Chromogranin A can act as a reversible processing enzyme inhibitor

FEBS Letters

Rossier, J.¹  Lazure, C.¹  Metters, K.M.¹  Hendy, G.N.¹  Chrétien, M.¹  Hamelin, J.¹  Seidah, N.G.¹  Paquin, J.¹ 

[1] Laboratories of Biochemical and Molecular Neuroendocrinology, Clinical Research Institute of Montreal (Affiliated with the University of Montreal), 110 Pine Avenue West, Montreal, Quebec H2W 1R7, Canada

关键词: Chromogranin;    Processing enzyme;    Enzyme inhibitor;    Pro-enkephalin;    IRCM-serine protease 1;    Pro-opiomelanocortin;   

DOI  :  10.1016/0014-5793(87)81425-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Bovine parathyroid chromogranin A inhibits the cleavage of Z-Ala-Lys-Arg-AMC by either trypsin or IRCM-serine protease 1 (IRCM-SP1), a putative novel processing enzyme originally isolated from porcine pituitary anterior and neurointermediate lobes. On larger substrates, chromogranin A is a reversible competitive inhibitor of the cleavage at pairs of basic amino acids by IRCM-SP1. The substrates tested included pituitary ACTH and adrenal medulla pro-enkephalin-derived peptides such as the 8.6 kDa synenkephalincontaining precursor and peptide B. Chromogranin A is itself selectively processed by IRCM-SP1, and ACTH was shown to compete for such cleavage. These data suggest that chromogranins as a class of acidic proteins could participate in the tissue-specific processing of pro-hormones.

【 授权许可】

Unknown