Search

Your search keyword '"Gomas, Emmanuel"' showing total 13 results
Start Over Author "Gomas, Emmanuel"
13 results on '"Gomas, Emmanuel"'

1. Essential Role of Chicken Ovalbumin Upstream Promoter-Transcription Factor II in Insulin Secretion and Insulin Sensitivity Revealed by Conditional Gene Knockout

Author

Bardoux, Pascale, Zhang, Pili, Flamez, Daisy, Perilhou, Anaïs, Lavin, Tiphaine Aguirre, Tanti, Jean-François, Hellemans, Karine, Gomas, Emmanuel, Godard, Cécile, Andreelli, Fabrizio, Buccheri, Maria Antonietta, Kahn, Axel, Le Marchand-Brustel, Yannick, Burcelin, Rémy, Schuit, Frans, and Vasseur-Cognet, Mireille

Published
2005

2. The AMP-activated protein kinase α2 catalytic subunit controls whole-body insulin sensitivity

Author

Viollet, Benoit, Andreelli, Fabrizio, Jørgensen, Sebastian B., Perrin, Christophe, Geloen, Alain, Flamez, Daisy, Mu, James, Lenzner, Claudia, Baud, Olivier, Bennoun, Myriam, Gomas, Emmanuel, Nicolas, Gaël, Wojtaszewski, Jørgen F.P., Kahn, Axel, Carling, David, Schuit, Frans C., Birnbaum, Morris J., Richter, Erik A., Burcelin, Rémy, and Vaulont, Sophie

Published
2003

3. (Cryo)preserving your research: Bringing welfare, logistical and cost benefits to modern preclinical drug development studies

Author

Gomas, Emmanuel

Subjects
Cryopreservation -- Research -- Methods, Drugs -- Research, Textiles, Retirement benefits, Animal genetic engineering, Insurance, Business, Chemicals, plastics and rubber industries, Engineering and manufacturing industries, Business, international
Abstract

Maintaining the integrity of research and obtaining reliable, repeatable data depends on the stability of a research model. Given the cost and complexity of managing model breeding, cryopreservation is often [...]

Published
2019

4. The AMP-activated protein kinase alpha 2 catalytic subunit controls whole-body insulin sensitivity

Author

Viollet, Benoit, Andreelli, Fabrizio, Jorgensen, Sebastian B, Perrin, Christophe, Geloen, Alain, Flamez, Daisy, Mu, James, Lenzner, Claudia, Baud, Olivier, Bennoun, Myriam, Gomas, Emmanuel, Nicolas, Gaël, Wojtaszewski, Jorgen FP, Kahn, Axel, Carling, David, Schuit, Frans C, Birnbaum, Morris J, Richter, Erik A, Burcelin, Rémy, and Vaulont, Sophie

Subjects
GLUCOSE-UTILIZATION, LEPTIN, CONTRACTION, INFUSION, INHIBITION, Biology and Life Sciences, PANCREATIC BETA-CELLS, ACETYL-COA CARBOXYLASE, RAT SKELETAL-MUSCLE, METABOLISM, TRANSPORT
Abstract

AMP-activated protein kinase (AMPK) is viewed as a fuel sensor for glucose and lipid metabolism. To better understand the physiological role of AMPK, we generated a knockout mouse model in which the AMPKalpha2 catalytic subunit gene was inactivated. AMPKalpha2(-/-) mice presented high glucose levels in the fed period and during an oral glucose challenge associated with low insulin plasma levels. However, in isolated AMPKalpha2(-/-) pancreatic islets, glucose- and L-arginine-stimulated insulin secretion were not affected. AMPKalpha2(-/-) mice have reduced insulin-stimulated whole-body glucose utilization and muscle glycogen synthesis rates assessed in vivo by the hyperinsulinemic euglycemic clamp technique. Surprisingly, both parameters were not altered in mice expressing a dominant-negative mutant of AMPK in skeletal muscle. Furthermore, glucose transport was normal in incubated isolated AMPKalpha2(-/-) muscles. These data indicate that AMPKalpha2 in tissues other than skeletal muscles regulates insulin action. Concordantly, we found an increased daily urinary catecholamine excretion in AMPKalpha2(-/-) mice, suggesting altered function of the autonomic nervous system that could explain both the impaired insulin secretion and insulin sensitivity observed in vivo. Therefore, extramuscular AMPKalpha2 catalytic subunit is important for whole-body insulin action in vivo, probably through modulation of sympathetic nervous activity.

Published
2003

5. The AMP-activated protein kinase alpha2 catalytic subunit controls whole-body insulin sensitivity

Author

Viollet, Benoit, Andreelli, Fabrizio, Jørgensen, Sebastian B., Perrin, Christophe, Geloen, Alain, Flamez, Daisy, Mu, James, Lenzner, Claudia, Baud, Olivier, Bennoun, Myriam, Gomas, Emmanuel, Nicolas, Gaël, Wojtaszewski, Jørgen, Kahn, Axel, Carling, David, Schuit, Frans C., Birnbaum, Morris J., Richter, Erik A., Burcelin, Rémy, Vaulont, Sophie, Viollet, Benoit, Andreelli, Fabrizio, Jørgensen, Sebastian B., Perrin, Christophe, Geloen, Alain, Flamez, Daisy, Mu, James, Lenzner, Claudia, Baud, Olivier, Bennoun, Myriam, Gomas, Emmanuel, Nicolas, Gaël, Wojtaszewski, Jørgen, Kahn, Axel, Carling, David, Schuit, Frans C., Birnbaum, Morris J., Richter, Erik A., Burcelin, Rémy, and Vaulont, Sophie

Published
2003

12. The AMP-activated protein kinase α2 catalytic subunit controls whole-body insulin sensitivity.

Author

Violett, Benoit, Andreelli, Fabrizio, Jorgensen, Sebastian B., Perrin, Christophe, Geloen, Alain, Flamez, Daisy, Mu, James, Lenzner, Claudia, Baud, Olivier, Bennoun, Myriam, Gomas, Emmanuel, Nicolas, Gael, Wojtaszewski, Jorgen F.P., Kahn, Axel, Carling, David, Schuit, Frans C., Birnbaum, Morris J., Richter, Erik A., and Burcelin, Remy

Subjects
*PROTEIN kinases, *PHYSIOLOGY
Abstract

Offers information on a study which investigated the physiological role of adenosine monophosphate-activated protein kinase Methods; Results; Discussion.

Published
2003
Full Text
View/download PDF

13. The AMP-activated protein kinase alpha2 catalytic subunit controls whole-body insulin sensitivity.

Author

Viollet B, Andreelli F, Jørgensen SB, Perrin C, Geloen A, Flamez D, Mu J, Lenzner C, Baud O, Bennoun M, Gomas E, Nicolas G, Wojtaszewski JF, Kahn A, Carling D, Schuit FC, Birnbaum MJ, Richter EA, Burcelin R, and Vaulont S

Subjects
AMP-Activated Protein Kinases, Alleles, Animals, Biological Transport, Blotting, Southern, Body Weight, Catalytic Domain, Dose-Response Relationship, Drug, Genotype, Glucose pharmacology, Glucose Tolerance Test, Glycogen metabolism, Insulin pharmacology, Liver metabolism, Mice, Mice, Inbred C57BL, Mice, Knockout, Muscle, Skeletal cytology, Muscle, Skeletal metabolism, Muscles metabolism, Protein Structure, Tertiary, Time Factors, Insulin metabolism, Multienzyme Complexes chemistry, Multienzyme Complexes metabolism, Protein Serine-Threonine Kinases chemistry, Protein Serine-Threonine Kinases metabolism
Abstract

AMP-activated protein kinase (AMPK) is viewed as a fuel sensor for glucose and lipid metabolism. To better understand the physiological role of AMPK, we generated a knockout mouse model in which the AMPKalpha2 catalytic subunit gene was inactivated. AMPKalpha2(-/-) mice presented high glucose levels in the fed period and during an oral glucose challenge associated with low insulin plasma levels. However, in isolated AMPKalpha2(-/-) pancreatic islets, glucose- and L-arginine-stimulated insulin secretion were not affected. AMPKalpha2(-/-) mice have reduced insulin-stimulated whole-body glucose utilization and muscle glycogen synthesis rates assessed in vivo by the hyperinsulinemic euglycemic clamp technique. Surprisingly, both parameters were not altered in mice expressing a dominant-negative mutant of AMPK in skeletal muscle. Furthermore, glucose transport was normal in incubated isolated AMPKalpha2(-/-) muscles. These data indicate that AMPKalpha2 in tissues other than skeletal muscles regulates insulin action. Concordantly, we found an increased daily urinary catecholamine excretion in AMPKalpha2(-/-) mice, suggesting altered function of the autonomic nervous system that could explain both the impaired insulin secretion and insulin sensitivity observed in vivo. Therefore, extramuscular AMPKalpha2 catalytic subunit is important for whole-body insulin action in vivo, probably through modulation of sympathetic nervous activity.

Published
2003
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results