
Expression of ammonia transporters Rhbg and Rhcg in mouse skeletal muscle and the effect of 6‐week training on these proteins
Author(s) -
Takeda Kohei,
Takemasa Tohru
Publication year - 2015
Publication title -
physiological reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.918
H-Index - 39
ISSN - 2051-817X
DOI - 10.14814/phy2.12596
Subject(s) - skeletal muscle , transporter , microbiology and biotechnology , chemistry , biology , bioinformatics , biochemistry , endocrinology , gene
The purposes of our study were to examine (1) Rh B glycoprotein (Rhbg) and Rh C glycoprotein (Rhcg) expressions in mouse skeletal muscle; and (2) the effect of 6‐week training on Rhbg and Rhcg expressions. The levels of Rhbg and Rhcg expressions were much higher in the soleus (Sol) than in the plantaris (Pla) or gastrocnemius (Gas). Immunofluorescence microscopy demonstrated that Rhbg colocalizes with dystrophin, a plasma membrane protein marker, whereas Rhcg colocalizes with CD 31, a vascular endothelial cell marker. In a 6‐week swim training study, we set up two different training groups. Endurance ( END ) group underwent swim training without load for 30 min and exercise time was increased by 30 min every 2 weeks. High‐intensity interval training ( HIIT ) group underwent 10–12 sets of swim training at 20 sec per set and intervals of 10 sec, with a load of 10% body weight. After 6 weeks of training, all mice performed exhaustive swimming performance test ( PT ), with 9% of body weight to exhaustion. HIIT group could significantly swim more and showed significantly lower blood ammonia level compared with control ( CON ) group at immediately after PT . Rhbg and Rhcg levels did not change after 6 weeks in both END and HIIT groups. Our results indicate that ammonia transporters are more abundant in slow fiber than fast fiber muscles and 6 weeks swim training suppresses blood ammonia elevation induced by high‐intensity exercise with performance improvement, although the levels of ammonia transporter proteins does not change.