Journal: Journal of molecular and cellular cardiology

Article Title: PKC? II Modulation of Myocyte Contractile Performance

doi: 10.1016/j.yjmcc.2012.05.001

Figure Lengend Snippet: Expression of PKC isoforms and myosin after gene transfer of PKCβII or PKCβDN (10 MOI) into rat myocytes. A. Representative expression of PKCβII and PKCβDN protein 1–3 days after gene transfer into adult rat myocytes. A silver-stained (Ag) portion of the SDS-PAGE gel is shown below blots in A, B, D and E to indicate protein load in each lane. B. Quantitative analysis of increased PKCβII and PKCβDN expression 1–3 days after gene transfer into rat myocytes. PKC expression is normalized to actin expression for each group and an asterisk indicates a statistically significant difference (p<0.05) compared to the control group. The number of samples analyzed for each data set is shown in the figure. C. Representative expression of PKCα, PKCβII, PKCδ, and PKCε isoforms in adult rat myocytes 2 days after PKCβII gene transfer compared to time-matched control myocytes. Protein expression of PKCα, PKCδ, and PKCε remained comparable to control levels 2 days after gene transfer (see Table 1). D. Representative detection of the increased PKCβ phosphorylation after gene transfer of PKCβII, and the negligible phosphorylation detected in time-matched controls and myocytes expressing PKCβDN. E. PKCβII up-regulation in failing (F) compared to non-failing (NF) human heart tissue. Total homogenate protein loaded into each lane was 40 µg for the first two NF samples and 10 µg protein for the third NF sample and all F samples (upper panel). Proteins were separated by 12% SDS-PAGE, transferred onto PVDF and probed for PKCβII. Quantitative analysis and significant up-regulation of PKCβII in failing versus non-failing human hearts is shown in the lower panel. F. Representative myosin heavy chain (MHC) isoform expression resolved with 8% SDS-PAGE in adult rat myocytes.

Article Snippet: Separated protein bands were transferred onto PVDF membrane for 2000 V-hours, and expression detected on milk-blocked membranes using PKCβ II primary antibody (Ab) (1:400; BD Biosciences, San Jose, CA).

Techniques: Expressing, Staining, SDS Page

Journal: BioMed Research International

Article Title: Restricted Water Intake and Hydration with Fructose-Containing Beverages during Infancy Predispose to Aggravate an Acute Renal Ischemic Insult in Adolescent Rats

doi: 10.1155/2020/4281802

Figure Lengend Snippet: Various parameters at the end of the 6 wks of follow-up evaluated preacute kidney injury (AKI) by ischemia/reperfusion: (a) urinary osmolality; (b) plasma copeptin; (c) creatinine clearance (CrCl); (d) nitrate/nitrite concentration (NO 2 /NO 3 ) in plasma; (e) nitrate/nitrite concentration (NO 2 /NO 3 ) in urine; (f) fructokinase (KHK) renal cortex expression; (g) angiotensin-converting enzyme 2 renal cortex expression; (h) angiotensin II renal cortex expression; (i) angiotensin II receptor type 1 (AT1-R) renal cortex expression; (j) kidney injury molecule 1 (KIM-1) renal cortex expression; (k) neutrophil gelatinase-associated lipocalin (NGAL) renal cortex expression; (l) lipid peroxidation measured in renal cortex homogenates. C: control; +W: increased water intake; +SB: sweetened beverage (SB) ad libitum; -W: fluid restriction plus hydration with tap water; -SB: fluid restriction plus hydration with SB. ∗ p < 0.05; ∗∗ p < 0.01; ∗∗∗ p < 0.001.

Article Snippet: Antibodies against kidney injury molecule 1 (KIM-1, Cat. GTX85067, dilution 1 : 2500), fructokinase (KHK, Cat. GTX109591, dilution 1 : 5000), angiotensin-converting enzyme 2 (ACE2, Cat. GTX101395, dilution 1 : 1500), and angiotensin II (Cat. GTX37789, dilution 1 : 1000) were obtained from GeneTex, Inc., Irvine, CA, USA.

Techniques: Clinical Proteomics, Concentration Assay, Expressing, Control