RESUMO
OBJECTIVE: To assess the performance of the contact lens fitting software built into anterior segment optical coherence tomography (AS-OCT). METHODS: This retrospective study enrolled patients with keratoconus prescribed with spherical corneal rigid gas-permeable contact lenses based on a contact lens fitting software. Subjects were classified into four subgroups based on corneal morphology: nipple, oval, globus, and marginal type. Software performance was evaluated according to the correlation between the back optical zone radius (BOZR) calculated by the contact lens fitting program and the BOZR of the lens prescribed, and the number of trial lens replacements required.Results:A total of 340 eyes of 254 patients with a mean age of 40.4 ± 13.6 years were included. The oval type was the most common (61.8%), followed by the nipple type (26.2%). Linear regression analysis revealed a significant correlation between the prescribed and the calculated BOZR in all subgroups (R 2 = 0.92, P < 0.01 for the nipple type; R 2 = 0.76, P < 0.01 for the oval type; R 2 = 0.93, P < 0.01 for the globus type; and R 2 = 0.79, P < 0.01 for the marginal type). Furthermore, the globus type had the highest proportion of cases requiring at least one trial lens replacement (36.3%), followed by the nipple group (27.0%). There were no significant differences among the subgroups ( P = 0.14). CONCLUSIONS: In conclusion, our findings reveal that the contact lens fitting software built into AS-OCT may be useful for accurate contact lens prescription for any corneal shape.
Assuntos
Lentes de Contato , Ceratocone , Humanos , Adulto , Pessoa de Meia-Idade , Ceratocone/terapia , Topografia da Córnea/métodos , Tomografia de Coerência Óptica , Estudos Retrospectivos , Ajuste de Prótese/métodos , SoftwareRESUMO
A photo-sensitive amino acid analogue was introduced into an outer membrane lipoprotein, Pal, and then subjected to photo-crosslinking with the lipoprotein-specific ABC transporter LolCDE. Pal crosslinked to LolE but not LolC in vivo despite that both are structurally similar membrane subunits. LolCDE liganded with Pal containing the photo-sensitive amino acid analogue was isolated and subjected to in vitro photo-crosslinking. LolE was found to be the binding site for Pal. ATP binding to LolD decreased the LolE-Pal crosslinking by decreasing their hydrophobic interaction. ATP hydrolysis in the presence of LolA completely abolished the LolE-Pal crosslinking and, concomitantly, generated a new LolA-Pal crosslinked product.
Assuntos
Transportadores de Cassetes de Ligação de ATP/metabolismo , Proteínas da Membrana Bacteriana Externa/metabolismo , Proteínas de Escherichia coli/metabolismo , Complexos Multiproteicos/metabolismo , Subunidades Proteicas/metabolismo , Transportadores de Cassetes de Ligação de ATP/química , Transportadores de Cassetes de Ligação de ATP/genética , Transportadores de Cassetes de Ligação de ATP/isolamento & purificação , Trifosfato de Adenosina/metabolismo , Proteínas da Membrana Bacteriana Externa/química , Proteínas da Membrana Bacteriana Externa/genética , Proteínas da Membrana Bacteriana Externa/isolamento & purificação , Benzofenonas/química , Western Blotting , Cromatografia de Afinidade , Códon de Terminação , Reagentes de Ligações Cruzadas/química , Eletroforese em Gel de Poliacrilamida , Proteínas de Escherichia coli/química , Proteínas de Escherichia coli/genética , Proteínas de Escherichia coli/isolamento & purificação , Interações Hidrofóbicas e Hidrofílicas , Ligantes , Complexos Multiproteicos/química , Complexos Multiproteicos/genética , Complexos Multiproteicos/isolamento & purificação , Mutagênese Sítio-Dirigida , Proteínas Mutantes/química , Proteínas Mutantes/metabolismo , Fenilalanina/análogos & derivados , Fenilalanina/química , Processos Fotoquímicos , Domínios e Motivos de Interação entre Proteínas , Subunidades Proteicas/química , Subunidades Proteicas/genética , Subunidades Proteicas/isolamento & purificação , Proteínas Recombinantes/química , Proteínas Recombinantes/metabolismoRESUMO
In Gram-negative bacteria, lipoproteins are targeted to either the inner or outer membrane depending on their sorting signals. An ABC transporter LolCDE complex in Escherichia coli releases outer membrane-specific lipoproteins. Inner membrane-specific lipoproteins remain in the inner membrane because they each have a LolCDE-avoidance signal and therefore are not released by LolCDE. Only the LolC(A40P) mutation was previously found to cause outer membrane localization of lipoproteins despite their inner membrane-retention signals. Here, we isolated several new LolCDE mutants that cause outer membrane localization of lipoproteins possessing LolCDE-avoidance signals. Mutations were found in all three subunits of LolCDE, including the cytoplasmic ATPase subunit LolD. However, the extent of outer membrane sorting of inner membrane-specific lipoproteins differed depending on the mutation. Based on these observations, the molecular events underlying the recognition of lipoproteins by the LolCDE complex are discussed.
