ABSTRACT
PURPOSE: To report unexplained severe central vision loss accompanied by a dense central scotoma as an uncommon complication following epiretinal membrane removal. METHODS: Retrospective, multicentred, case series. RESULTS: Six patients underwent uncomplicated vitrectomy surgery between 2000 and 2007 at four separate retina practices for removal of an epiretinal membrane. Preoperative vision ranged from 20/60 to 20/100, with a median of 20/70. On the first day postoperatively, all patients noted decreased vision ranging from counting fingers to light perception and were found to have a dense central scotoma. Posterior segment examination revealed a white, oedematous macula in all affected eyes. Vision improved minimally during the follow-up period, which ranged from 2 months to 5 years. The final vision ranged from 20/200 to hand movements. No anatomic or physiologic cause for the decreased vision and central scotoma was identified. CONCLUSIONS: While uncommon, severe, permanent, central vision loss accompanied by a dense central scotoma can occur following epiretinal membrane removal and should be considered when assessing the risks and benefits of such surgery.
Subject(s)
Blindness/etiology , Epiretinal Membrane/surgery , Vitrectomy/adverse effects , Aged , Female , Humans , Macular Edema/etiology , Male , Middle Aged , Retrospective Studies , Scotoma/etiologyABSTRACT
Although airbags measurably reduce the overall risk of injury to adults (including eye injury), and death from motor vehicle accidents, injuries attributed to airbag deployment have been reported. To identify reported cases of ocular trauma related to airbag deployment, a MEDLINE search from 1991 to 2000 was performed. A total of 263 injuries in 101 patients were identified. Patient demographics, details of the accident, specific ocular structures injured, and visual outcomes when available where tabulated and analyzed. The most common of these affect the eyes. Damage to the orbit and virtually every ocular and adnexal structure has been seen. Although most injuries are self-limited and do not significantly compromise vision, some result in severe, permanent visual loss. Most common is damage to anterior structures due to either blunt, contusive forces and/or chemical injury. Posterior segment trauma is less common but generally more visually devastating because of the involvement of the retina or optic nerve. Data are not available to determine whether the wearing of eyeglasses or previous intraocular surgery affects the nature, severity, or outcome of these injuries. Awareness of the spectrum of airbag-associated ocular trauma will help physicians recognize these problems early and optimize their management. Data derived from analyses of these injuries will be critical to the development of safer, more effective devices.
Subject(s)
Air Bags/adverse effects , Eye Injuries/epidemiology , Accidents, Traffic , Eye Injuries/etiology , Humans , Risk Factors , United States/epidemiologyABSTRACT
Using genetic and physical assays for protein-protein interactions, we identified a fast isoform of troponin T that binds to dystrophin. Troponin T specifically bound to the first of two highly conserved leucine zipper motifs in the carboxy terminus of dystrophin [1,2]. Single amino acid changes in the zipper predicted to disrupt alpha-helix formation or cause steric hindrance abolished this binding. These data support the hypothesis that dystrophin couples the contractile apparatus to the sarcolemma and indicate that leucine zipper mediated protein-protein interactions are functionally important in the cytoskeleton as well as the nucleus.
Subject(s)
Dystrophin/metabolism , Leucine Zippers , Saccharomyces cerevisiae Proteins , Transcription Factors , Troponin/metabolism , Amino Acid Sequence , Animals , Binding Sites , Blotting, Southern , Conserved Sequence , DNA/chemistry , DNA/metabolism , DNA-Binding Proteins , Dystrophin/chemistry , Dystrophin/genetics , Fungal Proteins/chemistry , Fungal Proteins/genetics , Mice , Mice, Inbred C57BL , Molecular Sequence Data , Peptide Fragments/chemistry , Peptide Fragments/metabolism , Recombinant Fusion Proteins/chemistry , Recombinant Fusion Proteins/metabolism , Repetitive Sequences, Nucleic Acid , Restriction Mapping , Troponin/chemistry , Troponin T , beta-Galactosidase/genetics , beta-Galactosidase/metabolismABSTRACT
The myotonic dystrophy mutation has recently been identified; however, the molecular mechanism of the disease is still unknown. The sequence of the myotonin-protein kinase gene was determined, and messenger RNA spliced forms were identified in various tissues. Antisera were developed for analytical studies. Quantitative reverse transcription-polymerase chain reaction and radioimmunoassay were used to demonstrate that decreased levels of the messenger RNA and protein expression are associated with the adult form of myotonic dystrophy.
Subject(s)
Muscles/metabolism , Myotonic Dystrophy/genetics , Protein Kinases/genetics , Protein Serine-Threonine Kinases , RNA, Messenger/genetics , Adult , Alternative Splicing , Amino Acid Sequence , Base Sequence , Gene Expression , Humans , Molecular Sequence Data , Molecular Weight , Muscles/chemistry , Myotonic Dystrophy/metabolism , Myotonin-Protein Kinase , Polymerase Chain Reaction , Protein Kinases/biosynthesis , Protein Kinases/chemistryABSTRACT
Duchenne's muscular dystrophy (DMD) is an X-linked progressive myopathy caused by a defect in the DMD gene locus. The gene corresponding to the DMD locus produces a 14-kilobase (kb) messenger RNA that codes for a large cytoskeletal membrane protein, dystrophin. DMD and Becker's muscular dystrophy are the consequences of dystrophin mutations. The exact biological function of dystrophin remains unknown but it has been demonstrated that it is localized to the cytoplasmic face of the cell membrane and has direct interaction with several other membrane proteins. We report here the synthesis of a 14-kb full-length complementary DNA for the mouse muscle dystrophin mRNA and the expression of this cDNA in COS cells. The recombinant dystrophin is indistinguishable from mouse muscle dystrophin by western blot analysis with anti-dystrophin antibodies and was shown by an immunofluorescent technique to be localized in the cell membrane. Our successful construction of a functional full-length cDNA opens opportunities for the study of structure and function of dystrophin and provides an opportunity to initiate gene therapy studies.
Subject(s)
Cell Membrane/metabolism , Dystrophin/genetics , Gene Expression , Animals , Bacteriophage lambda/genetics , Base Sequence , Blotting, Western , Cell Line , Cloning, Molecular , DNA/genetics , Fluorescent Antibody Technique , Genetic Vectors , Mice , Molecular Sequence Data , Muscles/chemistry , RNA, Messenger/genetics , Recombinant Proteins/genetics , Restriction Mapping , TransfectionABSTRACT
Complementary DNA clones were isolated that represent the 5' terminal 2.5 kilobases of the murine Duchenne muscular dystrophy (Dmd) messenger RNA (mRNA). Mouse Dmd mRNA was detectable in skeletal and cardiac muscle and at a level approximately 90 percent lower in brain. Dmd mRNA is also present, but at much lower than normal levels, in both the muscle and brain of three different strains of dystrophic mdx mice. The identification of Dmd mRNA in brain raises the possibility of a relation between human Duchenne muscular dystrophy (DMD) gene expression and the mental retardation found in some DMD males. These results also provide evidence that the mdx mutations are allelic variants of mouse Dmd gene mutations.
