LIVIVO - Search results -

Search results

Result 1 - 10 of total 24

Search options

Article ; Online: Genomic imprinting-an epigenetic gene-regulatory model.

Koerner, Martha V / Barlow, Denise P

Current opinion in genetics & development

2010 Volume 20, Issue 2, Page(s) 164–170

Abstract: Epigenetic mechanisms (Box 1) are considered to play major gene-regulatory roles in development, differentiation and disease. However, the relative importance of epigenetics in defining the mammalian transcriptome in normal and disease states is unknown. ...

Abstract	Epigenetic mechanisms (Box 1) are considered to play major gene-regulatory roles in development, differentiation and disease. However, the relative importance of epigenetics in defining the mammalian transcriptome in normal and disease states is unknown. The mammalian genome contains only a few model systems where epigenetic gene regulation has been shown to play a major role in transcriptional control. These model systems are important not only to investigate the biological function of known epigenetic modifications but also to identify new and unexpected epigenetic mechanisms in the mammalian genome. Here we review recent progress in understanding how epigenetic mechanisms control imprinted gene expression.
MeSH term(s)	Animals ; Epigenesis, Genetic/genetics ; Female ; Gene Expression Regulation, Developmental ; Genomic Imprinting ; Germ Cells/metabolism ; Humans ; Male ; Models, Genetic
Language	English
Publishing date	2010-02-12
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1077312-5
ISSN	1879-0380 ; 0959-437X
ISSN (online)	1879-0380
ISSN	0959-437X
DOI	10.1016/j.gde.2010.01.009
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 3240: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (2.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Neuronal non-CG methylation is an essential target for MeCP2 function.

Tillotson, Rebekah / Cholewa-Waclaw, Justyna / Chhatbar, Kashyap / Connelly, John C / Kirschner, Sophie A / Webb, Shaun / Koerner, Martha V / Selfridge, Jim / Kelly, David A / De Sousa, Dina / Brown, Kyla / Lyst, Matthew J / Kriaucionis, Skirmantas / Bird, Adrian

Molecular cell

2021 Volume 81, Issue 6, Page(s) 1260–1275.e12

Abstract: DNA methylation is implicated in neuronal biology via the protein MeCP2, the mutation of which causes Rett syndrome. MeCP2 recruits the NCOR1/2 co-repressor complexes to methylated cytosine in the CG dinucleotide, but also to sites of non-CG methylation, ...

Abstract	DNA methylation is implicated in neuronal biology via the protein MeCP2, the mutation of which causes Rett syndrome. MeCP2 recruits the NCOR1/2 co-repressor complexes to methylated cytosine in the CG dinucleotide, but also to sites of non-CG methylation, which are abundant in neurons. To test the biological significance of the dual-binding specificity of MeCP2, we replaced its DNA binding domain with an orthologous domain from MBD2, which can only bind mCG motifs. Knockin mice expressing the domain-swap protein displayed severe Rett-syndrome-like phenotypes, indicating that normal brain function requires the interaction of MeCP2 with sites of non-CG methylation, specifically mCAC. The results support the notion that the delayed onset of Rett syndrome is due to the simultaneous post-natal accumulation of mCAC and its reader MeCP2. Intriguingly, genes dysregulated in both Mecp2 null and domain-swap mice are implicated in other neurological disorders, potentially highlighting targets of relevance to the Rett syndrome phenotype.
MeSH term(s)	Animals ; CpG Islands ; DNA Methylation ; Gene Knock-In Techniques ; HeLa Cells ; Humans ; Male ; Methyl-CpG-Binding Protein 2/genetics ; Methyl-CpG-Binding Protein 2/metabolism ; Mice ; Mice, Transgenic ; Mutation ; NIH 3T3 Cells ; Neurons/metabolism ; Neurons/pathology ; Protein Domains ; Rett Syndrome/genetics ; Rett Syndrome/metabolism ; Rett Syndrome/pathology
Chemical Substances	Mecp2 protein, mouse ; Methyl-CpG-Binding Protein 2
Language	English
Publishing date	2021-02-08
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1415236-8
ISSN	1097-4164 ; 1097-2765
ISSN (online)	1097-4164
ISSN	1097-2765
DOI	10.1016/j.molcel.2021.01.011
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 5055: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (2.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Affinity for DNA Contributes to NLS Independent Nuclear Localization of MeCP2.

Lyst, Matthew J / Ekiert, Robert / Guy, Jacky / Selfridge, Jim / Koerner, Martha V / Merusi, Cara / De Sousa, Dina / Bird, Adrian

Cell reports

2018 Volume 24, Issue 9, Page(s) 2213–2220

Abstract: MeCP2 is a nuclear protein that is mutated in the severe neurological disorder Rett syndrome (RTT). The ability to target β-galactosidase to the nucleus was previously used to identify a conserved nuclear localization signal (NLS) in MeCP2 that interacts ...

Abstract	MeCP2 is a nuclear protein that is mutated in the severe neurological disorder Rett syndrome (RTT). The ability to target β-galactosidase to the nucleus was previously used to identify a conserved nuclear localization signal (NLS) in MeCP2 that interacts with the nuclear import factors KPNA3 and KPNA4. Here, we report that nuclear localization of MeCP2 does not depend on its NLS. Instead, our data reveal that an intact methyl-CpG binding domain (MBD) is sufficient for nuclear localization, suggesting that MeCP2 can be retained in the nucleus by its affinity for DNA. Consistent with these findings, we demonstrate that disease progression in a mouse model of RTT is unaffected by an inactivating mutation in the NLS of MeCP2. Taken together, our work reveals an unexpected redundancy between functional domains of MeCP2 in targeting this protein to the nucleus, potentially explaining why NLS-inactivating mutations are rarely associated with disease.
MeSH term(s)	Animals ; Cell Line, Tumor ; Cell Nucleus/metabolism ; CpG Islands ; DNA/genetics ; DNA/metabolism ; Disease Models, Animal ; Male ; Methyl-CpG-Binding Protein 2/genetics ; Methyl-CpG-Binding Protein 2/metabolism ; Mice ; Mice, Inbred C57BL ; NIH 3T3 Cells ; Nuclear Localization Signals/metabolism ; Rett Syndrome/metabolism ; alpha Karyopherins/metabolism
Chemical Substances	Mecp2 protein, mouse ; Methyl-CpG-Binding Protein 2 ; Nuclear Localization Signals ; alpha Karyopherins ; DNA (9007-49-2)
Language	English
Publishing date	2018-04-11
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2018.07.099
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: A mutation-led search for novel functional domains in MeCP2.

Guy, Jacky / Alexander-Howden, Beatrice / FitzPatrick, Laura / DeSousa, Dina / Koerner, Martha V / Selfridge, Jim / Bird, Adrian

Human molecular genetics

2018 Volume 27, Issue 14, Page(s) 2531–2545

Abstract: Most missense mutations causing Rett syndrome (RTT) affect domains of MeCP2 that have been shown to either bind methylated DNA or interact with a transcriptional co-repressor complex. Several mutations, however, including the C-terminal truncations that ... ...

Abstract	Most missense mutations causing Rett syndrome (RTT) affect domains of MeCP2 that have been shown to either bind methylated DNA or interact with a transcriptional co-repressor complex. Several mutations, however, including the C-terminal truncations that account for ∼10% of cases, fall outside these characterized domains. We studied the molecular consequences of four of these 'non-canonical' mutations in cultured neurons and mice to see if they reveal additional essential domains without affecting known properties of MeCP2. The results show that the mutations partially or strongly deplete the protein and also in some cases interfere with co-repressor recruitment. These mutations therefore impact the activity of known functional domains and do not invoke new molecular causes of RTT. The finding that a stable C-terminal truncation does not compromise MeCP2 function raises the possibility that small molecules which stabilize these mutant proteins may be of therapeutic value.
MeSH term(s)	Animals ; Chromosomal Proteins, Non-Histone/genetics ; DNA Methylation/genetics ; Disease Models, Animal ; Female ; Humans ; Methyl-CpG-Binding Protein 2/genetics ; Mice ; Mutation, Missense/genetics ; Neurons/pathology ; Repressor Proteins/genetics ; Rett Syndrome/genetics ; Rett Syndrome/pathology
Chemical Substances	Chromosomal Proteins, Non-Histone ; MECP2 protein, human ; Mecp2 protein, mouse ; Methyl-CpG-Binding Protein 2 ; Repressor Proteins
Language	English
Publishing date	2018-04-09
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1108742-0
ISSN	1460-2083 ; 0964-6906
ISSN (online)	1460-2083
ISSN	0964-6906
DOI	10.1093/hmg/ddy159
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 3469: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (2.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: An Orphan CpG Island Drives Expression of a

Koerner, Martha V / Chhatbar, Kashyap / Webb, Shaun / Cholewa-Waclaw, Justyna / Selfridge, Jim / De Sousa, Dina / Skarnes, Bill / Rosen, Barry / Thomas, Mark / Bottomley, Joanna / Ramires-Solis, Ramiro / Lelliott, Christopher / Adams, David J / Bird, Adrian

Epigenomes

2019 Volume 3, Issue 1, Page(s) 7

Abstract: Most human genes are associated with promoters embedded in non-methylated, G + C-rich CpG islands (CGIs). Not all CGIs are found at annotated promoters, however, raising the possibility that many serve as promoters for transcripts that do not code for ... ...

Abstract	Most human genes are associated with promoters embedded in non-methylated, G + C-rich CpG islands (CGIs). Not all CGIs are found at annotated promoters, however, raising the possibility that many serve as promoters for transcripts that do not code for proteins. To test this hypothesis, we searched for novel transcripts in embryonic stem cells (ESCs) that originate within orphan CGIs. Among several candidates, we detected a transcript that included three members of the
Language	English
Publishing date	2019-03-13
Publishing country	Switzerland
Document type	Journal Article
ISSN	2075-4655
ISSN (online)	2075-4655
DOI	10.3390/epigenomes3010007
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article: Neuronal non-CG methylation is an essential target for MeCP2 function

Molecular cell. 2021 Mar. 18, v. 81, no. 6

2021

Abstract	DNA methylation is implicated in neuronal biology via the protein MeCP2, the mutation of which causes Rett syndrome. MeCP2 recruits the NCOR1/2 co-repressor complexes to methylated cytosine in the CG dinucleotide, but also to sites of non-CG methylation, which are abundant in neurons. To test the biological significance of the dual-binding specificity of MeCP2, we replaced its DNA binding domain with an orthologous domain from MBD2, which can only bind mCG motifs. Knockin mice expressing the domain-swap protein displayed severe Rett-syndrome-like phenotypes, indicating that normal brain function requires the interaction of MeCP2 with sites of non-CG methylation, specifically mCAC. The results support the notion that the delayed onset of Rett syndrome is due to the simultaneous post-natal accumulation of mCAC and its reader MeCP2. Intriguingly, genes dysregulated in both Mecp2 null and domain-swap mice are implicated in other neurological disorders, potentially highlighting targets of relevance to the Rett syndrome phenotype.
Keywords	DNA ; DNA methylation ; brain ; cytosine ; mutation ; neurons ; phenotype
Language	English
Dates of publication	2021-0318
Size	p. 1260-1275.e12.
Publishing place	Elsevier Inc.
Document type	Article
Note	NAL-AP-2-clean
ZDB-ID	1415236-8
ISSN	1097-4164 ; 1097-2765
ISSN (online)	1097-4164
ISSN	1097-2765
DOI	10.1016/j.molcel.2021.01.011
Database	NAL-Catalogue (AGRICOLA)

In stock of ZB MED Bonn / Germany

Z 2005/501: Show issues

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Details ▾
- See ZB MED holdings
- Order with fees

Article: An Orphan CpG Island Drives Expression of a <i>let-7</i> miRNA Precursor with an Important Role in Mouse Development

Koerner, Martha V / Chhatbar, Kashyap / Webb, Shaun / Cholewa-Waclaw, Justyna / Selfridge, Jim / De Sousa, Dina / Skarnes, Bill / Rosen, Barry / Thomas, Mark / Bottomley, Joanna / Ramirez-Solis, Ramiro / Lelliott, Christopher / Adams, David J / Bird, Adrian

Epigenomes. 2019 Mar. 13, v. 3, no. 1

2019

Abstract	Most human genes are associated with promoters embedded in non-methylated, G + C-rich CpG islands (CGIs). Not all CGIs are found at annotated promoters, however, raising the possibility that many serve as promoters for transcripts that do not code for proteins. To test this hypothesis, we searched for novel transcripts in embryonic stem cells (ESCs) that originate within orphan CGIs. Among several candidates, we detected a transcript that included three members of the let-7 micro-RNA family: Let-7a-1, let-7f-1, and let-7d. Deletion of the CGI prevented expression of the precursor RNA and depleted the included miRNAs. Mice homozygous for this mutation were sub-viable and showed growth and other defects. The results suggest that despite the identity of their seed sequences, members of the let-7 miRNA family exert distinct functions that cannot be complemented by other members.
Keywords	genomic islands ; homozygosity ; humans ; mice ; microRNA ; mutation
Language	English
Dates of publication	2019-0313
Publishing place	Multidisciplinary Digital Publishing Institute
Document type	Article
Note	NAL-AP-2-clean
ISSN	2075-4655
DOI	10.3390/epigenomes3010007
Database	NAL-Catalogue (AGRICOLA)

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article ; Online: Toxicity of overexpressed MeCP2 is independent of HDAC3 activity.

Koerner, Martha V / FitzPatrick, Laura / Selfridge, Jim / Guy, Jacky / De Sousa, Dina / Tillotson, Rebekah / Kerr, Alastair / Sun, Zheng / Lazar, Mitchell A / Lyst, Matthew J / Bird, Adrian

Genes & development

2018 Volume 32, Issue 23-24, Page(s) 1514–1524

Abstract: Duplication of the X- ... ...

Abstract	Duplication of the X-linked
MeSH term(s)	Animals ; Co-Repressor Proteins/metabolism ; Disease Models, Animal ; Enzyme Activation/genetics ; Gene Expression ; Gene Knockout Techniques ; Histone Deacetylases/genetics ; Histone Deacetylases/metabolism ; Male ; Mental Retardation, X-Linked/genetics ; Mental Retardation, X-Linked/physiopathology ; Methyl-CpG-Binding Protein 2/genetics ; Methyl-CpG-Binding Protein 2/toxicity ; Mice ; Mutation ; Nervous System Diseases/genetics ; Neuroglia/metabolism ; Neurons/metabolism ; Nuclear Receptor Co-Repressor 1/metabolism ; Nuclear Receptor Co-Repressor 2/metabolism ; Protein Domains ; tau Proteins/metabolism
Chemical Substances	Co-Repressor Proteins ; Mapt protein, mouse ; Mecp2 protein, mouse ; Methyl-CpG-Binding Protein 2 ; Ncor1 protein, mouse ; Ncor2 protein, mouse ; Nuclear Receptor Co-Repressor 1 ; Nuclear Receptor Co-Repressor 2 ; tau Proteins ; Histone Deacetylases (EC 3.5.1.98) ; histone deacetylase 3 (EC 3.5.1.98)
Language	English
Publishing date	2018-11-21
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	806684-x
ISSN	1549-5477 ; 0890-9369
ISSN (online)	1549-5477
ISSN	0890-9369
DOI	10.1101/gad.320325.118
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 2292: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 54: Show issues

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Carbonyl reductase 1 amplifies glucocorticoid action in adipose tissue and impairs glucose tolerance in lean mice.

Bell, Rachel M B / Villalobos, Elisa / Nixon, Mark / Miguelez-Crespo, Allende / Murphy, Lee / Fawkes, Angie / Coutts, Audrey / Sharp, Matthew G F / Koerner, Martha V / Allan, Emma / Meijer, Onno C / Houtman, Renè / Odermatt, Alex / Beck, Katharina R / Denham, Scott G / Lee, Patricia / Homer, Natalie Z M / Walker, Brian R / Morgan, Ruth A

Molecular metabolism

2021 Volume 48, Page(s) 101225

Abstract: Objective: Carbonyl reductase 1 (Cbr1), a recently discovered contributor to tissue glucocorticoid metabolism converting corticosterone to 20β-dihydrocorticosterone (20β-DHB), is upregulated in adipose tissue of obese humans and mice and may contribute ... ...

Abstract	Objective: Carbonyl reductase 1 (Cbr1), a recently discovered contributor to tissue glucocorticoid metabolism converting corticosterone to 20β-dihydrocorticosterone (20β-DHB), is upregulated in adipose tissue of obese humans and mice and may contribute to cardiometabolic complications of obesity. This study tested the hypothesis that Cbr1-mediated glucocorticoid metabolism influences glucocorticoid and mineralocorticoid receptor activation in adipose tissue and impacts glucose homeostasis in lean and obese states. Methods: The actions of 20β-DHB on corticosteroid receptors in adipose tissue were investigated first using a combination of in silico, in vitro, and transcriptomic techniques and then in vivo administration in combination with receptor antagonists. Mice lacking one Cbr1 allele and mice overexpressing Cbr1 in their adipose tissue underwent metabolic phenotyping before and after induction of obesity with high-fat feeding. Results: 20β-DHB activated both the glucocorticoid and mineralocorticoid receptor in adipose tissue and systemic administration to wild-type mice induced glucose intolerance, an effect that was ameliorated by both glucocorticoid and mineralocorticoid receptor antagonism. Cbr1 haploinsufficient lean male mice had lower fasting glucose and improved glucose tolerance compared with littermate controls, a difference that was abolished by administration of 20β-DHB and absent in female mice with higher baseline adipose 20β-DHB concentrations than male mice. Conversely, overexpression of Cbr1 in adipose tissue resulted in worsened glucose tolerance and higher fasting glucose in lean male and female mice. However, neither Cbr1 haploinsfficiency nor adipose overexpression affected glucose dyshomeostasis induced by high-fat feeding. Conclusions: Carbonyl reductase 1 is a novel regulator of glucocorticoid and mineralocorticoid receptor activation in adipose tissue that influences glucose homeostasis in lean mice.
MeSH term(s)	Adipose Tissue/metabolism ; Alcohol Oxidoreductases/genetics ; Alcohol Oxidoreductases/metabolism ; Animals ; Corticosterone/analogs & derivatives ; Corticosterone/blood ; Corticosterone/pharmacology ; Diet, High-Fat/adverse effects ; Disease Models, Animal ; Female ; Gene Knockdown Techniques ; Glucocorticoids/metabolism ; Glucose/metabolism ; Glucose Intolerance/genetics ; Glucose Intolerance/metabolism ; HEK293 Cells ; Homeostasis/genetics ; Humans ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Transgenic ; Obesity/genetics ; Obesity/metabolism ; Receptors, Glucocorticoid/metabolism ; Receptors, Mineralocorticoid/metabolism ; Signal Transduction/drug effects ; Signal Transduction/genetics
Chemical Substances	Glucocorticoids ; NR3C2 protein, human ; Receptors, Glucocorticoid ; Receptors, Mineralocorticoid ; 20-dihydrocorticosterone (35531-74-9) ; Alcohol Oxidoreductases (EC 1.1.-) ; carbonyl reductase 1, mouse (EC 1.1.-) ; Glucose (IY9XDZ35W2) ; Corticosterone (W980KJ009P)
Language	English
Publishing date	2021-03-27
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2708735-9
ISSN	2212-8778 ; 2212-8778
ISSN (online)	2212-8778
ISSN	2212-8778
DOI	10.1016/j.molmet.2021.101225
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Carbonyl reductase 1 amplifies glucocorticoid action in adipose tissue and impairs glucose tolerance in lean mice

Rachel M.B. Bell / Elisa Villalobos / Mark Nixon / Allende Miguelez-Crespo / Lee Murphy / Angie Fawkes / Audrey Coutts / Matthew G.F. Sharp / Martha V. Koerner / Emma Allan / Onno C. Meijer / Renè Houtman / Alex Odermatt / Katharina R. Beck / Scott G. Denham / Patricia Lee / Natalie Z.M. Homer / Brian R. Walker / Ruth A. Morgan

Molecular Metabolism, Vol 48, Iss , Pp 101225- (2021)

2021

Abstract	Objective: Carbonyl reductase 1 (Cbr1), a recently discovered contributor to tissue glucocorticoid metabolism converting corticosterone to 20β-dihydrocorticosterone (20β-DHB), is upregulated in adipose tissue of obese humans and mice and may contribute to cardiometabolic complications of obesity. This study tested the hypothesis that Cbr1-mediated glucocorticoid metabolism influences glucocorticoid and mineralocorticoid receptor activation in adipose tissue and impacts glucose homeostasis in lean and obese states. Methods: The actions of 20β-DHB on corticosteroid receptors in adipose tissue were investigated first using a combination of in silico, in vitro, and transcriptomic techniques and then in vivo administration in combination with receptor antagonists. Mice lacking one Cbr1 allele and mice overexpressing Cbr1 in their adipose tissue underwent metabolic phenotyping before and after induction of obesity with high-fat feeding. Results: 20β-DHB activated both the glucocorticoid and mineralocorticoid receptor in adipose tissue and systemic administration to wild-type mice induced glucose intolerance, an effect that was ameliorated by both glucocorticoid and mineralocorticoid receptor antagonism. Cbr1 haploinsufficient lean male mice had lower fasting glucose and improved glucose tolerance compared with littermate controls, a difference that was abolished by administration of 20β-DHB and absent in female mice with higher baseline adipose 20β-DHB concentrations than male mice. Conversely, overexpression of Cbr1 in adipose tissue resulted in worsened glucose tolerance and higher fasting glucose in lean male and female mice. However, neither Cbr1 haploinsfficiency nor adipose overexpression affected glucose dyshomeostasis induced by high-fat feeding. Conclusions: Carbonyl reductase 1 is a novel regulator of glucocorticoid and mineralocorticoid receptor activation in adipose tissue that influences glucose homeostasis in lean mice.
Keywords	Obesity ; Glucocorticoid ; Metabolism ; Glucose ; Corticosterone ; Mineralocorticoid receptor ; Internal medicine ; RC31-1245
Subject code	670
Language	English
Publishing date	2021-06-01T00:00:00Z
Publisher	Elsevier
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

Full text online

Full text

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

To top

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

In stock of ZB MED Bonn / Germany

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

Full text online

More links

Kategorien

Inter-library loan at ZB MED