RESUMEN
The ionic composition of the airway surface liquid (ASL) in healthy individuals and in patients with cystic fibrosis (CF) has been debated. Ion transport properties of the upper airway epithelium are similar to those of the lower airways and it is easier to collect nasal ASL from the nose. ASL was collected with ion exchange beads, and the elemental composition of nasal fluid was determined by X-ray microanalysis in healthy subjects, CF patients, CF heterozygotes, patients with rhinitis, and with primary ciliary dyskinesia (PCD). In healthy subjects, the ionic concentrations were approximately isotonic. In CF patients, CF heterozygotes, rhinitis, and PCD patients, [Na] and [Cl] were significantly higher compared when compared with those in controls. [K] was significantly higher in CF and PCD patients compared with that in controls. Severely affected CF patients had higher ionic concentrations in their nasal ASL than in patients with mild or moderate symptoms. Female CF patients had higher levels of Na, Cl, and K than male patients. As higher salt concentrations in the ASL are also found in other patients with airway diseases involving chronic inflammation, it appears likely that inflammation-induced epithelial damage is important in determining the ionic composition of the ASL.
Asunto(s)
Líquidos Corporales/química , Fibrosis Quística/metabolismo , Síndrome de Kartagener/metabolismo , Líquido del Lavado Nasal/química , Mucosa Nasal/química , Rinitis/metabolismo , Adolescente , Adulto , Niño , Cloro/análisis , Microanálisis por Sonda Electrónica , Femenino , Heterocigoto , Humanos , Masculino , Persona de Mediana Edad , Potasio/análisis , Sales (Química)/análisis , Factores Sexuales , Sodio/análisisRESUMEN
The distribution of the inhibitory glycine receptor was studied in rat and human cerebral cortex using a monoclonal antibody (MAb 4a) directed against the ligand-binding subunit. Significant amounts of glycine receptor antigen were found in forebrain structures such as caudatum and neocortex, although cortical levels were significantly below those seen in spinal cord. Immunohistochemically, glycine receptors were preferentially localized to the apical dendrites of pyramidal neurons in layers III and V. Ultrastructurally, these sites corresponded to synaptic neuronal contacts. Immunoreactivity was found in neuronal perikarya, dendrites and postsynaptic membranes which may correspond to sites of intracellular synthesis, transport and membrane incorporation of the glycine receptor. These immunological data corroborate previous pharmacological studies suggesting the existence of glycinergic transmission in mammalian cerebral cortex.