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.