The p21-activated kinase 2 (PAK2), but not PAK1, regulates contraction-stimulated skeletal muscle glucose transport

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The p21-activated kinase 2 (PAK2), but not PAK1, regulates contraction-stimulated skeletal muscle glucose transport. / Møller, Lisbeth Liliendal Valbjørn; Nielsen, Ida L; Knudsen, Jonas Roland; Andersen, Nicoline Resen; Jensen, Thomas Elbenhardt; Sylow, Lykke; Richter, Erik A.

I: Physiological Reports, Bind 8, Nr. 12, e14460, 2020.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Møller, LLV, Nielsen, IL, Knudsen, JR, Andersen, NR, Jensen, TE, Sylow, L & Richter, EA 2020, 'The p21-activated kinase 2 (PAK2), but not PAK1, regulates contraction-stimulated skeletal muscle glucose transport', Physiological Reports, bind 8, nr. 12, e14460. https://doi.org/10.14814/phy2.14460

APA

Møller, L. L. V., Nielsen, I. L., Knudsen, J. R., Andersen, N. R., Jensen, T. E., Sylow, L., & Richter, E. A. (2020). The p21-activated kinase 2 (PAK2), but not PAK1, regulates contraction-stimulated skeletal muscle glucose transport. Physiological Reports, 8(12), [e14460]. https://doi.org/10.14814/phy2.14460

Vancouver

Møller LLV, Nielsen IL, Knudsen JR, Andersen NR, Jensen TE, Sylow L o.a. The p21-activated kinase 2 (PAK2), but not PAK1, regulates contraction-stimulated skeletal muscle glucose transport. Physiological Reports. 2020;8(12). e14460. https://doi.org/10.14814/phy2.14460

Author

Møller, Lisbeth Liliendal Valbjørn ; Nielsen, Ida L ; Knudsen, Jonas Roland ; Andersen, Nicoline Resen ; Jensen, Thomas Elbenhardt ; Sylow, Lykke ; Richter, Erik A. / The p21-activated kinase 2 (PAK2), but not PAK1, regulates contraction-stimulated skeletal muscle glucose transport. I: Physiological Reports. 2020 ; Bind 8, Nr. 12.

Bibtex

@article{d2c94a9f119747118308f3a7cd91472e,

title = "The p21-activated kinase 2 (PAK2), but not PAK1, regulates contraction-stimulated skeletal muscle glucose transport",

abstract = "Aim: Muscle contraction stimulates skeletal muscle glucose transport. Since it occurs independently of insulin, it is an important alternative pathway to increase glucose transport in insulin-resistant states, but the intracellular signaling mechanisms are not fully understood. Muscle contraction activates group I p21-activated kinases (PAKs) in mouse and human skeletal muscle. PAK1 and PAK2 are downstream targets of Rac1, which is a key regulator of contraction-stimulated glucose transport. Thus, PAK1 and PAK2 could be downstream effectors of Rac1 in contraction-stimulated glucose transport. The current study aimed to test the hypothesis that PAK1 and/or PAK2 regulate contraction-induced glucose transport.Methods: Glucose transport was measured in isolated soleus and extensor digitorum longus (EDL) mouse skeletal muscle incubated either in the presence or absence of a pharmacological inhibitor (IPA-3) of group I PAKs or originating from whole-body PAK1 knockout, muscle-specific PAK2 knockout or double whole-body PAK1 and muscle-specific PAK2 knockout mice.Results: IPA-3 attenuated (-22%) the increase in glucose transport in response to electrically stimulated contractions in soleus and EDL muscle. PAK1 was dispensable for contraction-stimulated glucose transport in both soleus and EDL muscle. Lack of PAK2, either alone (-13%) or in combination with PAK1 (-14%), partly reduced contraction-stimulated glucose transport compared to control littermates in EDL, but not soleus muscle.Conclusion: Contraction-stimulated glucose transport in isolated glycolytic mouse EDL muscle is partly dependent on PAK2, but not PAK1.",

keywords = "Faculty of Science, Contraction, Glucose uptake, p21-activated kinase, Skeletal muscle",

author = "M{\o}ller, {Lisbeth Liliendal Valbj{\o}rn} and Nielsen, {Ida L} and Knudsen, {Jonas Roland} and Andersen, {Nicoline Resen} and Jensen, {Thomas Elbenhardt} and Lykke Sylow and Richter, {Erik A.}",

note = "{\textcopyright} 2020 The Authors. Physiological Reports published by Wiley Periodicals LLC on behalf of The Physiological Society and the American Physiological Society.",

year = "2020",

doi = "10.14814/phy2.14460",

language = "English",

volume = "8",

journal = "Physiological Reports",

issn = "2051-817X",

publisher = "Wiley Periodicals, Inc.",

number = "12",

}

RIS

TY - JOUR

T1 - The p21-activated kinase 2 (PAK2), but not PAK1, regulates contraction-stimulated skeletal muscle glucose transport

AU - Møller, Lisbeth Liliendal Valbjørn

AU - Nielsen, Ida L

AU - Knudsen, Jonas Roland

AU - Andersen, Nicoline Resen

AU - Jensen, Thomas Elbenhardt

AU - Sylow, Lykke

AU - Richter, Erik A.

PY - 2020

Y1 - 2020

N2 - Aim: Muscle contraction stimulates skeletal muscle glucose transport. Since it occurs independently of insulin, it is an important alternative pathway to increase glucose transport in insulin-resistant states, but the intracellular signaling mechanisms are not fully understood. Muscle contraction activates group I p21-activated kinases (PAKs) in mouse and human skeletal muscle. PAK1 and PAK2 are downstream targets of Rac1, which is a key regulator of contraction-stimulated glucose transport. Thus, PAK1 and PAK2 could be downstream effectors of Rac1 in contraction-stimulated glucose transport. The current study aimed to test the hypothesis that PAK1 and/or PAK2 regulate contraction-induced glucose transport.Methods: Glucose transport was measured in isolated soleus and extensor digitorum longus (EDL) mouse skeletal muscle incubated either in the presence or absence of a pharmacological inhibitor (IPA-3) of group I PAKs or originating from whole-body PAK1 knockout, muscle-specific PAK2 knockout or double whole-body PAK1 and muscle-specific PAK2 knockout mice.Results: IPA-3 attenuated (-22%) the increase in glucose transport in response to electrically stimulated contractions in soleus and EDL muscle. PAK1 was dispensable for contraction-stimulated glucose transport in both soleus and EDL muscle. Lack of PAK2, either alone (-13%) or in combination with PAK1 (-14%), partly reduced contraction-stimulated glucose transport compared to control littermates in EDL, but not soleus muscle.Conclusion: Contraction-stimulated glucose transport in isolated glycolytic mouse EDL muscle is partly dependent on PAK2, but not PAK1.

AB - Aim: Muscle contraction stimulates skeletal muscle glucose transport. Since it occurs independently of insulin, it is an important alternative pathway to increase glucose transport in insulin-resistant states, but the intracellular signaling mechanisms are not fully understood. Muscle contraction activates group I p21-activated kinases (PAKs) in mouse and human skeletal muscle. PAK1 and PAK2 are downstream targets of Rac1, which is a key regulator of contraction-stimulated glucose transport. Thus, PAK1 and PAK2 could be downstream effectors of Rac1 in contraction-stimulated glucose transport. The current study aimed to test the hypothesis that PAK1 and/or PAK2 regulate contraction-induced glucose transport.Methods: Glucose transport was measured in isolated soleus and extensor digitorum longus (EDL) mouse skeletal muscle incubated either in the presence or absence of a pharmacological inhibitor (IPA-3) of group I PAKs or originating from whole-body PAK1 knockout, muscle-specific PAK2 knockout or double whole-body PAK1 and muscle-specific PAK2 knockout mice.Results: IPA-3 attenuated (-22%) the increase in glucose transport in response to electrically stimulated contractions in soleus and EDL muscle. PAK1 was dispensable for contraction-stimulated glucose transport in both soleus and EDL muscle. Lack of PAK2, either alone (-13%) or in combination with PAK1 (-14%), partly reduced contraction-stimulated glucose transport compared to control littermates in EDL, but not soleus muscle.Conclusion: Contraction-stimulated glucose transport in isolated glycolytic mouse EDL muscle is partly dependent on PAK2, but not PAK1.

KW - Faculty of Science

KW - Contraction

KW - Glucose uptake

KW - p21-activated kinase

KW - Skeletal muscle

U2 - 10.14814/phy2.14460

DO - 10.14814/phy2.14460

M3 - Journal article

C2 - 32597567

VL - 8

JO - Physiological Reports

JF - Physiological Reports

SN - 2051-817X

IS - 12

M1 - e14460

ER -

ID: 244042875