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Título: Novel insight into current models of NADPH oxidase regulation, assembly and localization in human polymorphonuclear leukocytes
Fecha de publicación: 1999
Editorial: Murcia : F. Hernández
ISSN: 0213-3911
Materias relacionadas: CDU::6 - Ciencias aplicadas::61 - Medicina
Palabras clave: Cytochemistry
Degranulation
Resumen: We review herein the definition of the NADPH oxidase-activating site in human neutrophils and eosinophils, together with the new biochemical findings of the assembly of NADPH oxidase components and the signal transduction for the activation of NADPH oxidase. The activation of this enzyme is associated with multiple interrelated signaling pathways. Upon cell stimulation, the second messengers act on the assembly of NADPH oxidase components. The cytosolic components are first phosphorylated, and then associated with the membrane components. Small GTP-binding proteins and cytoskeletal components also participate in the activation of the NADPH oxidase. The cytochemical findings demonstrate that the superoxide generated by NADPH oxidase activity is initially localized in distinct types of intracellular granules, and not at the plasma membrane as previously believed. Thus, the assembly of NADPH oxidase components possibly occurs at the limiting membrane of the intracellular compartments. The oxidant-producing compartments mobilize and become associated with the plasma membrane upon cell stimulation with soluble stimulants, or fuse to phagosomes upon stimulation with particulate stimulants. Accordingly, superoxide is released to the extracellular space and into phagosomes in proportion to the oxidant-producing intracellular granule association with the plasma membrane and with the phagosomal membrane, respectively.
Autor/es principal/es: Kobayashi, T.
Seguchi, H.
Publicado en: Histology and histopathology
URI: http://hdl.handle.net/10201/19256
Tipo de documento: info:eu-repo/semantics/article
Número páginas / Extensión: 14
Derechos: info:eu-repo/semantics/openAccess
Aparece en las colecciones:Vol.14, nº 4 (1999)



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