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Unique reactive site domains of neuroendocrine isoforms of alpha 1 ‐antichymotrypsin from bovine adrenal medulla and pituitary revealed by molecular cloning
Author(s) -
ShinRong Hwang,
Andrea B. Kohn,
Vivian Hook
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00709-i
Subject(s) - gene isoform , cloning (programming) , adrenal medulla , molecular cloning , alpha (finance) , medulla , endocrinology , pituitary gland , chemistry , microbiology and biotechnology , biology , medicine , biochemistry , peptide sequence , gene , hormone , computer science , catecholamine , programming language , construct validity , nursing , patient satisfaction
Molecular cloning of bovine adrenal medulla (AM) and pituitary (Pit)α 1 ‐antichymotrypsin cDNAs indicated novel isoforms of ACT. The deduced primary sequences indicated that the AM ACT and Pit ACT possess COOH‐terminal reactive‐site domains that are characteristic of serpins (serineproteaseinhibitors). Of high interest was the finding of unique reactive sites within AM ACT and Pit ACT which are predicted to possess Arg as P 1 residue. Arginine as P 1 residue parallels the cleavage specificity of neuroendocrine prohormone processing enzymes cleaving at basic residues. Furthermore, RT‐PCR indicated tissue‐specific expression of AM and Pit ACT mRNAs. The AM and Pit isoforms of ACT may regulate novel target proteases involved in neuroendocrine function.