Insulin-stimulated glucose uptake partly relies on p21-activated kinase (PAK)2, but not PAK1, in mouse skeletal muscle.


Journal

The Journal of physiology
ISSN: 1469-7793
Titre abrégé: J Physiol
Pays: England
ID NLM: 0266262

Informations de publication

Date de publication:
12 2020
Historique:
received: 08 06 2020
accepted: 24 08 2020
pubmed: 28 8 2020
medline: 2 3 2021
entrez: 27 8 2020
Statut: ppublish

Résumé

Muscle-specific genetic ablation of p21-activated kinase (PAK)2, but not whole-body PAK1 knockout, impairs glucose tolerance in mice. Insulin-stimulated glucose uptake partly relies on PAK2 in glycolytic extensor digitorum longus muscle By contrast to previous reports, PAK1 is dispensable for insulin-stimulated glucose uptake in mouse muscle. The group I p21-activated kinase (PAK) isoforms PAK1 and PAK2 are activated in response to insulin in skeletal muscle and PAK1/2 signalling is impaired in insulin-resistant mouse and human skeletal muscle. Interestingly, PAK1 has been suggested to be required for insulin-stimulated glucose transporter 4 translocation in mouse skeletal muscle. Therefore, the present study aimed to examine the role of PAK1 in insulin-stimulated muscle glucose uptake. The pharmacological inhibitor of group I PAKs, IPA-3 partially reduced (-20%) insulin-stimulated glucose uptake in isolated mouse soleus muscle (P < 0.001). However, because there was no phenotype with genetic ablation of PAK1 alone, consequently, the relative requirement for PAK1 and PAK2 in whole-body glucose homeostasis and insulin-stimulated muscle glucose uptake was investigated. Whole-body respiratory exchange ratio was largely unaffected in whole-body PAK1 knockout (KO), muscle-specific PAK2 KO and in mice with combined whole-body PAK1 KO and muscle-specific PAK2 KO. By contrast, glucose tolerance was mildly impaired in mice lacking PAK2 specifically in muscle, but not PAK1 KO mice. Moreover, while PAK1 KO muscles displayed normal insulin-stimulated glucose uptake in vivo and in isolated muscle, insulin-stimulated glucose uptake was slightly reduced in isolated glycolytic extensor digitorum longus muscle lacking PAK2 alone (-18%) or in combination with PAK1 KO (-12%) (P < 0.05). In conclusion, glucose tolerance and insulin-stimulated glucose uptake partly rely on PAK2 in glycolytic mouse muscle, whereas PAK1 is dispensable for whole-body glucose homeostasis and insulin-stimulated muscle glucose uptake.

Identifiants

pubmed: 32844438
doi: 10.1113/JP280294
pmc: PMC7771197
mid: NIHMS1649808
doi:

Substances chimiques

Insulin 0
p21-Activated Kinases EC 2.7.11.1
Glucose IY9XDZ35W2

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

5351-5377

Subventions

Organisme : NIAMS NIH HHS
ID : R01 AR046207
Pays : United States
Organisme : The Danish Council for Independent Research, Medical Sciences
ID : 6108-00203
Organisme : NIAMS NIH HHS
ID : R01 AR070231
Pays : United States
Organisme : NIAMS NIH HHS
ID : AR070231
Pays : United States
Organisme : NIAMS NIH HHS
ID : AR046207
Pays : United States
Organisme : The Danish Council for Independent Research, Medical Sciences
ID : DFF-4004-00233
Organisme : Danish Diabetes Academy (funded by The Novo Nordisk Foundation)
ID : NNF17SA0031406

Informations de copyright

© 2020 The Authors. The Journal of Physiology © 2020 The Physiological Society.

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Auteurs

Lisbeth L V Møller (LLV)

Section of Molecular Physiology, Department of Nutrition, Exercise and Sports, Faculty of Science, University of Copenhagen, Copenhagen, Denmark.

Merna Jaurji (M)

Section of Molecular Physiology, Department of Nutrition, Exercise and Sports, Faculty of Science, University of Copenhagen, Copenhagen, Denmark.

Rasmus Kjøbsted (R)

Section of Molecular Physiology, Department of Nutrition, Exercise and Sports, Faculty of Science, University of Copenhagen, Copenhagen, Denmark.

Giselle A Joseph (GA)

Department of Cell, Developmental, and Regenerative Biology, Icahn School of Medicine at Mount Sinai, NY, USA.

Agnete B Madsen (AB)

Section of Molecular Physiology, Department of Nutrition, Exercise and Sports, Faculty of Science, University of Copenhagen, Copenhagen, Denmark.

Jonas R Knudsen (JR)

Section of Molecular Physiology, Department of Nutrition, Exercise and Sports, Faculty of Science, University of Copenhagen, Copenhagen, Denmark.
Microsystems Laboratory 2, Institute of Microengineering, École Polytechnique Fédérale de Lausanne, Lausanne, Switzerland.

Anne-Marie Lundsgaard (AM)

Section of Molecular Physiology, Department of Nutrition, Exercise and Sports, Faculty of Science, University of Copenhagen, Copenhagen, Denmark.

Nicoline R Andersen (NR)

Section of Molecular Physiology, Department of Nutrition, Exercise and Sports, Faculty of Science, University of Copenhagen, Copenhagen, Denmark.

Peter Schjerling (P)

Institute of Sports Medicine, Department of Orthopaedic Surgery M, Bispebjerg Hospital, Copenhagen, Denmark.
Center for Healthy Aging, Faculty of Health Sciences, University of Copenhagen, Copenhagen, Denmark.

Thomas E Jensen (TE)

Section of Molecular Physiology, Department of Nutrition, Exercise and Sports, Faculty of Science, University of Copenhagen, Copenhagen, Denmark.

Robert S Krauss (RS)

Department of Cell, Developmental, and Regenerative Biology, Icahn School of Medicine at Mount Sinai, NY, USA.

Erik A Richter (EA)

Section of Molecular Physiology, Department of Nutrition, Exercise and Sports, Faculty of Science, University of Copenhagen, Copenhagen, Denmark.

Lykke Sylow (L)

Section of Molecular Physiology, Department of Nutrition, Exercise and Sports, Faculty of Science, University of Copenhagen, Copenhagen, Denmark.

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