Methods: Sixteen shots of 2 x 2 square grids (64 laser spots) were delivered using green (532-nm), yellow (577-nnn) and red (647-nm) lasers to the retinas of mice with mild cataract induced by chloral hydrate (400 mg/kg). Three eyes with clear lenses served as controls.

One week after laser coagulation, the ratio of appropriate burns, defined as coagulation restricted to the outer half of the retina without retinal or choroidal hemorrhage, was investigated histologically. Results: With the green laser, we confirmed only 3.0 +/- 2.0 appropriate burns in eyes with an opaque lens, in contrast to 13.7 +/- 4.0 effective burns in eyes with a clear lens. On the other hand, the yellow and red lasers produced 18 +/- 5.2 AZD9291 clinical trial and 13 +/- 1.5 appropriate burns, respectively, in eyes with an opaque lens. Conclusion: Although all three PSL wavelengths successfully delivered appropriate burns restricted to the outer half of the retina in eyes with an opaque lens, the longer-wavelength yellow and red lasers were significantly more effective than the green laser. PSL may be a treatment option to accompany anti-vascular endothelial growth factor drug therapy. (C) 2014 S. Karger AG, Basel”
“Native fibrinogen is a key blood plasma protein whose main function is to maintain hemostasis

by virtue of producing cross-linked fibrin clots under the influence IPI-549 chemical structure of thrombin and fibrin-stabilizing factor (FXIIIa).

The aim of this study was to investigate mechanisms of impairment of both the molecular structure and the spatial organization of fibrinogen under ozone-induced oxidation. FTIR analysis showed that ozone treatment of the whole fibrinogen molecule results in the growth of hydroxyl, carbonyl, and carboxyl group content. A similar analysis of fibrinogen D and E fragments isolated from the oxidized protein also revealed transformation of distinct important functional groups. In particular, a remarkable decay of N-H groups within the peptide backbone was observed along with a lowering of the content of C-H groups belonging to either the aromatic moieties or the aliphatic chain CH2 and CH3 units. The model experiments performed showed that the rather unexpected selleck compound decay of the aliphatic CH units might be caused by the action of hydroxyl radicals, these being produced in the water solution from ozone. The observed dissimilarities in the shapes of amide I bands of the fibrinogen D and E fragments before and after ozone treatment are interpreted in terms of feasible local conformational changes affecting the secondary structure of the protein. Taken as a whole, the FTIR data suggests that the terminal D fragments of fibrinogen are markedly more susceptible to the ozone-induced oxidation than the central E fragment.