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Phorbol ester‐induced protein kinase C translocation and lysosomal enzyme release in normal and cystic fibrosis fibroblasts
Author(s) -
Hermelin B.,
Cherqui G.,
Bertrand F.,
Wicek D.,
Paul A.,
Garcia I.,
Picard J.
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80818-4
Subject(s) - chromosomal translocation , cystic fibrosis , phorbol ester , protein kinase c , chemistry , enzyme , protein kinase a , microbiology and biotechnology , biochemistry , biology , medicine , gene
The ability of the tumor‐promoting phorbol ester 4β‐phorbol 12β‐myristate 13α‐acetate (PMA) to induce protein kinase C (PKC) translocation and lysosomal enzyme release was examined in skin fibroblasts from normal subjects and from patients with cystic fibrosis (CF). As compared to normal fibroblasts, those CF exhibited: (i) an increased sensitivity to the effect of PMA on the disappearance of PKC from cytosolic fractions as well as a greater and earlier recovery, in the membrane fraction, of the PKC activity lost in the cytosolic fraction; (ii) an earlier response to PMA for its effect on β‐ N ‐acetylglucosaminidase release. In contrast, the inactive phorbol ester 4α‐phorbol 12,13‐didecanoate (4αPDD) proved ineffective in inducing PKC translocation and β‐ N ‐acetylglucosaminidase release in both normal and CF fibroblasts. The data suggest a defect in the regulation of PKC activity in CF fibroblasts, which may lead to altered secretion.