S-carbocysteine-lysine salt monohydrate and cAMP cause non-additive activation of the cystic fibrosis transmembrane regulator channel in human respiratory epithelium.
FEBS Lett
; 404(1): 11-4, 1997 Mar 03.
Article
en En
| MEDLINE
| ID: mdl-9074627
ABSTRACT
S-Carbocysteine-lysine salt monohydrate (S-CMC-Lys) has been shown to open a Cl- channel in the trachea, thus aiding fluid secretion. The aim of this study was to characterize the channel and the action mechanism on a culture line of human respiratory epithelial cells. The patch-clamp technique (in cell-attached or inside-out configuration) and conventional micro-electrodes were used. The activity and density of a cAMP-dependent Cl- channel, identical to the cystic fibrosis transmembrane regulator (CFTR) channel, proved to be maximally stimulated by 100 microM S-CMC-Lys present in the cAMP-free cell incubation medium for 240-290 min (cell-attached configuration). Subsequent addition of cAMP to the medium did not determine any further activation. S-CMC-Lys acted mostly indirectly as, when placed in direct contact with a membrane patch, activation of the CFTR channel was nil (cytoplasmic side) or limited (external side).
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
8-Bromo Monofosfato de Adenosina Cíclica
/
Carbocisteína
/
Regulador de Conductancia de Transmembrana de Fibrosis Quística
Límite:
Humans
Idioma:
En
Revista:
FEBS Lett
Año:
1997
Tipo del documento:
Article
País de afiliación:
Italia