Effect of different mutations on the structure and levels of REP-1 mRNA and protein.

<p><b>a</b>, Effect of different nonsense mutations on the structure of REP-1 protein (Q273X, I460X, M1I and K234X). <b>b</b>, Distribution and position of the mutations in the REP-1 protein, note that 4 of 9 mutations localized in the beta sheet of the REP-1 (blue) and 7 of 9 mutations (P179X, K234X, I244X, I460X, Y504 X, L550P and I553X, <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0008402#pone-0008402-t001" target="_blank"><b>Table 1</b></a>) localized to domain 2 of the REP-1 protein. <b>c</b>. Levels of mRNA determined by the microarray analysis of the expression profiles from monocytes and fibroblasts from CHM and control patients. Control group, n = 5; group CHM1 includes patients with low levels of REP1 mRNA, n = 7; group CHM2 includes patients with REP-1 mRNA similar to the controls, n = 6. <b>d</b>. Expression levels of REP-1 and REP-2 in different cell types derived from CHM and control patients. Lane: 1, 10 ng of rat recombinant REP-1 or 10 ng of rat recombinant REP-2 with HisTag; cell lysates (40 µg of protein for each) 2, ARPE19; 3, human fetal RPE; 4, MO- monocytes from control; 5, MO-monocytes from patient CHM4; 6, cultured human umbilical vein endothelial cells (HUVECs); 7, primary fibroblasts from control; 8, primary fibroblasts from CHM2 patient. β-actin was used as a loading control.</p>

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