Opioid Peptide - Opioid Peptides Produced By The Body

Opioid Peptides Produced By The Body

The human genome contains several homologous genes that are known to code for endogenous opioid peptides.

  • The nucleotide sequence of the human gene for proopiomelanocortin (POMC) was characterized in 1980. The POMC gene codes for endogenous opiates such as β-endorphin and gamma-endorphin. The peptides with opiate activity that are derived from proopiomelanocortin comprise the class of endogenous opioid peptides called "endorphins".
  • The human gene for enkephalins was isolated and its sequence described in 1982.
  • The human gene for dynorphins (originally called the "Enkephalin B" gene because of sequence similarity to the enkephalin gene) was isolated and its sequence described in 1983.
  • The PNOC gene encoding prepronociceptin, which is cleaved into nociceptin and potentially two additional neuropeptides.
  • Adrenorphin, amidorphin, and leumorphin were discovered in the 1980s.
  • Opiorphin and spinorphin, enkephalinase inhibitors (i.e., prevent the metabolism of enkephalins).
  • Hemorphins, hemoglobin-derived opioid peptides, including hemorphin-4, valorphin, and spinorphin, among others.

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