Fig. 2
From: Network approach identifies Pacer as an autophagy protein involved in ALS pathogenesis
Pacer levels are reduced during ALS pathology. a Human Pacer (hPacer) and human Rubicon (hRubicon) protein levels were determined in post-mortem spinal cord sections from sALS patients and age-matched control subjects. Left panel, cervical spinal cord section with Controls n = 2 and sALS patients n = 6; middle panel, thoracic spinal cord section with Controls n = 2 and sALS patients n = 7; and right panel, lumbar spinal cord section with Controls n = 6 and sALS patients n = 7. β-Actin serves as a loading control. Densitometric quantifications of hPacer and hRubicon normalized to β-Actin levels are shown. b Pacer and Rubicon protein levels were determined in lumbar spinal cord samples of late symptomatic TDP43A315T transgenic mice (TDP43A315T-Tg, n = 5) and their non-transgenic littermate controls (n = 3), respectively. TDP43 aggregate levels under non-reducing (−DTT) conditions are shown as positive controls. β-Actin serves as a loading control. Densitometric quantifications of Pacer protein levels normalized to β-Actin levels are shown. c, Pacer and Rubicon protein levels were determined in the lumbar spinal cord of late symptomatic SOD1G93A transgenic mice (SOD1G93A-Tg) and their non-transgenic littermate controls (both groups n = 7). p62 protein levels were detected as a positive control of impaired autophagy. SOD1 aggregate levels under non-reduced (−DTT) conditions are shown as a positive control for SOD1G93A-Tg mice. β-Actin serves as a loading control. Densitometric quantifications of Pacer protein levels normalized to β-Actin levels are shown. In a-c Statistical analyses were performed using Student’s t-test. Mean and SEM with only statistical significant p-values are shown: *, p ≤ 0.05; **, p ≤ 0.01; and ***, p ≤ 0.001