The neuroendocrine chaperone 7B2 can enhance in vitro POMC cleavage by prohormone convertase PC2

FEBS Letters

Martens, Gerard J.M.¹  Braks, Joanna A.M.¹ 

[1] Department of Animal Physiology, University of Nijmegen, Toernooiveld, 6525 ED Nijmegen, The Netherlands

关键词: 7B2;    PC2;    Chaperone;    POMC cleavage;    Xenopus intermediate pituitary;    PC1 and PC2;    prohormone convertase 1 and 2;    ER;    endoplasmic reticulum;    TGN;    trans-Golgi network;    POMC;    proopiomelanocortin;    MSH;    melanophore stimulating hormone;    ACTH;    adrenocorticotropic hormone;    PAGE;    polyacrylamide gel electrophoresis;    SDS;    sodium dodecyl sulphate;    MES;    4-morpholineethanesulfonic acid;   

DOI  :  10.1016/0014-5793(95)00915-V

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We previously showed that the neuroendocrine polypeptide 7B2 transiently interacts with prohormone convertase PC2 in the secretory pathway of neuroendocrine cells. Here we demonstrate that the processed, but not the intact, form of 7B2 can enhance the in vitro cleavage of newly synthesized prohormone proopiomelanocortin (POMC) in lysates of Xenopus intermediate pituitary cells. PC2 is presumably the cleavage enzyme involved since intact 7B2 abolishes the enhancing effect of processed 7B2 and is known to act as a specific inhibitor of PC2. Furthermore, processed 7B2 stimulates in vitro POMC cleavage by immunopurified Xenopus PC2. Our results indicate that 7B2 can display chaperone activity towards PC2.

【 授权许可】

Unknown