Only one of the six control grafts was patent, but all of the paclitaxel-coated grafts were

patent, with little neointima. The mean +/- standard error values of percentage luminal stenosis were 75.7% +/- 12.7% (control), 17.5% +/- 3.1% (low dose), and 19.7% +/- 3.0% (high dose). The values for the neointimal area (in mm(2)) were 8.77 +/- 1.66 (control), 3.53 +/- Liproxstatin-1 solubility dmso 0.73 (lose dose), and 4.24 +/- 0.99 (high dose). Compared with the control group, paclitaxel inner-coated vascular grafts significantly suppressed neointimal hyperplasia (low dose, P = .001; high dose, P = .002). Myofibroblast proliferation and migration into the graft interstices confirmed the firm attachment of the implanted graft to the surrounding tissue. Conclusions: Paclitaxel coating on the inner luminal surface of vascular grafts was effective in suppressing neointimal hyperplasia, with little inhibition of myofibroblast infiltration within the graft wall. (J Vasc Surg 2012; 55: 806-14.)

Clinical Relevance. Paclitaxel-coated vascular buy Elacridar grafts effectively inhibited the neointimal hyperplasia of hemodialysis grafts. However, paclitaxel on the outer surface of expanded polytetrafluoroethylene grafts might prevent myofibroblast proliferation, which might cause hematomas, seromas, infections, or pseudoaneurysms

in the space between the graft and surrounding tissue and result in incomplete hemodialysis needle insertion. Therefore, paclitaxel inner-coated expanded polytetrafluoroethylene grafts can reduce the coated amount of this potentially toxic drug to avoid such unwanted effects, whilst preserving its efficacy in inhibiting stenosis.”
“Spinocerebellar ataxia type 1 (SCA1) is one of a group of nine expanded CAG repeat

diseases, in which polyglutamine (polyQ) Amyloid precursor protein secretase expansion above a threshold is associated with increased disease risk and aggregation. SCA1 is unique in which the polyQ in the disease protein, ataxin1, often contains a few His residues that appear to block toxicity. Here, we ask how His insertions affect aggregation by comparing a Q(30) peptide with and without a centrally inserted His-Gln-His sequence. We found that at pH 7.5-8.5, His interruptions decrease polyQ aggregation rates but do not change the spontaneous growth mechanism: nucleated growth polymerization with a critical nucleus of one without non-fibrillar intermediates. The decreased aggregation rates are because of reductions in nucleation equilibrium constants. At pH 6, however, the His-interrupted peptide aggregates by a different mechanism that involves a low ThT-binding intermediate and produces a polymorphic amyloid product. In aggregates grown at pH 7.5, the His residues are solvent-accessible. Aggregates of His-inserted polyQ are good seeds for Q(30) elongation, suggesting the potential to recruit polyQ proteins in the cell. Our data are therefore most consistent with His insertions blocking toxicity by suppressing rates and/or altering pathways of spontaneous aggregation.