Neurogenic dry eye associated with intravitreal injection of anti-VEGF agents.

PURPOSE: To report a case of neurogenic dry eye (NDE) that developed after intravitreal ranibizumab injection (IVR). CASE REPORT: A 71-year-old woman had a history of cataract phacoemulsification and intraocular lens (IOL) implantation, Nd:YAG laser posterior capsulotomy and femtosecond laser-assisted laser in situ keratomileusis (FS-LASIK). Aneurysmal dilatation of the inferior temporal retina was found in the left fundus, which was diagnosed as retinal aneurysm, and intravitreal ranibizumab injection was administered. Dry eye was found in the left eye after the first injection. After the second injection, the patient developed severe dry eye with left eye dryness, photophobia, irritation, and blurred vision. The tear film breakup time (TBUT) value was 3 s, the Schirmer test value was 2 mm/5 min, corneal fluorescein staining (CFS) showed diffuse patellar staining of the corneal epithelium with a staining area of >50% and irregular staining at the edge of the corneal flap, and the corneal touch threshold value in the filament length was 1.5 cm in the left eye. CONCLUSIONS: Patients with a history of intraocular lens implantation, Nd:YAG laser posterior capsulotomy, and femtosecond laser-assisted laser in situ keratomileusis surgery may have increased drug permeability due to an increased concentration of anti-VEGF drugs in the aqueous layer and thinning of the stromal layer of the cornea. The corneal subepithelial nerve repair mechanism was destroyed, causing neurogenic dry eye.

Improving Catalytic Activity, Acid-Tolerance, and Thermal Stability of Glutathione Peroxidase by Systematic Site-Directed Selenocysteine Incorporation.

Glutathione peroxidase (GPx) is an important antioxidant enzyme. Selenocysteine (Sec)-containing GPxs (Sec-GPxs) are usually superior to their conventional cysteine-containing counterparts (Cys-GPxs), which make up the majority of the natural GPxs but display unsuitable activity and stability for industrial applications. This study first heterologously expressed and characterized a Cys-GPx from Lactococcus lactis (LlGPx), systematically exchanged all the three Cys to Sec and introduced an extra Sec. The results showed that the insertion of Sec at the active site could effectively increase the enzyme activity and confer a lower optimal pH value on the mutants. The double mutant C36U/L157U increased by 2.65 times (5.12 U/mg). The thermal stability of the C81U mutant was significantly improved. These results suggest that site-directed Sec incorporation can effectively improve the enzymatic properties of LlGPx, which may be also used for the protein engineering of other industrial enzymes containing catalytic or other functional cysteine residues.