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Dynorphin functions primarily as a kappa opioid receptor agonist, meaning that it acts mainly at kappa opioid receptors. Other opioid peptides include beta-endorphin, met-enkephalin, leu-enkephalin and endomorphins.
The dynorphins, which include dynorphin A, dynorphin B, alpha- and beta-neoendorphin, and big dynorphin, are all the products of a single gene, 'preprodynorphin'.
Dynorphin is produced in many different parts of the brain, including the hypothalamus, the hippocampus and the spinal cord, and has many different physiological actions, depending upon its site of production.
Blocking dynorphin may help alleviate depression.
Recent research has demonstrated that pulmonary delivery may be an effective means of distributing dynorphin derivatives.
It was discovered in the mid-1970s in the laboratory of Avram Goldstein, one of the most important researchers in the field of opioid receptors and endogenous opioid peptides. At first, it was described as an opioid activity present in porcine pituitary extract that proved resistant to chemical degradation by cyanogen bromide, indicating that the activity was not due to the well-known pituitary endogenous opioid peptide beta-endorphin. The molecular identification was achieved by Goldstein in collaboration with the Japanese biochemist, Shinro Tachibana for purification, and M. Hunkapiller and L. Hood, who performed the microsequencing.
|This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Dynorphin". A list of authors is available in Wikipedia.|