Diabetic Zucker rat Tibialis anterior muscle high-frequency electrical stimulation (HFES) data: Regulation of MAPKs associated proteins

Anaerobic exercise has been advocated as a prescribed treatment for the management of diabetes: however, alterations in exercise-induced signaling remain largely unexplored in the diabetic muscle. Here, we compare the basal and the in situ contraction-induced phosphorylation of the mitogen-activated protein kinases (MAPKs) ERK 1/2, p38, and JNK in the lean and obese (fa/fa) Zucker rat tibialus anterior (TA) muscle following a single bout of contractile stimuli. This article represents data associated with prior publications from our lab (Katta et al., 2009, Katta et al., 2009, Tullgren et al., 1991) [1–3] and concurrent Data in Brief articles (Ginjupalli et al., 2017, Rice et al., 2017, Rice et al., 2017, Rice et al., 2017) [4–7].

& 2017 The Authors. Published by Elsevier Inc. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).

Subject area
Biology More specific subject area Diabetic skeletal muscle response to exercise Type of data graph, figure How data was acquired immunoblotting

Data format analyzed Experimental factors
A high-frequency electrical stimulation (HFES) was used to produce 10 sets of 6 contractions over a 22-minute period. Tissues were collected and protein was then isolated from tissue for western blot analysis.

Experimental features
TA obtained from Lean and Obese male Zucker rats were used in this experiment

Data source location
Huntington, WV USA Data accessibility Data is with this article and is related to articles published and in review [1][2][3][4][5][6][7] Value of the data The data presented in this brief is vital to understanding the effect of diabetes on skeletal muscle mechanotransduction.
This data sheds light on how diabetes alters tissue response to stimuli. This data provides a more thorough understanding of the MAPKs involvement in exercise mediated signaling in both diabetic and non-diabetic muscle tissue.

ERK 1/2
To determine the effect of high-frequency electrical stimulation (HFES) on TA in diabetic male obese syndrome-X Zucker (OSXZ) animals and nondiabetic male lean Zucker (LNZ) animals we evaluated the expression of extracellular-signal-regulated kinase (ERK 1/2 -p44/p42). TA basal p42 content was lower (19.5 7 1.8%, po 0.05) in the OSXZ when compared to LNZ. HFES resulted in a decrease in p42 in the LNZ TA (11.87 1.5%, 15.2 71.9%, and 16.2 71.3%, at 0, 1,and 3 h, p o0.05) when compared to LNZ contralateral control. However HFES did not elicit a response in the OSZX TA when compared to contralateral OXSZ control. TA basal p44 content demonstrated no significant difference in the OSXZ when compared to LNZ. HFES did not elicit a change in p44 in the LNZ TA when compared to LNZ contralateral control. However HFES resulted in a decrease (19.5 77.7%, at 3 h, p o0.05) in the OSZX TA when compared to contralateral OXSZ control (Fig. 1).

P38
To determine the effect of HFES on TA in OSXZ and LNZ animals we evaluated the expression of p38 alpha and gamma. TA basal p38 alpha content demonstrated no significant difference in the OSXZ when compared to LNZ. HFES did not elicit a significant change in p38 alpha in the LNZ TA when compared to LNZ contralateral control. HFES did not elicit a response in the OSZX TA when compared to contralateral OXSZ control. TA basal p38 gamma content demonstrated no significant difference in the OSXZ when compared to LNZ. HFES did not elicit a significant change in p38 gamma in the LNZ TA when compared to LNZ contralateral control. HFES did not elicit a significant change in p38 gamma in the OSZX TA when compared to contralateral OXSZ control (Fig. 2).
To determine the effect of HFES on TA in OSXZ and LNZ animals, we evaluated the phosphorylation of p38 alpha and gamma at threonine 180 and tyrosine 182 (p38 thr 180/tyr 182). TA basal phosphorylation of p38 alpha thr 180/tyr 182 was lower (23.  (Fig. 2).
To determine the effect of HFES on TA in OSXZ and LNZ animals we evaluated the ratio of phosphorylation of p38 alpha and gamma thr 180/tyr 182 to total p38 alpha and gamma. TA basal phosphorylation of p38 alpha thr 180/tyr 182 to total p38 alpha was not significantly different in the OSXZ when compared to LNZ. HFES resulted in an increase (139.7 720.6%, 95.2 77.6%, and 28.1 75.1%, at 0, 1,and 3 h, p o0.05) in phosphorylation of p38 alpha thr180/tyr 182 to total p38 alpha in the LNZ TA when compared to LNZ contralateral control. HFES resulted in an increase (118.8 7 9.2%, 100.5 75.7%, and 84.1 712.7%, at 0, 1 and 3 h, po 0.05) in phosphorylation of p38 thr 180/tyr 182 to total p38 alpha in the OSXZ TA when compared to OSXZ contralateral control. TA basal phosphorylation of p38 gamma thr 180/tyr 182 to total p38 gamma demonstrated no significant difference in the OSXZ when compared to LNZ. HFES did not elicit a significant change in phosphorylation of p38 gamma thr 180/tyr 182 to total p38 gamma in the LNZ TA when compared to LNZ contralateral control. HFES did not elicit a significant change in phosphorylation of p38 gamma thr 180/tyr 182 in the OSXZ TA when compared to OSXZ contralateral control (Fig. 2).

Animals
All procedures were conducted as described elsewhere [1][2][3][4][5][6][7] in strict accordance with the Guide for the Care and Use of Laboratory Animals as approved by the Council of the American Physiological Society and the Animal Use Review Board of Marshall University. Young (10 week, n ¼12) male lean Zucker (non-diabetic) (LNZ) and young (10 week, n ¼12) male obese syndrome-X Zucker (diabetic) (OSXZ) rats were obtained from the Charles River Laboratories and barrier housed one per cage in an AAALAC approved vivarium. Housing conditions consisted of a 12H:12H dark-light cycle and the temperature was maintained at 2272°C. Animals were provided food and water ad libitum. Rats were allowed to recover from shipment for at least two weeks before the commencement of experimentation during which time the animals were carefully observed and weighed weekly.

Contractile stimulation of skeletal muscles
The high-frequency electrical stimulation (HFES) model has been previously described [8] and was chosen on the basis of its efficacy in stimulating protein translation and muscle hypertrophy in vivo [9]. The HFES model used in the present study produced 10 sets of 6 contractions with an overall protocol time of 22 min. Animals were killed by a lethal dose of sodium pentobarbital at baseline, immediately following, 1 h or 3 h (n ¼6 normal, n¼ 6 diabetic for 0, 1, and 3 h) after HFES. Once excised, muscles were blotted dry, trimmed of visible fat and tendon projections, weighed, immediately frozen in liquid nitrogen, and stored at −80°C.

Data analysis
Data were analyzed using Sigma Stat 12.0 statistical software and the results are presented as mean 7SEM. Two-way ANOVA followed by the Student-Newman-Keuls post-hoc test was conducted to determine differences between groups. The level of significance accepted a priori was o0.05.