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Formation[edit | edit source]
β-endorphin is a peptide, 31 amino acids long, resulting from processing of the precursor proopiomelanocortin (POMC). (Note, POMC also gives rise to other peptide hormones, including ACTH ( Adrenocorticotropic hormone ), as well α- and γ-MSH ( Melanocyte-Stimulating Hormone ), resulting from intracellular processing by internal enzymes known as prohormone convertases.)
Function[edit | edit source]
It is an agonist of the opioid receptors, with evidence suggesting it serves as the endogenous ligand of the μ-opioid receptor, the same receptor to which the chemicals extracted from opium, such as morphine and codeine, have their analgesic and addictive effects (indeed, the μ-opioid receptor was named based on its most renowned ligand, morphine).
History[edit | edit source]
β-endorphin was discovered in the 1970s by the prolific laboratory of Avram Goldstein.
Effects[edit | edit source]
It is used as an analgesic in the body to numb or dull pains. That is the reason why we start to feel better immediately after an acute physical trauma even though the symptoms are still present. The reason the pain dulls is because it breaks down bradykinins, which accumulate in response to injury.
- Promotes feeling of well-being
- Decreases pain
- Increases relaxation
[edit | edit source]
Neuropeptides: opioid peptides
|Dynorphin - Endorphin (Beta-endorphin) - Enkephalin|
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