Prodynorphin Biosynthesis and Posttranslational Processing

Abstract

In 1979 Goldstein and colleagues (Goldstein et al. 1979) reported the characterization and partial sequence of a highly potent endogenous opioid peptide, obtained from pituitary extracts, that contained the amino acid sequence for leu-enkephalin at its amino-terminus (this peptide was found to be 17 amino acids in length when sequencing was completed; Goldstein et al. 1981). They were so impressed with the potency of the peptide that they named it dynorphin, from the Greek prefix dyn-, signifying strength or power. The same year, Kangawa and colleagues (Kangawa and Matsuo 1979) reported the partial sequence of another highly potent opioid peptide, obtained from hypothalamic extracts, containing the sequence for leu-enkephalin at its amino-terminus (this peptide, which they named α-neo-endorphin, was found to be ten amino acids in length when sequencing was completed; Kangawa et al. 1981). Subsequently, several other leu-enkephalin-extended peptides were isolated from brain and pituitary, including dynorphin A 1–8 (Minamino et al. 1980), β-neo-endorphin (Minamino et al. 1981), and dynorphin B (also known as rimorphin; Fischli et al. 1982a,b; Kilpatrick et al. 1982a).