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Journal: Journal of neurochemistry
Article Title: Parkin mediates the degradation-independent ubiquitination of Hsp70
doi: 10.1111/j.1471-4159.2008.05261.x
Figure Lengend Snippet: (a) Hsp70 levels are not altered in parkin-deficient AR-JP brains. Equivalent detergent-soluble and -insoluble protein fractions extracted from frontal cortex tissue of control (1–4) and parkin-deficient AR-JP brains (1–4) were analyzed by Western blot with anti-Hsp70 antibody, or anti-actin antibody as a protein loading control. Hsp70 levels were quantified by densitometry and normalized to β-actin levels in the detergent-soluble and -insoluble fraction of control (n = 4) and AR-JP (n = 4) brains. Data are expressed as a percentage (%) of control levels as the ratio of Hsp70 to β-actin, and bars represent the mean ± SEM. (b) Hsp70 displays reduced detergent-solubility in sporadic PD/DLB brains. Equivalent detergent-soluble and -insoluble protein fractions extracted from cin-gulate cortex tissue of control (5–6), Alzheimer’s disease (AD; 1–2) and PD/DLB (1–5) brains, were analyzed by Western blot with anti-Hsp70 antibody, or with anti-SOD1 and anti-β-tubulin antibodies as protein loading controls. Hsp70 levels were quantified by densitometry and normalized in the detergent-soluble and -insoluble fraction of control (control + AD; n = 4) and PD/DLB (n = 5) brains. Data are expressed as a percentage (%) of control levels as the ratio of Hsp70 to SOD1 (soluble) or β-tubulin (insoluble), and bars represent the mean ± SEM. Differences between means were analyzed by two-tailed unpaired Student’s t-test, *p < 0.05 when compared with control, ns, non-significant.
Article Snippet: Quantitation of protein levels was performed using
Techniques: Control, Western Blot, Solubility, Two Tailed Test