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1.
J Biochem ; 133(2): 211-8, 2003 Feb.
Artículo en Inglés | MEDLINE | ID: mdl-12761184

RESUMEN

The structure and subcellular localization of a number of molecules change during apoptosis. These molecules are recognized by the immune system, leading to the development of autoimmunity when apoptotic cells fail to be effectively cleared by phagocytosis. We searched for such molecules by analyzing sera from 12 individuals who suffered from autoimmune diseases and from 3 patients with amyotrophic lateral sclerosis. One serum sample, designated 681, detected an antigen that fulfilled the above criteria. In Western blotting of lysates of human Jurkat T cells, the 681 antigen appeared as a distinct signal with a molecular mass of 60 kDa in normal cells, and 2 additional signals with faster mobilities were detected in apoptotic cells. The results of subcellular fractionation and immunofluorescence experiments revealed this antigen to be strictly localized in the nucleus of normal cells, but to be translocated to a region near the plasma membrane, to membrane blebs in particular, after the induction of apoptosis. Under conditions in which membrane blebbing was inhibited in apoptotic cells, the antigen still moved away from the nucleus, but its accumulation at the periplasmic region was completely abolished. The apparent partial cleavage and intracellular redistribution of the 681 antigen in apoptotic cells mimics changes previously reported for the nuclear autoantigen La, but the 681 antigen was clearly distinct from La. These results suggest that cleavage-dependent exit from the nucleus during apoptosis is a phenomenon common to nuclear autoantigens.


Asunto(s)
Transporte Activo de Núcleo Celular , Antígenos Nucleares/metabolismo , Apoptosis , Autoantígenos/metabolismo , Membrana Celular/metabolismo , Esclerosis Amiotrófica Lateral/sangre , Antígenos Nucleares/análisis , Antígenos Nucleares/sangre , Autoantígenos/análisis , Autoantígenos/sangre , Enfermedades Autoinmunes/sangre , Fraccionamiento Celular , Membrana Celular/ultraestructura , Humanos , Células Jurkat , Peso Molecular
2.
J Agric Food Chem ; 52(8): 2301-8, 2004 Apr 21.
Artículo en Inglés | MEDLINE | ID: mdl-15080637

RESUMEN

The potential utility of micrometer-sized particles as controlled-release devices for the volatilization of insect pheromones for mating disruption applications is evaluated in this study for two pheromone/model compound systems (codlemone/1-dodecanol and disparlure/1,2-epoxyoctadecane). To expedite the measurement of release rates from these particle devices, two techniques based on thermogravimetric analysis (TGA) have been exploited: isothermal TGA (I-TGA) at elevated temperatures (40-80 degrees C) with N(2) convection and volatilization temperature (VT) by dynamic TGA. A correlation between these two methods has been established. Samples that exhibit a higher VT provide a lower release rate from a particle substrate. Using these techniques, it has been demonstrated that chemical interactions between adsorbed liquids and particle surfaces may play a small role in defining release characteristics under conditions of low surface area, whereas parameters associated with total surface area and micropore structure appear to be much more significant in retarding evaporation for uncoated particles containing an adsorbed liquid. Additional regulation of release rates was achieved by coating the particle systems with water-soluble or water-dispersible polymers. By careful selection of particle porosity and coating composition, it is envisioned that the evaporation rate of pheromones can be tailored to specific insect control applications.


Asunto(s)
Dodecanol/análogos & derivados , Control Biológico de Vectores/instrumentación , Feromonas/administración & dosificación , Alcanos/administración & dosificación , Animales , Dodecanol/administración & dosificación , Microesferas , Mariposas Nocturnas
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