Chromogranin A can act as a reversible processing enzyme inhibitor. Evidence from the inhibition of the IRCM-serine protease 1 cleavage of pro-enkephalin and ACTH at pairs of basic amino acids |
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Authors: | N G Seidah G N Hendy J Hamelin J Paquin C Lazure K M Metters J Rossier M Chrétien |
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Institution: | 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;2. Departments of Medicine, Royal Victoria Hospital and McGill University, Montreal, Quebec H3A 1A1, Canada;3. Laboratoire de Physiologie Nerveuse, CNRS, 91190 Gif-sur-Yvette, France |
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Abstract: | 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 synenkephalin-containing 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. |
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