Consistent pattern in positional instability of polyfocal full-optics accommodative IOL.

PURPOSE: We describe cases of dislocation or subluxation of the WIOL-CF® polyfocal full-optics intraocular lens (IOL) and suggest a consistent pattern and possible mechanism for the IOL instability. METHODS: This is a retrospective case series of five consecutive eyes in three patients with WIOL-CF® IOL instability at Keimyung University Dongsan Medical Center and Kimkisan Eye Center from 2012 to 2014. The medical records and ocular exam data for these patients were analyzed. RESULTS: A 50-year-old male had uneventful phacoemulsification in both eyes with WIOL-CF® IOL implantation. At 27 months after surgery, the patient was referred to our clinic with a dislocated IOL in the left eye. The IOL in the right eye was dislocated in the same pattern 38 months after cataract surgery. Another 50-year-old male, who had phacoemulsification and WIOL-CF® IOL implantation in both eyes, was referred to our clinic following diagnosis of a subluxated IOL. Both IOLs were well centered; however, the infranasal aspect of the IOLs tilted posteriorly, and the supratemporal portion the IOLs tilted anteriorly, with overlying iris atrophy in a symmetric pattern. The inferonasal continuous curvilinear capsulorrhexis (CCC) edge was dragged superotemporally, and the supratemporal CCC edge was identified on the posterior surface of the IOL. A 16-year-old female had uneventful phacoemulsification and WIOL-CF® IOL implantation to treat a cataract in the right eye, and 3 years later, the IOL tilted with the same pattern as the previous case. CONCLUSIONS: Years after uncomplicated phacoemulsification, an implanted WIOL-CF® IOL may tilt and dislocate in the absence of trauma, in a consistent and characteristic pattern.

Beta ig-h3 promotes renal proximal tubular epithelial cell adhesion, migration and proliferation through the interaction with alpha3beta1 integrin.

Betaig-h3 (betaig-h3) is a secretory protein composed of fasciclin I-like repeats containing sequences that allows binding of integrins and glycosaminoglycans in vivo. Expression of betaig-h3 is responsive to TGF-Beta and the protein is found to be associated with extracellular matrix (ECM) molecules, implicating betaig-h3 as an ECM adhesive protein of developmental processes. We previously observed predominant expression of betaig-h3 expression in the basement membrane of proximal tubules of kidney. In this study, the physiological relevance of such localized expression of betaig-h3 was examined in the renal proximal tubular epithelial cells (RPTEC). RPTEC constitutively expressed betaig-h3 and the expression was dramatically induced by exogenous TGF-Beta1 treatment. betaig-h3 and its second and fourth FAS1 domain were able to mediate RPTEC adhesion, spreading and migration. Two known alpha3beta1 integrin-interaction motifs including aspartatic acid and isoleucine residues, NKDIL and EPDIM in betaig-h3 were responsible to mediate RPTEC adhesion, spreading, and migration. By using specific antibodies against integrins, we confirmed that alpha3beta1 integrin mediates the adhesion and migration of RPTECs on betaig-h3. In addition, it also enhanced proliferation of RPTECs through NKDIL and EPDIM. These results indicate that betaig-h3 mediates adhesion, spreading, migration and proliferation of RPTECs through the interaction with alpha3beta1 integrin and is intimately involved in the maintenance and the regeneration of renal proximal tubular epithelium.

Alteration of cadherin in dexamethasone-induced cataract organ-cultured rat lens.

PURPOSE: A side effect associated with long-term treatment of various diseases with steroids is a high incidence of posterior subcapsular cataracts (PSC). To understand the mechanism underlying steroid-induced cataract, the cultured lens model was developed, and the expression of potential candidate proteins during opacity formation was examined. METHOD: Rat lenses were carefully dissected from the surrounding ocular tissue and incubated in medium 199. Dexamethasone was then added to the medium. The lenses were cultured for 7 days and photographed daily to record the development of opacity. Differential expression of candidate proteins was examined by Western blot analysis. RESULT: Various degrees of opacity were observed on the posterior subcapsular region as early as 5 days after incubation with dexamethasone. The expression of E-cadherin and N-cadherin decreased in the cultured rat lenses during the development of opacity. CONCLUSIONS: The pattern of opacity that developed in cultured rat lenses closely resembled that observed in patients with PSC. The results suggest that the decrease in E-cadherin plays a role in the formation of steroid-induced cataract.

Molecular properties of wild-type and mutant betaIG-H3 proteins.

PURPOSE: BetaIG-H3 is a TGF-beta-induced cell adhesion molecule, the mutations of which are responsible for a group of 5q31-linked corneal dystrophies. The characteristic findings in these diseases are accumulation of protein deposits of different ultrastructures. To understand the mechanisms of protein deposits in 5q31-linked corneal dystrophies, the molecular properties of betaIG-H3 and the effects of mutation on these properties were studied in vitro. METHODS: Substitution mutations were generated by two-step PCR. Wild-type and mutant recombinant betaIG-H3 proteins were raised in Escherichia coli. For structural study, nondenaturing gel electrophoresis, cross-linking experiments, and electron microscopy examination were performed. A solid-phase interaction assay was performed for the interaction of betaIG-H3 with other matrix proteins. Wild-type and mutant betaIG-H3 cDNAs were cloned into a mammalian expression vector and overexpressed in the corneal epithelial cells by transient transfection. Immunoprecipitation and immunoblot analysis were performed with an antibody against human betaIG-H3. Cell adhesion was assayed by measuring enzyme activities of N-acetyl-beta-D-glucosaminidase. RESULTS: The recombinant betaIG-H3 protein self-assembled to form multimeric bands and appeared to have a fibrillar structure. Solid-phase in vitro interaction assay showed that it bound strongly to type I collagen, fibronectin, and laminin; moderately to collagen type II and VI; and minimally to collagen type IV. Five recombinant mutant forms of betaIG-H3 (R124C, R124H, R124L, R555W, and R555Q) commonly found in 5q31-linked corneal dystrophies did not significantly affect the fibrillar structure, interactions with other extracellular matrix proteins, or adhesion activity in cultured corneal epithelial cells. In addition, the mutations apparently produced degradation products similar to those of wild-type betaIG-H3. CONCLUSIONS: BetaIG-H3 polymerizes to form a fibrillar structure and strongly interacts with type I collagen, laminin, and fibronectin. Mutations found in the 5q31-linked corneal dystrophies do not significantly affect these properties. The results suggest that mutant forms of betaIG-H3 may require other cornea-specific factors, to form the abnormal accumulations in 5q31-linked corneal dystrophies.