RESULTS: The study comprised 98 patients (195 eyes). The femtosecond laser energy for flap preparation was 160 to 200 nJ. The mean achieved flap thickness was 91.35 mu m +/- 12.26 (SD) (attempted 80 mu m), 98.5 +/- 14.39 mu m (attempted 90 mu m), 109.94 +/- 13.43

mu m (attempted 100 mu m), 112.7 +/- 7.45 mu m (attempted 110 mu m), and 123.82 +/- 9.64 mu m (attempted 120 mu m). Post-operatively, 87% of eyes were within +/- 0.25 diopter of the Selleck BEZ235 intended spherical equivalent, 75% had a UDVA of 20/16 (-0.1 logMAR) or better, and 42% gained 1 or more lines of visual acuity; no eye lost CDVA. No statistically significant relationships were found between energy, side-cut angle, achieved flap thickness, and refractive and visual outcomes. Complications were mild and did not affect final visual outcomes.

CONCLUSION: The femtosecond laser yielded precise flap dimensions with a narrow standard deviation and a high level of safety.”
“Amyloid beta protein (A beta) is the primary component of senile plaques in Alzheimer’s disease brains and its aggregate form is neurotoxic. A beta is

generated through proteolysis of beta-amyloid precursor protein (APP) by two proteases: beta-secretase and gamma-secretase. BACE1, the beta-secretase in vivo and the key rate-limiting enzyme see more that initiates the formation of A beta, is an attractive drug target for AD Staurosporine ic50 therapy. Our previous study demonstrated that BACE1 is ubiquitinated and its degradation and effect on APP cleaving process are mediated by the ubiquitin-proteasome pathway. However, the specific underlying mechanism is still not well defined. In present study, we determined the specific binding sites responsible for the proteasomal degradation of BACE1. Ten fragments of human BACE1 cDNA with each of them containing 1 to 3 Lys codons were cloned,

and HEK293 cells transfected with these recombinant plasmids were treated with specific proteasome inhibitor lactacystin. The protein levels of fragment-3 (Pro(149)-Leu(180)), -4 (IIe(179)-Ser(230)) and -8 (Met(349)-Arg(400)) were significantly increased by lactacystin treatment, and immunocytochemical staining results showed that fragment-3, -4 and -8 proteins were colocalized with ubiquitin. Site-directed mutagenesis at Lys(203) and Lys(382) of BACE1 abolished the proteasomal degradation of BACE1 and affected APP processing at beta site and A beta production. Taken together, our study demonstrated that BACE1 Lys(203) and Lys(382) are essential for its proteasomal degradation, and the results may advance our understanding of regulation of BACE1 and APP processing by the ubiquitin proteasome system in AD pathogenesis and shed new insights on its pharmaceutical potential.