargo, Simone M R / Verrey, François

PloS one

2020 Volume 15, Issue 5, Page(s) e0233863

Abstract: Adaptive regulation of epithelial transporters to nutrient intake is essential to decrease energy costs of their synthesis and maintenance, however such regulation is understudied. Previously we demonstrated that the transport function of the basolateral ...

Abstract	Adaptive regulation of epithelial transporters to nutrient intake is essential to decrease energy costs of their synthesis and maintenance, however such regulation is understudied. Previously we demonstrated that the transport function of the basolateral amino acid uniporter LAT4 (Slc43a2) is increased by dephosphorylation of serine 274 (S274) and nearly abolished by dephosphorylation of serine 297 (S297) when expressed in Xenopus oocytes. Phosphorylation changes in the jejunum of food-entrained mice suggested an increase in LAT4 transport function during food expectation. Thus, we investigated further how phosphorylation, expression and localization of mouse intestinal LAT4 respond to food-entrained diurnal rhythm and dietary protein content. In mice entrained with 18% protein diet, LAT4 mRNA was not submitted to diurnal regulation, unlike mRNAs of luminal symporters and antiporters. Only in duodenum, LAT4 protein expression increased during food intake. Concurrently, S274 phosphorylation was decreased in all three small intestinal segments, whereas S297 phosphorylation was increased only in jejunum. Interestingly, during food intake, S274 phosphorylation was nearly absent in ileum and accompanied by strong phosphorylation of mTORC1 target S6. Entraining mice with 8% protein diet provoked a shift in jejunal LAT4 localization from the cell surface to intracellular stores and increased S274 phosphorylation in both jejunum and ileum during food anticipation, suggesting decreased transport function. In contrast, 40% dietary protein content led to increased LAT4 expression in jejunum and its internalization in ileum. Ex vivo treatments of isolated intestinal villi fraction demonstrated that S274 phosphorylation was stimulated by protein kinase A. Rapamycin-sensitive insulin treatment and amino acids increased S297 phosphorylation, suggesting that the response to food intake might be regulated via the insulin-mTORC1 pathway. Ghrelin, an oscillating orexigenic hormone, did not affect phosphorylation of intestinal LAT4. Overall, we show that phosphorylation, expression and localization of intestinal mouse LAT4 responds to diurnal and dietary stimuli in location-specific manner.
MeSH term(s)	Amino Acid Transport System L/metabolism ; Amino Acid Transport System y+/metabolism ; Amino Acids/metabolism ; Animals ; Antiporters/metabolism ; Circadian Rhythm/drug effects ; Cyclic AMP-Dependent Protein Kinases/metabolism ; Dietary Proteins/pharmacology ; Food ; Gene Expression Regulation/drug effects ; Ghrelin/administration & dosage ; Ghrelin/pharmacology ; Insulin/metabolism ; Intestine, Small/metabolism ; Intestines/physiology ; Mechanistic Target of Rapamycin Complex 1/metabolism ; Mice, Inbred C57BL ; Microvilli/drug effects ; Microvilli/metabolism ; Phosphorylation/drug effects ; Phosphoserine/metabolism ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; Subcellular Fractions/metabolism ; Symporters/metabolism ; TOR Serine-Threonine Kinases/metabolism
Chemical Substances	Amino Acid Transport System L ; Amino Acid Transport System y+ ; Amino Acids ; Antiporters ; Dietary Proteins ; Ghrelin ; Insulin ; RNA, Messenger ; Slc43a2 protein, mouse ; Symporters ; Phosphoserine (17885-08-4) ; TOR Serine-Threonine Kinases (EC 2.7.1.1) ; Mechanistic Target of Rapamycin Complex 1 (EC 2.7.11.1) ; Cyclic AMP-Dependent Protein Kinases (EC 2.7.11.11)
Language	English
Publishing date	2020-05-29
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.0233863
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Phosphorylation of mouse intestinal basolateral amino acid uniporter LAT4 is controlled by food-entrained diurnal rhythm and dietary proteins.

Lalita Oparija-Rogenmozere / Anuradha Rajendran / Nadège Poncet / Simone M R Camargo / François Verrey

PLoS ONE, Vol 15, Iss 5, p e

2020 Volume 0233863

Abstract	Adaptive regulation of epithelial transporters to nutrient intake is essential to decrease energy costs of their synthesis and maintenance, however such regulation is understudied. Previously we demonstrated that the transport function of the basolateral amino acid uniporter LAT4 (Slc43a2) is increased by dephosphorylation of serine 274 (S274) and nearly abolished by dephosphorylation of serine 297 (S297) when expressed in Xenopus oocytes. Phosphorylation changes in the jejunum of food-entrained mice suggested an increase in LAT4 transport function during food expectation. Thus, we investigated further how phosphorylation, expression and localization of mouse intestinal LAT4 respond to food-entrained diurnal rhythm and dietary protein content. In mice entrained with 18% protein diet, LAT4 mRNA was not submitted to diurnal regulation, unlike mRNAs of luminal symporters and antiporters. Only in duodenum, LAT4 protein expression increased during food intake. Concurrently, S274 phosphorylation was decreased in all three small intestinal segments, whereas S297 phosphorylation was increased only in jejunum. Interestingly, during food intake, S274 phosphorylation was nearly absent in ileum and accompanied by strong phosphorylation of mTORC1 target S6. Entraining mice with 8% protein diet provoked a shift in jejunal LAT4 localization from the cell surface to intracellular stores and increased S274 phosphorylation in both jejunum and ileum during food anticipation, suggesting decreased transport function. In contrast, 40% dietary protein content led to increased LAT4 expression in jejunum and its internalization in ileum. Ex vivo treatments of isolated intestinal villi fraction demonstrated that S274 phosphorylation was stimulated by protein kinase A. Rapamycin-sensitive insulin treatment and amino acids increased S297 phosphorylation, suggesting that the response to food intake might be regulated via the insulin-mTORC1 pathway. Ghrelin, an oscillating orexigenic hormone, did not affect phosphorylation of intestinal ...
Keywords	Medicine ; R ; Science ; Q
Subject code	570
Language	English
Publishing date	2020-01-01T00:00:00Z
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: Managers’ influence on company capabilities / A influência dos gestores nas capacidades da empresa

Juliana C. N. Costa / Shirlei M. Camargo / Ana M. M. Toaldo / Simone R. Didonet

RAM. Revista de Administração Mackenzie, Vol 20, Iss

2019 Volume 06

Abstract: Purpose: This study aims to verify the moderating role of managers’ characteristics, age, and tenure (time in the sector, position, company), in the relation between the realized absorptive capacity (RACAP) and the architectural marketing capabilities ( ... ...

Abstract	Purpose: This study aims to verify the moderating role of managers’ characteristics, age, and tenure (time in the sector, position, company), in the relation between the realized absorptive capacity (RACAP) and the architectural marketing capabilities (CAM). Originality/value: The present study considers the human element as a factor that affects the relations between the capacities of the company. It contributes theoretically to help understand what can impact the formulation and implementation of marketing strategies and theoretically strengthen the role of the human element. As a practical contribution, it has been shown that it is not enough to seek external knowledge, it is necessary that it is transformed and then used effectively in the design and implementation of marketing strategies. Design/method/approach: Quantitative research, with transverse temporal data collection. This study empirically tested the hypotheses based on a sample of 343 marketing managers from Brazilian manufacturing industries. Data were collected through a survey. Data were processed by means of modeling of structural equations in AMOS software. Findings: The characteristics of managers (age and tenure) moderate the relationship between a part of RACAP (knowledge transformation) and CAM (architectural marketing capability). More experienced managers should be valued because it has been proven that in this sector, they make a difference when it comes to transforming knowledge and using it in their strategies. Objetivo: Verificar o papel moderador das características dos gestores, como idade e tenure (tempo no setor, cargo, empresa), na relação entre a capacidade absortiva realizada (RACAP) e a capacidade arquitetural de marketing (CAM). Originalidade/valor: O presente estudo considera o elemento humano como fator que afeta as relações entre as capacidades da empresa. Contribui teoricamente ao auxiliar o entendimento do que pode impactar a formulação e implementação de estratégias de marketing, além de fortalecer teoricamente o papel do elemento humano. Como contribuição prática, demonstrou-se que não basta apenas buscar o conhecimento externo, mas também é necessário que ele seja transformado para então ser utilizado de maneira eficaz na elaboração e aplicação das estratégias de marketing. Design/metodologia/abordagem: Trata-se de pesquisa de caráter quantitativo, com corte temporal transversal. Este estudo testou empiricamente as hipóteses com base em uma amostra de 343 gestores de marketing de indústrias brasileiras de manufatura. Os dados foram coletados por meio de survey e tratados por meio de modelagem de equações estruturais no software AMOS. Resultados: As características dos gestores (idade e tenure) moderam a relação entre uma parte da RACAP (transformação do conhecimento) e a CAM (capacidade arquitetural de marketing). Gestores mais experientes devem ser valorizados, pois comprovou-se que, nesse setor, eles fazem a diferença na hora de transformar o conhecimento e utilizá-lo em suas estratégias.
Keywords	absorptive capacity ; marketing capability ; managers’ characteristics ; age ; capacidade absortiva ; capacidade de marketing ; características dos gestores ; idade ; Social Sciences ; H ; Commerce ; HF1-6182 ; Business ; HF5001-6182
Language	Spanish
Publishing date	2019-12-01T00:00:00Z
Publisher	Universidade Presbiteriana Mackenzie
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Expression and regulation of the neutral amino acid transporter B0AT1 in rat small intestine.

Jando, Julia / Camargo, Simone M R / Herzog, Brigitte / Verrey, François

PloS one

2017 Volume 12, Issue 9, Page(s) e0184845

Abstract: Absorption of neutral amino acids across the luminal membrane of intestinal enterocytes is mediated by the broad neutral amino acid transporter B0AT1 (SLC6A19). Its intestinal expression depends on co-expression of the membrane-anchored peptidase ... ...

Abstract	Absorption of neutral amino acids across the luminal membrane of intestinal enterocytes is mediated by the broad neutral amino acid transporter B0AT1 (SLC6A19). Its intestinal expression depends on co-expression of the membrane-anchored peptidase angiotensin converting enzyme 2 (ACE2) and is additionally enhanced by aminopeptidase N (CD13). We investigated in this study the expression of B0AT1 and its auxiliary peptidases as well as its transport function along the rat small intestine. Additionally, we tested its possible short- and long-term regulation by dietary proteins and amino acids. We showed by immunofluorescence that B0AT1, ACE2 and CD13 co-localize on the luminal membrane of small intestinal villi and by Western blotting that their protein expression increases in distal direction. Furthermore, we observed an elevated transport activity of the neutral amino acid L-isoleucine during the nocturnal active phase compared to the inactive one. Gastric emptying was delayed by intragastric application of an amino acid cocktail but we observed no acute dietary regulation of B0AT1 protein expression and L-isoleucine transport. Investigation of the chronic dietary regulation of B0AT1, ACE2 and CD13 by different diets revealed an increased B0AT1 protein expression under amino acid-supplemented diet in the proximal section but not in the distal one and for ACE2 protein expression a reverse localization of the effect. Dietary regulation for CD13 protein expression was not as distinct as for the two other proteins. Ring uptake experiments showed a tendency for increased L-isoleucine uptake under amino acid-supplemented diet and in vivo L-isoleucine absorption was more efficient under high protein and amino acid-supplemented diet. Additionally, plasma levels of branched-chain amino acids were elevated under high protein and amino acid diet. Taken together, our experiments did not reveal an acute amino acid-induced regulation of B0AT1 but revealed a chronic dietary adaptation mainly restricted to the proximal segment of the small intestine.
MeSH term(s)	Amino Acid Transport Systems, Neutral/biosynthesis ; Animals ; CD13 Antigens/metabolism ; Dietary Supplements ; Gene Expression Regulation/drug effects ; Intestine, Small/metabolism ; Isoleucine/pharmacology ; Male ; Peptidyl-Dipeptidase A/metabolism ; Rats ; Rats, Wistar
Chemical Substances	Amino Acid Transport Systems, Neutral ; SLC6A19 protein, rat ; Isoleucine (04Y7590D77) ; CD13 Antigens (EC 3.4.11.2) ; Peptidyl-Dipeptidase A (EC 3.4.15.1) ; angiotensin converting enzyme 2 (EC 3.4.17.-)
Keywords	covid19
Language	English
Publishing date	2017
Publishing country	United States
Document type	Journal Article
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0184845
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Article: Artificial feeding of Ornithodoros fonsecai (Acari: Argasidae) with the anticoagulant Alsever

Ana C. Castro-Santiago / Simone M. Simons / Leidiane Lima-Duarte / Jaqueline V. Camargo / Rosangela Z. Machado / Marco R. André / Darci M. Barros-Battesti

Entomological Communications. 2021, v. 3

2021

Abstract: Ornithodoros fonsecai is a species of argasid tick endemic to Brazil, described in the “São Miguel” cave located in the municipality of Bonito, state of Mato Grosso do Sul, central-western region of Brazil. The artificial feeding technique makes it ... ...

Abstract	Ornithodoros fonsecai is a species of argasid tick endemic to Brazil, described in the “São Miguel” cave located in the municipality of Bonito, state of Mato Grosso do Sul, central-western region of Brazil. The artificial feeding technique makes it possible to study the biology of hematophagous arthropods using artificial or natural membranes, as well as different types of blood and anticoagulants. Thus, the aim of the present study was to feed artificially O. fonsecai second instar (N2) nymphs with rabbit blood using parafilm membrane and the anticoagulant Alsever. Ninety percent of the total N2 nymphs engorged and molted to N3 nymphs between 27 and 30 days after feeding, indicating that the use of this anticoagulant is efficient for artificially feeding O. fonsecai N2 nymphs under laboratory conditions.
Keywords	Ornithodoros ; anticoagulants ; blood ; instars ; nutritional support ; rabbits ; ticks ; Brazil
Language	English
Publishing place	Sociedade Entomológica do Brasil
Document type	Article
ISSN	2675-1305
DOI	10.37486/2675-1305.ec03047
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Expression and regulation of the neutral amino acid transporter B0AT1 in rat small intestine.

Julia Jando / Simone M R Camargo / Brigitte Herzog / François Verrey

PLoS ONE, Vol 12, Iss 9, p e

2017 Volume 0184845

Abstract	Absorption of neutral amino acids across the luminal membrane of intestinal enterocytes is mediated by the broad neutral amino acid transporter B0AT1 (SLC6A19). Its intestinal expression depends on co-expression of the membrane-anchored peptidase angiotensin converting enzyme 2 (ACE2) and is additionally enhanced by aminopeptidase N (CD13). We investigated in this study the expression of B0AT1 and its auxiliary peptidases as well as its transport function along the rat small intestine. Additionally, we tested its possible short- and long-term regulation by dietary proteins and amino acids. We showed by immunofluorescence that B0AT1, ACE2 and CD13 co-localize on the luminal membrane of small intestinal villi and by Western blotting that their protein expression increases in distal direction. Furthermore, we observed an elevated transport activity of the neutral amino acid L-isoleucine during the nocturnal active phase compared to the inactive one. Gastric emptying was delayed by intragastric application of an amino acid cocktail but we observed no acute dietary regulation of B0AT1 protein expression and L-isoleucine transport. Investigation of the chronic dietary regulation of B0AT1, ACE2 and CD13 by different diets revealed an increased B0AT1 protein expression under amino acid-supplemented diet in the proximal section but not in the distal one and for ACE2 protein expression a reverse localization of the effect. Dietary regulation for CD13 protein expression was not as distinct as for the two other proteins. Ring uptake experiments showed a tendency for increased L-isoleucine uptake under amino acid-supplemented diet and in vivo L-isoleucine absorption was more efficient under high protein and amino acid-supplemented diet. Additionally, plasma levels of branched-chain amino acids were elevated under high protein and amino acid diet. Taken together, our experiments did not reveal an acute amino acid-induced regulation of B0AT1 but revealed a chronic dietary adaptation mainly restricted to the proximal segment of ...
Keywords	Medicine ; R ; Science ; Q
Language	English
Publishing date	2017-01-01T00:00:00Z
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: Artificial feeding of Ornithodoros fonsecai (Acari

Ana C. Castro-Santiago / Simone M. Simons / Leidiane Lima-Duarte / Jaqueline V. Camargo / Rosangela Z. Machado / Marco R. André / Darci M. Barros-Battesti

Entomological Communications, Vol

Argasidae) with the anticoagulant Alsever

2021 Volume 3

Abstract	Ornithodoros fonsecai is a species of argasid tick endemic to Brazil, described in the “São Miguel” cave located in the municipality of Bonito, state of Mato Grosso do Sul, central-western region of Brazil. The artificial feeding technique makes it possible to study the biology of hematophagous arthropods using artificial or natural membranes, as well as different types of blood and anticoagulants. Thus, the aim of the present study was to feed artificially O. fonsecai second instar (N2) nymphs with rabbit blood using parafilm membrane and the anticoagulant Alsever. Ninety percent of the total N2 nymphs engorged and molted to N3 nymphs between 27 and 30 days after feeding, indicating that the use of this anticoagulant is efficient for artificially feeding O. fonsecai N2 nymphs under laboratory conditions.
Keywords	argasid tick ; artificial feeding ; anticoagulant ; biology ; Zoology ; QL1-991
Language	English
Publishing date	2021-12-01T00:00:00Z
Publisher	Sociedade Entomológica do Brasil
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Collectrin and ACE2 in renal and intestinal amino acid transport.

Singer, Dustin / Camargo, Simone M R

Channels (Austin, Tex.)

2011 Volume 5, Issue 5, Page(s) 410–423

Abstract: Neutral amino acid transporters of the SLC6 family are expressed at the apical membrane of kidney and/or small intestine, where they (re-)absorb amino acids into the body. In this review we present the results concerning the dependence of their apical ... ...

Abstract	Neutral amino acid transporters of the SLC6 family are expressed at the apical membrane of kidney and/or small intestine, where they (re-)absorb amino acids into the body. In this review we present the results concerning the dependence of their apical expression with their association to partner proteins. We will in particular focus on the situation of B0AT1 and B0AT3, that associate with members of the renin-angiotensin system (RAS), namely Tmem27 and angiotensin-converting enzyme 2 (ACE2), in a tissue specific manner. The role of this association in relation to the formation of a functional unit related to Na+ or amino acid transport will be assessed. We will conclude with some remarks concerning the relevance of this association to Hartnup disorder, where some mutations have been shown to differentially interact with the partner proteins.
MeSH term(s)	Amino Acid Transport Systems, Neutral/genetics ; Amino Acid Transport Systems, Neutral/metabolism ; Amino Acids/genetics ; Amino Acids/metabolism ; Animals ; Biological Transport/physiology ; Hartnup Disease/genetics ; Hartnup Disease/metabolism ; Humans ; Intestine, Small/metabolism ; Kidney/metabolism ; Membrane Glycoproteins/genetics ; Membrane Glycoproteins/metabolism ; Mice ; Organ Specificity/physiology ; Peptidyl-Dipeptidase A/genetics ; Peptidyl-Dipeptidase A/metabolism ; Renin-Angiotensin System/physiology ; Sodium/metabolism
Chemical Substances	Amino Acid Transport Systems, Neutral ; Amino Acids ; CLTRN protein, human ; Membrane Glycoproteins ; SLC6A19 protein, human ; SLC6A19 protein, mouse ; Tmem27 protein, mouse ; Sodium (9NEZ333N27) ; Peptidyl-Dipeptidase A (EC 3.4.15.1) ; angiotensin converting enzyme 2 (EC 3.4.17.-)
Keywords	covid19
Language	English
Publishing date	2011-09-01
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2262854-X
ISSN	1933-6969 ; 1933-6950
ISSN (online)	1933-6969
ISSN	1933-6950
DOI	10.4161/chan.5.5.16470
Database	MEDical Literature Analysis and Retrieval System OnLINE

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