Vascular mechanotransduction data in a rodent model of diabetes: Pressure-induced regulation of SHP2 and associated signaling in the rat inferior vena cava

The effect of diabetes on vascular mechano-transductive response is of great concern. Given the higher rate of vein graft failures associated with diabetes, understanding the multiple cellular and molecular events associated with vascular remodeling is of vital importance. This article represents data related to a study published in Cardiovascular Diabetology [1] (Rice et al., 2006) and Open Journal of Endocrine and Metabolic Diseases [2] (Rice et al., 2015) evaluating the effect of pressurization on rat inferior venae cavae (IVC). Provided within this articles is information related to the method and processing of raw data related to our prior publish work and Data in Brief articles [3], [4] (Rice et al., 2017), as well as the evaluation of alternation in SHP-2 signaling and associated proteins in response to mechanical force. IVC from lean and obese animals were exposed to a 30 min perfusion of 120 mm Hg pressure and evaluated for changes in expression of SHP2, BCL-3, BCL-XL, HSP 27, HSP 70, and PI3K p85, along with the phosphorylation of SHP-2 (Tyr 542).


Data source location
The data is presented within this document Data accessibility Data is wit this article and is related to articles published and in review [1][2][3][4] Value of the data The data presented in this Brief is vital to understanding the effect of diabetes on tissue This data gives insight into the how diabetes alters tissue response to stimuli The data can provide comprehensive analysis of the effect of diabetes on vascular signaling in vein transplant surgery These data provides a more thorough understanding of the SHP-2 involvement in pressure mediated signaling in both diabetic and lean IVC 1. Data

BCL-3
BCL-3 is a member of the IκB family of NFκB and is regulated by GSK3 [6]. SHP-2 is activated by GSK3 inhibition but is not a direct target of GSK3 [7]. To investigate the possible link between SHP-2 and BCL-3 through GSK3 we looked at changes in BCL-3 expression. OSXZ control IVC showed no significant change in BCL-3 basal expression when compared to LNZ control. Examination of the effect of pressurization of inferior vena cava expression of BCL-3 demonstrated significant increase in LNZ (113 76.4% p o0.05) but no change in OSXZ animals, this absence of a pressure induced increase in the OSXZ IVC was significantly different compared to lean (Fig. 2-A).

BCL-XL
The BCL-2 homolog BCL-XL prominent pro-survival functions by binding to its multi-domain proapoptotic counterparts BAX and BAK, thus preventing the formation of lethal pores in the mitochondrial outer membrane [8]. The vasoactive peptide angiotensin II (Ang II) activated SHP-2 inhibits nucleolin binding to BCL-XL mRNA thereby altering the equilibrium and expression of antiand pro-apoptotic regulators [9]. OSXZ control IVC showed no significant change in BCL-XL basal expression when compared to LNZ control. Examination of the effect of pressurization of IVC expression of BCL-XL demonstrated significant increase in LNZ (106 7 8.3% p o0.05) and OSXZ (72 7 12.7% p o0.05). However the pressure induced elevation in the OSXZ IVC was significantly less than that of the lean (34 7 21.0% p o0.05) (Fig. 2-B).

HSP 27
The small heat shock protein HSP 27 has been shown to be involved in a number of cellular processes. Recently research has indicated that it is required for proper heart tube formation [10]. SHP-2 inhibition has been shown to have no effect on the expression of HSP 27 a known marker for cardiac differentiation [11]. To confirm that HSP 27 and SHP-2 demonstrated no association in vascular remodeling we looked at the expression of HSP 27 in the pressurized IVC. OSXZ control IVC showed no significant change in HSP 27 basal expression when compared to LNZ control. Examination of the effect of pressurization of IVC expression of SHP 27 demonstrated no significant increase in LNZ or OSXZ (Fig. 3-A).

HCP 70
The 70 kDa heat shock proteins (HSP 70) is a ubiquitously expressed chaperone protein activated by various cellular stresses including oxygen-free radicals, inflammation, heat shock, oncogenes, and proto-oncogenes [12]. HSP70 play an important role in protecting the cells from stress and regulating the cell's machinery for protein folding [13,14]. HSP70 has been shown to bind SHP-2 and effect SHP-2 related signaling [12,15]. IVCs obtained from the OSXZ control group showed a significant decrease in the basal expression of HSP 70 when compared to the LNZ control animals (43 7 1.4% p o0.05). Pressurization resulted in a significant increase in HSP 70 in the LNZ IVC (54 7 2.9% po 0.05) and OSXZ IVC (91 7 3.0% p o0.05) (Fig. 1-B). However the pressure induced elevation in the OSXZ IVC was significantly greater than that of the lean (37 7 6.9% p o0.05) (Fig. 3-B).

Animals
Young (10 week, n ¼12) male normal 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. All procedures were conducted in strict accordance with the Public Health Service policy on animal welfare. Housing conditions consisted of a 12 H: 12 H dark-light cycle and temperature was maintained at 2272°C. Animals were provided food and water ad libitum. Rats were allowed to recover from shipment stress for at least two weeks before the commencement of experimentation during which time the animals were carefully observed and weighed weekly. All procedures were performed in 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. [1][2][3][4].

Materials
Antibodies . SDS-PAGE precast gels were purchased from Lonza (Rockland, ME). Enhanced chemiluminescence (ECL) western blotting detection reagent was purchased from Amersham Biosciences (Piscataway, NJ). All other chemicals were from Sigma (St. Louis, MO).

Data analysis
Data were analyzed using the Sigma Stat 3.0 and results were presented as mean 7 SEM. A oneway analysis of variance (ANOVA) was performed for overall comparisons followed by the Student-Newman-Keuls post hoc test to determine differences between groups. The level of significance accepted a priori was r 0.05.