The effect of pepstatin A, an inhibitor of the pro‐opiomelanocortin (POMC)‐converting enzyme, on POMC processing in mouse intermediate pituitary

FEBS Letters

Loh, Y.Peng¹ 

[1] Section on Cellular Neurobiology, Laboratory of Neurochemistry and Neuroimmunology, National Insitute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA

关键词: Prohormone processing enzyme;    Intermediate lobe;    ACTH/endorphin prohormone;    Aspartyl protease;    Protease inhibitor;    POMC;    pro-opiomelanocortin;    ACTH;    adrenocorticotropin;    α-MSH;    α-melanotropin or N α-acetyl-ACTH1–13 NH2;    PCE;    pro-opiomelanocortin-converting enzyme;    DMSO;    dimethyl sulfoxide;   

DOI  :  10.1016/0014-5793(88)80244-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

In our previous studies, we have purified a unique, paired basic residue-specific, prohormone-converting enzyme from pituitary intermediate lobe secretory vesicles. This enzyme, an aspartyl protease, was shown to cleave the intermediate lobe prohormone, pro-opiomelanocortin (POMC), to adrenocorticotropin, β-endorphin and a 16 kDa NH₂-terminal glycopeptide, in vitro [(1985) J. Biol. Chem. 260, 7194–7205]. To provide some evidence that this enzyme plays a role in prohormone conversion in the intact cell, the ability of pepstatin A, an aspartyl protease inhibitor, to block POMC processing in the mouse intermediate pituitary was investigated. By the use of a radioactive pulse-chase paradigm, [³H]POMC processing was found to be inhibited by 36.4% in pepstatin A-treated intermediate lobes. This result is consistent with the inactivation of pro-opiomelanocortin-converting enzyme by pepstatin A in the intact pituitary and further supports a role of this enzyme in POMC processing in vivo.

【 授权许可】

Unknown