
beta-endorphin
Sign in to saveAlso known as ß-endorphin, POMC(237-267)
β-Endorphin (beta-endorphin) is an endogenous opioid neuropeptide and peptide hormone that is produced in certain neurons within the central nervous system and peripheral nervous system. It is one of three endorphins that are produced in humans, the others being α-endorphin and γ-endorphin.
Research
9,780 papers- Beta-endorphin: cytokine and neuropeptide.Immunological reviews · 1991
- Beta-endorphin response to exercise. An update.Sports medicine (Auckland, N.Z.) · 1997
- [Beta-endorphin].Nihon rinsho. Japanese journal of clinical medicine · 1999
- Beta-endorphin in the brain. A role in nociception.Acta anaesthesiologica Scandinavica · 1997
- Peripheral beta-endorphin and pain modulation.Anesthesia progress · 1991
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Wikidata facts
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- chemical formula
- C₁₅₈H₂₅₁N₃₉O₄₆S
Sources (3)
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Article
11 sectionsContents
- Formation and structure
- Function and effects
- Opioid agonist
- Pain management
- Exercise
- Sunlight
- Addiction
- Mechanism of action
- History
- References
- External links
β-Endorphin (beta-endorphin) is an endogenous opioid neuropeptide and peptide hormone that is produced in certain neurons within the central nervous system and peripheral nervous system. It is one of three endorphins that are produced in humans, the others being α-endorphin and γ-endorphin.
There are multiple forms of β-endorphins with the full sequence of Tyr-Gly-Gly-Phe-Met-Thr-Ser-Glu-Lys-Ser-Gln-Thr-Pro-Leu-Val-Thr-Leu-Phe-Lys-Asn-Ala-Ile-Ile-Lys-Asn-Ala-Tyr-Lys-Lys-Gly-Glu (31 amino acids) denoted as β-endorphin(1-31) and variants truncated to the first 26 and 27 amino acids as β-endorphin(1-26) and β-endorphin(1-27). However, β-endorphin(1-31) is the only form that possess a potent analgesic effect and it is the primary form located in the anterior pituitary gland, and regions such as the hypothalamus, midbrain, and amygdala. The first 16 amino acids are identical to α-endorphin. β-Endorphin is considered to be a part of the endogenous opioid and endorphin classes of neuropeptides; all of the established endogenous opioid peptides contain the same N-terminal amino acid sequence, Tyr-Gly-Gly-Phe, followed by either or .