Elsevier

Life Sciences

Volume 16, Issue 12, 15 June 1975, Pages 1777-1782
Life Sciences

A peptide-like substance from pituitary that acts like morphine
Purification and properties

https://doi.org/10.1016/0024-3205(75)90272-6Get rights and content

Abstract

We have demonstrated the existence of a peptide-like opioid in bovine and porcine pituitary, and determined some of its properties. It is an opioid agonist on the guinea pig myenteric plexus-longitudinal muscle preparation, and on the mouse vas deferens, and it binds to opiate receptors in homogenates of guinea pig brain. Its physiologic role and its possible presence in hypothalamic or other brain regions remain to be determined.

References (11)

  • W.A. Krivoy et al.

    Eur. J. Pharmacol.

    (1974)
  • E. Zimmermann et al.

    Prog. Brain Res.

    (1973)
  • O.H. Lowry et al.

    J. Biol. Chem.

    (1951)
  • H. Teschemacher et al.

    Life Sci.

    (1975)
  • W.A. Krivoy et al.
There are more references available in the full text version of this article.

Cited by (198)

  • Dynorphin and its role in alcohol use disorder

    2020, Brain Research
    Citation Excerpt :

    The discovery of Dynorphin B (13 amino acids) or rimorphin followed, in conjunction with the c-terminus extended form of dynorphin B, Big Dynorphin and leumorphin (Fischli et al., 1982; Kilpatrick et al., 1982; see Ferré et al., 2019 for sequences). This was preceded by discovery of the endogenous morphine-like substances and opioid peptides methionine and leucine enkephalin (Cox et al., 1976, 1975; Goldstein et al., 1971; Hughes et al., 1975; Li and Chung, 1976; Teschemacher et al., 1975; Tperenius and Wahlström, 1975). This era has been fondly described as the ‘golden era of neuropeptide discovery’ (Chavkin, 2013) a critical period during which our understanding of neuropeptide function was enhanced following new methods of neuropeptide detection and purification.

  • Structure and dynamics of dynorphin peptide and its receptor

    2019, Vitamins and Hormones
    Citation Excerpt :

    Dynorphin is an endogenous neuropeptide first isolated from porcine pituitary (Cox, Opheim, Teachemacher, & Goldstein, 1975) with a particularly potent opioid activity (Goldstein, Tachibana, Lowney, Hunkapiller, & Hood, 1979).

  • Endogenous morphine and its metabolites in mammals: History, synthesis, localization and perspectives

    2013, Neuroscience
    Citation Excerpt :

    These opioid receptors have seven transmembrane domains coupled to G proteins (for review: Kieffer and Evans, 2002, 2009; Trescot et al., 2008; Dietis et al., 2011; Al-Hasani and Bruchas, 2012; Feng et al., 2012). The presence of opioid receptors has led to the characterization of several endogenous ligands called opioids due to their peptidic nature: enkephalins (Hughes et al., 1975a,b; Simantov and Snyder, 1976), β-endorphin (Bradbury et al., 1976; Graf et al., 1976; Lazarus et al., 1976; Li and Chung, 1976; Li et al., 1976), dynorphin (Cox et al., 1975; Goldstein et al., 1979; Lowney et al., 1979), nociceptin/orphanin FQ (Meunier et al., 1995; Reinscheid et al., 1995) and endomorphins (Hackler et al., 1997; Zadina et al., 1997). In addition to endogenous opioid peptides, endogenous morphine-like molecules, which are known as endogenous opiates due to their alkaloid nature have been discovered (Gintzler et al., 1976a,b; Blume et al., 1977; Shorr et al., 1978).

  • Suicide neurobiology

    2009, Progress in Neurobiology
  • Dynorphin a

    2007, xPharm: The Comprehensive Pharmacology Reference
View all citing articles on Scopus
View full text