Endurance training increases LKB1 and MO25 protein but not AMP-activated protein kinase kinase activity in skeletal muscle

E B Taylor; D Hurst; L J Greenwood; J D Lamb; T D Cline; S N Sudweeks; W W Winder

doi:10.1152/ajpendo.00179.2004

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Endurance training increases LKB1 and MO25 protein but not AMP-activated protein kinase kinase activity in skeletal muscle

Journal article

Peer reviewed

Endurance training increases LKB1 and MO25 protein but not AMP-activated protein kinase kinase activity in skeletal muscle

E B Taylor, D Hurst, L J Greenwood, J D Lamb, T D Cline, S N Sudweeks and W W Winder

American journal of physiology: endocrinology and metabolism, Vol.287(6), pp.E1082-1089

12/2004

DOI: 10.1152/ajpendo.00179.2004

PMID: 15292028

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Abstract

LKB1 complexed with MO25 and STRAD has been identified as an AMP-activated protein kinase kinase (AMPKK). We measured relative LKB1 protein abundance and AMPKK activity in liver (LV), heart (HT), soleus (SO), red quadriceps (RQ), and white quadriceps (WQ) from sedentary and endurance-trained rats. We examined trained RQ for altered levels of MO25 protein and LKB1, STRAD, and MO25 mRNA. LKB1 protein levels normalized to HT (1 +/- 0.03) were LV (0.50 +/- 0.03), SO (0.28 +/- 0.02), RQ (0.32 +/- 0.01), and WQ (0.12 +/- 0.03). AMPKK activities in nanomoles per gram per minute were HT (79 +/- 6), LV (220 +/- 9), SO (22 +/- 2), RQ (29 +/- 2), and WQ (42 +/- 4). Training increased LKB1 protein in SO, RQ, and WQ (P < 0.05). LKB1 protein levels after training (%controls) were SO (158 +/- 17), RQ (316 +/- 17), WQ (191 +/- 27), HT (106 +/- 2), and LV (104 +/- 7). MO25 protein after training (%controls) was 595 +/- 71. Training did not affect AMPKK activity. MO25 but not LKB1 or STRAD mRNA increased with training (P < 0.05). Trained values (%controls) were MO25 (164 +/- 22), LKB1 (120 +/- 16), and STRAD (112 +/- 17). LKB1 protein content strongly correlated (r = 0.93) with citrate synthase activity in skeletal muscle (P < 0.05). In conclusion, endurance training markedly increased skeletal muscle LKB1 and MO25 protein without increasing AMPKK activity. LKB1 may be playing multiple roles in skeletal muscle adaptation to endurance training.

Protein Kinases - metabolism

Muscle, Skeletal - enzymology

Liver - enzymology

Liver - metabolism

Rats

Male

Muscle, Skeletal - metabolism

Physical Endurance

Rats, Sprague-Dawley

Myocardium - enzymology

Animals

Myocardium - metabolism

Adaptor Proteins, Signal Transducing - metabolism

Physical Conditioning, Animal

Protein-Serine-Threonine Kinases - metabolism

Details

Title: Subtitle: Endurance training increases LKB1 and MO25 protein but not AMP-activated protein kinase kinase activity in skeletal muscle
Creators: E B Taylor - Department of Physiology and Developmental Biology, Brigham Young University, Provo, Utah 84602, USA
D Hurst
L J Greenwood
J D Lamb
T D Cline
S N Sudweeks
W W Winder
Resource Type: Journal article
Publication Details: American journal of physiology: endocrinology and metabolism, Vol.287(6), pp.E1082-1089
Publisher: United States
DOI: 10.1152/ajpendo.00179.2004
PMID: 15292028
ISSN: 0193-1849
eISSN: 1522-1555
Grant note: AR 41438 / NIAMS NIH HHS
Language: English
Date published: 12/2004
Academic Unit: Molecular Physiology and Biophysics; Fraternal Order of Eagles Diabetes Research Center
Record Identifier: 9984025430002771

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