Phorbol ester‐induced protein kinase C translocation and lysosomal enzyme release in normal and cystic fibrosis fibroblasts

FEBS Letters

Picard, J.²  Wicek, D.²  Cherqui, G.²  Hermelin, B.²  Bertrand, F.²  Paul, A.²  Garcia, I.¹ 

[1] Laboratoire de Biochimie, Hôpital Sainte-Eugénie, 69310 Pierre Benite, France;Laboratoire de Biochimie, INSERM U 181, Faculté de Médecine Saint-Antoine, 75571 Paris Cedex 12, France

关键词: Protein kinase C;    Lysosomal enzyme release;    Phorbol ester;    Cystic fibrosis;    (Skin fibroblast);    BSA;    bovine serum albumin;    CF;    cystic fibrosis;    DMEM;    Dulbecco's modified Eagle's medium;    MUB;    methylumbelliferyl;    PBS;    phosphate-buffered saline;    PKC;    protein kinase C;    PMA;    4β-phorbol 12β-myristate 13α-acetate;    4αPDD;    4α-phorbol 12;    13-didecanoate;    PMSF;    phenylmethylsulfonyl fluoride;    PS;    phosphatidylserine;   

DOI  :  10.1016/0014-5793(88)80818-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown