Changes in accommodative function following small-incision lenticule extraction for high myopia.

PURPOSE: To examine whether the amplitude of accommodation, the accommodative response, and the accommodative facility is affected and correlated with changes in higher-order aberrations for patients with high myopia surgically treated with small-incision lenticule extraction (SMILE). METHODS: 35 highly myopic eyes (myopic spherical equivalent of at least 6 diopters) of 35 patients treated with SMILE were included. Assessments were made before and 3 months after surgery. Donders push-up-method was used to measure the amplitude of accommodation. The accommodative response was assessed using an open-field autorefractor"Grand Seiko WAM-5500" (Grand Seiko Co. Ltd., Hiroshima, Japan) in combination with a Badal optometer and stimuli of accommodation at 0.0, 0.5, 1.25, 2.0, 3.0, and 4.0 D, respectively. Accommodative facility was measured at 40 cm with ±2,00D flipper lenses. All measurements of accommodation were performed monocularly with the refractive error corrected with soft contact lenses. RESULTS: The amplitude of accommodation did not change statistically significantly (mean difference -0.24 D (SD 0.98), 95% CI of mean difference -0.58 D to 0.11 D, paired-sample t(34) = -1.39; P = 0.17). The accommodative responses at 0.0, 0.5, 1.25, 2.0, 3.0, and 4.0 D did not statistically significantly change either (F(6,29) = 1.15; P = .36). Finally, the accommodative facility was also unchanged with a mean difference of 1.11 cycles per minute (SD 5.11, 95% CI of mean difference -0.64 to 2.87, paired-sample t(34) = 1.29; P = 0.21). No clinically significant associations between changes in accommodation and higher-order aberrations were found. CONCLUSIONS: SMILE does not alter the amplitude of accommodation, the accommodative response, nor the accommodative facility for highly myopic patients, and the surgically induced corneal higher-order aberrations do not affect the accommodative function.

Tear film proteins deposited on high water content contact lenses identified with two-dimensional gel electrophoresis and mass spectrometry.

PURPOSE: Tear film proteins adhere to the surface of contact lenses (CLs). While the proteins in the tears have been extensively studied with various proteomic techniques, adhered proteins to CLs are less studied. In this pilot study, we have separated proteins with 2D gel electrophoresis prior to the conventional mass spectrometry (MS) in order to analyse the deposited proteins on hydrogel CLs from myopic patients. METHODS: pHEMA and PVA hydrogel CLs worn by 3 patients for different time lengths were analysed. After wear, the CLs were frozen at -20°C. Proteins were extracted in lysis buffer, separated on 12% polyacrylamide gels and silver-stained. Protein spots were excised and identified with liquid chromatography - tandem MS. RESULTS: Deposited proteins were extracted with a yield of 26-66 µg and separated by 2D gel electrophoresis. The silver-stained gels showed similar protein patterns independent of the patient, hydrogel type and wear time. Seventy-two spots were analysed with MS, representing at least 12 different tear film proteins or protein fragments. CONCLUSIONS: Deposited tear film proteins from a single set of CLs worn for 1 day can successfully be analysed first with 2D gel electrophoresis and subsequently with MS, thus making examination of individual patients possible. The protein composition appeared homogeneous between the test persons which is a necessity for additional comparison analysis. The molecular masses of the identified proteins indicate that protein degradation occurs only as a minor event. Myopic patients were investigated in this pilot study, but the combined techniques can easily be applied to other eye diseases.