RESUMEN
Ocular angiogenesis is responsible for the majority of irreversible blindness in the developed world [1]. This debilitating complication affects all age groups and characterizes such diverse and widespread diseases as trachoma, retinopathy of prematurity, diabetic retinopathy, neovascular glaucoma and age-related macular degeneration. Although numerous relatively rare conditions also exhibit ocular angiogenesis, the aim of this review will be to briefly summarize our current knowledge regarding the clinical and laboratory findings of the most epidemiologically significant diseases. We will also describe current concepts regarding the pathogenesis of ocular angiogenesis. In this review the term 'neovascularization', which is more prevalent in the ophthalmic literature, will be used to describe the development of pathological new vessels and should be considered synonymous with 'angiogenesis'.
RESUMEN
The bronchopulmonary cellular immunological response to repeated intratracheal inoculation of aluminum chlorhydrate, sodium zirconium lactate, and zirconium aluminum glycine was examined in rabbits. Results of a dose-response experiment using 0.1, 1.0, and 10.0-mg intratracheal inoculations of each metallic salt demonstrated significant bronchopulmonary histopathology in the 10.0-mg dose-response groups only. Acute lesions were histologically characterized by an inflammatory response centered around respiratory bronchioles. Although epithelioid cell formation was evident in 10.0 mg of aluminum salt (aluminum chlorhydrate and zirconium aluminum glycine) -injected animals, no well-defined granulomas characterized by an orderly arrangement of epithelioid cells, lymphocytes, and giant cells were evident in any of the experimental groups employed. All three metallic salts induced "activated" bronchopulmonary macrophages as determined by an in vitro phagocytic assay. This activation was likely nonimmunological since no measurable differences were observed in metallic salt-induced delayed skin reactivity or migration inhibition factor production between inoculated and uninoculated rabbits. The above observations suggest that aluminum and zirconium salts administered in comparatively high dosage via the respiratory tract route can induce respiratory bronchiolitis and activation of alveolar macrophages in the absence of demonstrable delayed hypersensitivity.
Asunto(s)
Aluminio/inmunología , Bronquios/inmunología , Inmunidad Celular , Pulmón/inmunología , Circonio/inmunología , Aluminio/administración & dosificación , Animales , Antígenos , Bronquios/patología , Femenino , Pulmón/patología , Factores Inhibidores de la Migración de Macrófagos/inmunología , Macrófagos/inmunología , Fagocitosis , Conejos , Tráquea , Circonio/administración & dosificaciónRESUMEN
Plasmalogenase catalyzes the hydrolysis of ethanolamine plasmalogens to long-chain aldehydes and 2-acyl-sn-glycero-3-phosphoethanolamines. During development, plasmalogenase activity parallels myelination. The enzyme is most concentrated within oligodendroglial cells and is absent from myelin. The normal function of plasmalogenase in white matter may be related to its specificity for plasmalogens that contain most of the thromboxane and prostaglandin precursors. Plasmalogenase activities are elevated in demyelinating CNS tissues including canine white matter with lesions due to distemper virus. Elevated plasmalogenase activity precedes cellular invasion and lysosomal activation as indicated by beta-glucuronidase, acid proteinase and neutral proteinase activities. The elevation of plasmalogenase activity was 4.9-fold greater than normal in an early demyelinating lesion caused by the Snyder-Hill strain of distemper virus. Phospholipases acting on phosphatidyl ethanolamine were not activated in this tissue and have activities much lower than plasmalogenase in control tissues. Plasmalogenase activities are also elevated after intracerebral injections of complement-dependent anti-myelin antibody and after ischemia. Plasmalogenase acting on the oligodendrocyte plasma membrane may be responsible for necrosis of the oligodendrocyte that results in demyelination.