Comparison between clinical results of two diffractive multifocal lenses with the same platform but different additions

PURPOSE: To evaluate visual results with two multifocal diffractive lenses designed with the same platform but with different additions. SETTING: Grupo Innova Ocular clinics. METHODS: A total of 50 eyes from 50 patients were included. Group 1 (n = 25) was implanted with the TECNIS® 1 ZLB +3.25 and group 2 (n = 25) with the TECNIS® 1 ZKB +2.75. Patients were assessed at 24 hours, 1 week and 1 month postoperatively. At surgical discharge, corrected (CDVA) and uncorrected distance visual acuity (UCDVA), near visual acuity (VA) at 25, 40 and 80 cm, visual quality and the defocus curve were measured. RESULTS: Changes in sphere and spherical equivalent were statistically significant (p<0.01) in both groups at 1 week and 1 month compared to preoperative values. In group 1, UCDVA logMAR at 1 month was 0.06 ± 0.02. In group 2, UCDVA at 1 month was 0.03 ± 0.03. In near vision, the TECNIS® 1 ZLB group obtained a VA logMAR of 0.35 ± 0.02 at 25 cm, 0.13 ± 0.02 at 40 cm and 0.27 ± 0.02 at 80 cm, while in the TECNIS® 1 ZKB group, the values were 0.38  ± 0.03, 0.14 ± 0.03 and 0.23 ± 0.06, respectively. No statistically significant differences were found either when results for visual quality were compared. CONCLUSION: Both the TECNIS® 1 ZLB and TECNIS® 1 ZKB are excellent options for obtaining good distance and near vision, in addition to providing good intermediate vision, especially at distances such as those required for working with computers.

Synergistic action of actinoporin isoforms from the same sea anemone species assembled into functionally active heteropores

Among the toxic polypeptides secreted in the venom of sea anemones, actinoporins are pore forming toxins whose toxic activity relies on the formation of oligomeric pores within biological membranes. Intriguingly, actinoporins appear as multigene families which give rise to many protein isoforms in the same individual displaying high sequence identities but large functional differences. However, the evolutionary advantage of producing such similar isotoxins is not fully understood. Here, using sticholysins I and II (StnI and StnII) from the sea anemone Stichodactyla helianthus, it is shown that actinoporin isoforms can potentiate each other’s activity. Through hemolysis and calcein releasing assays, it is revealed that mixtures of StnI and StnII are more lytic than equivalent preparations of the corresponding isolated isoforms. It is then proposed that this synergy is due to the assembly of heteropores since (i) StnI and StnII can be chemically cross-linked at the membrane and (ii) the affinity of sticholysin mixtures for the membrane is increased with respect to any of them acting in isolation, as revealed by isothermal titration calorimetry experiments. These results help to understand the multigene nature of actinoporins and may be extended to other families of toxins that require oligomerization to exert toxicity.

Synergistic Action of Actinoporin Isoforms from the Same Sea Anemone Species Assembled into Functionally Active Heteropores

Among the toxic polypeptides secreted in the venom of sea anemones, actinoporins are the pore-forming toxins whose toxic activity relies on the formation of oligomeric pores within biological membranes. Intriguingly, actinoporins appear as multigene families that give rise to many protein isoforms in the same individual displaying high sequence identities but large functional differences. However, the evolutionary advantage of producing such similar isotoxins is not fully understood. Here,using sticholysins I and II (StnI and StnII) from the sea anemone Stichodactyla helianthus, it is shown that actinoporin isoforms can potentiate each other’s activity. Through hemolysis and calcein releasing assays, it is revealed that mixtures of StnI and StnII are more lytic than equivalent preparations of the corresponding isolated isoforms. It is then proposed that this synergy is due to the assembly of heteropores because (i) StnI and StnII can be chemically cross-linked at the membrane and (ii) the affinity of sticholysin mixtures for the membrane is increased with respect to any of them acting in isolation, as revealed by isothermal titration calorimetry experiments. These results help us understand the multigene nature of actinoporins and may be extended to other families of toxins that require oligomerization to exert toxicity.

Evidence for reciprocal antagonism between motion sensors tuned to coarse and fine features

Early visual processing analyses fine and coarse image features separately. Here we show that motion signals derived from fine and coarse analyses are combined in rather a surprising way: Coarse and fine motion sensors representing the same direction of motion inhibit one another and an imbalance can reverse the motion perceived. Observers judged the direction of motion of patches of filtered two-dimensional noise, centered on 1 and 3 cycles/deg. When both sets of noise were present and only the 3 cycles/deg noise moved, judgments were reversed at short durations. When both sets of noise moved, judgments were correct but sensitivity was impaired. Reversals and impairments occurred both with isotropic noise and with orientation-filtered noise. The reversals and impairments could be simulated in a model of motion sensing by adding a stage in which the outputs of motion sensors tuned to 1 and 3 cycles/deg and the same direction of motion were subtracted from one another. The subtraction model predicted and we confirmed in experiments with orientation-filtered noise that if the 1 cycle/deg noise flickered and the 3 cycles/deg noise moved, the 1 cycle/deg noise appeared to move in the opposite direction to the 3 cycles/deg noise even at long durations.