Lean and Obese Zucker Rat Extensor Digitorum Longus Muscle high-frequency electrical stimulation (HFES) Data: Regulation of p70S6kinase 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 AKT, GSK3beta, mTor, p70s6K, Pten, and Shp2 in the lean and obese (fa/fa) Zucker rat Extensor Digitorum Longus (EDL) muscle following a single bout of contractile stimuli. This article represents data associated with prior publications from our lab (Katta et al., 2009a, 2009b; Tullgren et al., 1991) [1–3] and concurrent Data in Brief articles (Ginjupalli et al., 2017a, 2017b; Rice et al., 2017a, 2017b) [4–7].


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-min period. Tissues were collected and protein was then isolated from tissue for western blot analysis. Experimental features EDL 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 gives insight into the how diabetes alters tissue response to stimuli. This data provides a more thorough understanding of the mTor pathway involvement in exercise mediated signaling in both diabetic and non-diabetic muscle tissue.
To determine the effect of HFES on EDL from OSXZ and LNZ animals we evaluated the phosphorylation of AKT Thr 308 and AKT Ser 473 to total AKT. EDL basal phosphorylation of AKT Thr 308 to total AKT was higher (12.1 7 5.6%, p o 0.05) in the OSXZ when compared to LNZ (Fig. 1D). HFES resulted in an increase in phosphorylation of AKT Thr 308 to total AKT in the LNZ EDL (19.3 7 2.0%, at 0 h, p o 0.05) and lower (20.8 7 0.5%, at 3 h, p o 0.05) when compared to LNZ contralateral control (Fig. 1D). HFES resulted in an increase in phosphorylation of AKT Thr 308 to total AKT in the OSXZ EDL (31.9 7 4.4% and 17. 3 7 4.1%, at 0 and 3 hours, p o 0.05) when compared to OSXZ contralateral control (Fig. 1D). EDL basal phosphorylation of AKT Ser 473 to total AKT was lower (53.

mTor
To determine the effect of HFES on EDL from OSXZ and LNZ animals we evaluated the phosphorylation of mTor at Serine 2448. EDL basal phosphorylation of mTor Ser 2448 was lower (49. To determine the effect of HFES on EDL from OSXZ and LNZ animals we evaluated the expression of mTor. EDL basal mTor content demonstrated no significant difference in the OSXZ when compared to LNZ (Fig. 3B). HFES resulted in no significant change in mTor in the LNZ EDL when compared to LNZ contralateral control (Fig. 3B). HFES did not produce a significant change in mTor in the OSXZ EDL when compared to contralateral OXSZ control (Fig. 3B).
To determine the effect of HFES on EDL from diabetic male OSXZ and LNZ animals we evaluated the phosphorylation of mTor at Serine 2448 to total mTor. EDL basal phosphorylation of mTor Ser 2448 to total mTor was lower (47.0 7 3.3%, p o 0.05) in the OSXZ when compared to LNZ (Fig. 3C).

PTEN
To determine the effect of HFES on EDL from OSXZ and LNZ animals we evaluated the phos-  (Fig. 5A).
To determine the effect of HFES on EDL from OSXZ and LNZ animals we evaluated the expression of PTEN. EDL basal PTEN was significant lower (39.4 7 4.2%, p o 0.05) in the OSXZ when compared to LNZ (Fig. 5B). HFES resulted in an increase in PTEN in the LNZ EDL (20.2 7 7.1%, at 3 h, p o 0.05) when compared to LNZ contralateral control (Fig. 5B). HFES resulted in an increase (37. 8 7 13.4%, at 3 h, p o 0.05) in PTEN in the OSZX EDL when compared to contralateral OXSZ control (Fig. 5B).
To determine the effect of HFES on EDL from OSXZ and LNZ animals we evaluated the expression of SHP23. EDL basal SHP2 content demonstrated no significant difference in the OSXZ when compared to LNZ (Fig. 6B). HFES resulted in an increase in SHP2 in the LNZ EDL (44.0 7 13.0%, at 3 h, p o 0.05) when compared to LNZ contralateral control (Fig. 6B). HFES resulted in an increase (185.1 7 23.8%, at 3 h, p o 0.05) in SHP2 in the OSZX EDL when compared to contralateral OXSZ control (Fig. 6B).
To determine the effect of HFES on EDL from OSXZ and LNZ animals we evaluated the phosphorylation of SHP2 Tyr 542 to total SHP2. EDL basal phosphorylation of SHP2 Tyr 542 to total SHP2 was lower (86.3 7 0.14%, p o 0.05) in the OSXZ when compared to LNZ (Fig. 6C). HFES resulted in a decrease in phosphorylation of SHP2 Tyr 542 to total SHP2 in the LNZ EDL (35.6 7 5.5% and 61.1 7 1.4%, at 0 and 1 h, p o 0.05) when compared to LNZ contralateral control (Fig. 6C). HFES resulted in an increase in phosphorylation of SHP2 Tyr 542 to total SHP2 in the OSXZ EDL (48.9 7 2.5% and 65.4 7 5.7%, at 0 and 3 h, p o 0.05) when compared to OSXZ contralateral control (Fig. 6C).

Animals
All procedures were conducted 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 ¼ 12) male lean Zucker (non-diabetic) (LNZ) and young (10 week, n ¼ 12) 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 22 7 2°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 pentobarbital sodium at baseline, immediately following, 1 h or 3 h (n ¼ 6 normal, n ¼ 6 diabetic for 0, 1, and 3 h) after HFES. Once Fig. 6. Diabetes alters HFES-induced expression and phosphorylation of SHP2 rat EDL. The basal (control) and HFES-induced expression of p42/p44 in EDL from non-diabetic lean Zucker (LNZ) and diabetic obese syndrome X Zucker (OSXZ) rats. * Significantly different from HFES EDL within the same group (p o 0.05). † Significantly different from corresponding LNZ EDL (p o 0.05). n ¼ 6/group. 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 3.0 statistical software and the results are presented as mean 7 SEM. Two-way ANOVA followed by the Student-Newman-Keuls post-hoc testing to determine differences between groups. The level of significance accepted a priori was o 0.05.