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Endorphins

February 15, 2024

For other uses, see Endorphins (disambiguation).

Endorphins (contracted from endogenous morphine)[1][2][3] are peptides produced in the brain that block the perception of pain and increase feelings of wellbeing. They are produced and stored in the pituitary gland of the brain. Endorphins are endogenous painkillers often produced in the brain and adrenal medulla during physical exercise or orgasm and inhibit pain, muscle cramps, and relieve stress.[4][5][6][7]

History edit

Opioid peptides in the brain were first discovered in 1973 by investigators at the University of Aberdeen, John Hughes and Hans Kosterlitz. They isolated "enkephalins" (from the Greek εγκέφαλος, cerebrum) from pig brain, identified as Met-enkephalin and Leu-enkephalin.[8][9][10][11] This came after the discovery of a receptor that was proposed to produce the pain-relieving analgesic effects of morphine and other opioids, which led Kosterlitz and Hughes to their discovery of the endogenous opioid ligands.[11] Research during this time was focused on the search for a painkiller that did not have the addictive character or overdose risk of morphine.[11][12]

Rabi Simantov and Solomon H. Snyder isolated morphine-like peptides from calf brain.[13] Eric J. Simon, who independently discovered opioid receptors, later termed these peptides as endorphins.[14] This term was essentially assigned to any peptide that demonstrated morphine-like activity.[15] In 1976, Choh Hao Li and David Chung recorded the sequences of α-, β-, and γ-endorphin isolated from camel pituitary glands for their opioid activity.[16][17] Li determined that β-endorphin produced strong analgesic effects.[18] Wilhelm Feldberg and Derek George Smyth in 1977 confirmed this, finding β-endorphin to be more potent than morphine. They also confirmed that its effects were reversed by naloxone, an opioid antagonist.[19]

Studies have subsequently distinguished between enkephalins, endorphins, and endogenously produced morphine,[20][21] which is not a peptide. Opioid peptides are classified based on their precursor propeptide: all endorphins are synthesized from the precursor proopiomelanocortin (POMC), encoded by proenkephalin A, and dynorphins encoded by pre-dynorphin.[12][22]

Etymology edit

The word endorphin is derived from ἔνδον / Greek: éndon meaning "within" (endogenous, ἐνδογενής / Greek: endogenes, "proceeding from within"), and morphine, from Morpheus (Ancient Greek: Μορφεύς, romanized: Morpheús), the god of dreams in the Greek mythology. Thus, endorphin is a contraction of 'endo(genous) (mo)rphin' (morphin being the old spelling of morphine).

Types edit

The class of endorphins consists of three endogenous opioid peptides: α-endorphin, β-endorphin, and γ-endorphin.[23] The endorphins are all synthesized from the precursor protein, proopiomelanocortin, and all contain a Met-enkephalin motif at their N-terminus: Tyr-Gly-Gly-Phe-Met.[12] α-endorphin and γ-endorphin result from proteolytic cleavage of β-endorphin between the Thr(16)-Leu(17) residues and Leu(17)-Phe(18) respectively.[24] α-endorphin has the shortest sequence, and β-endorphin has the longest sequence.

α-endorphin and γ-endorphin are primarily found in the anterior and intermediate pituitary.[25] While β-endorphin is studied for its opioid activity, α-endorphin and γ-endorphin both lack affinity for opiate receptors and thus do not affect the body in the same way that β-endorphin does. Some studies have characterized α-endorphin activity as similar to that of psychostimulants and γ-endorphin activity to that of neuroleptics separately.[25]

Name Sequence Reference
α-endorphin Tyr-Gly-Gly-Phe-Met-Thr-Ser-Glu-Lys-Ser-Gln-Thr-Pro-Leu-Val-Thr-OH [26][12]
β-endorphin 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 [27][28]
γ-endorphin Tyr-Gly-Gly-Phe-Met-Thr-Ser-Glu-Lys-Ser-Gln-Thr-Pro-Leu-Val-Thr-Leu-OH [26][12]

Synthesis edit

Endorphin precursors are primarily produced in the pituitary gland.[29][30][31] All three types of endorphins are fragments of the precursor protein proopiomelanocortin (POMC). At the trans-Golgi network, POMC binds to a membrane-bound protein, carboxypeptidase E (CPE).[32] CPE facilitates POMC transport into immature budding vesicles.[33] In mammals, pro-peptide convertase 1 (PC1) cleaves POMC into adrenocorticotropin (ACTH) and beta-lipotropin (β-LPH).[32] β-LPH, a pituitary hormone with little opiate activity, is then continually fragmented into different peptides, including α-endorphin, β-endorphin, and γ-endorphin.[28][34][35] Peptide convertase 2 (PC2) is responsible for cleaving β-LPH into β-endorphin and γ-lipotropin.[12] Formation of α-endorphin and γ-endorphin results from proteolytic cleavage of β-endorphin.[24]

Regulation edit

Noradrenaline has been shown to increase endorphins production within inflammatory tissues, resulting in an analgesic effect;[36] the stimulation of sympathetic nerves by electro-acupuncture is believed to be the cause of its analgesic effects.[37]

Mechanism of action edit

Endorphins are released from the pituitary gland, typically in response to pain, and can act in both the central nervous system (CNS) and the peripheral nervous system (PNS). In the PNS, β-endorphin is the primary endorphin released from the pituitary gland. Endorphins inhibit transmission of pain signals by binding μ-receptors of peripheral nerves, which block their release of neurotransmitter substance P. The mechanism in the CNS is similar but works by blocking a different neurotransmitter: gamma-aminobutyric acid (GABA). In turn, inhibition of GABA increases the production and release of dopamine, a neurotransmitter associated with reward learning.[27][38]

Functions edit

Endorphins play a major role in the body's inhibitory response to pain. Research has demonstrated that meditation by trained individuals can be used to trigger endorphin release.[39][failed verification] Laughter may also stimulate endorphin production and elevate one's pain threshold.[40]

Endorphin production can be triggered by vigorous aerobic exercise. The release of β-endorphin has been postulated to contribute to the phenomenon known as "runner's high".[41][42] However, several studies have supported the hypothesis that the runner's high is due to the release of endocannabinoids rather than that of endorphins.[43] Endorphins may contribute to the positive effect of exercise on anxiety and depression.[44] The same phenomenon may also play a role in exercise addiction. Regular intense exercise may cause the brain to downregulate the production of endorphins in periods of rest to maintain homeostasis, causing a person to exercise more intensely in order to receive the same feeling.[45]

References edit

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External links edit

February 15, 2024
endorphins, other, uses, disambiguation, contracted, from, endogenous, morphine, peptides, produced, brain, that, block, perception, pain, increase, feelings, wellbeing, they, produced, stored, pituitary, gland, brain, endogenous, painkillers, often, produced,. For other uses see Endorphins disambiguation Endorphins contracted from endogenous morphine 1 2 3 are peptides produced in the brain that block the perception of pain and increase feelings of wellbeing They are produced and stored in the pituitary gland of the brain Endorphins are endogenous painkillers often produced in the brain and adrenal medulla during physical exercise or orgasm and inhibit pain muscle cramps and relieve stress 4 5 6 7 Contents 1 History 2 Etymology 3 Types 4 Synthesis 5 Regulation 6 Mechanism of action 7 Functions 8 References 9 External linksHistory editOpioid peptides in the brain were first discovered in 1973 by investigators at the University of Aberdeen John Hughes and Hans Kosterlitz They isolated enkephalins from the Greek egkefalos cerebrum from pig brain identified as Met enkephalin and Leu enkephalin 8 9 10 11 This came after the discovery of a receptor that was proposed to produce the pain relieving analgesic effects of morphine and other opioids which led Kosterlitz and Hughes to their discovery of the endogenous opioid ligands 11 Research during this time was focused on the search for a painkiller that did not have the addictive character or overdose risk of morphine 11 12 Rabi Simantov and Solomon H Snyder isolated morphine like peptides from calf brain 13 Eric J Simon who independently discovered opioid receptors later termed these peptides as endorphins 14 This term was essentially assigned to any peptide that demonstrated morphine like activity 15 In 1976 Choh Hao Li and David Chung recorded the sequences of a b and g endorphin isolated from camel pituitary glands for their opioid activity 16 17 Li determined that b endorphin produced strong analgesic effects 18 Wilhelm Feldberg and Derek George Smyth in 1977 confirmed this finding b endorphin to be more potent than morphine They also confirmed that its effects were reversed by naloxone an opioid antagonist 19 Studies have subsequently distinguished between enkephalins endorphins and endogenously produced morphine 20 21 which is not a peptide Opioid peptides are classified based on their precursor propeptide all endorphins are synthesized from the precursor proopiomelanocortin POMC encoded by proenkephalin A and dynorphins encoded by pre dynorphin 12 22 Etymology editThe word endorphin is derived from ἔndon Greek endon meaning within endogenous ἐndogenhs Greek endogenes proceeding from within and morphine from Morpheus Ancient Greek Morfeys romanized Morpheus the god of dreams in the Greek mythology Thus endorphin is a contraction of endo genous mo rphin morphin being the old spelling of morphine Types editThis section needs expansion You can help by adding to it December 2018 The class of endorphins consists of three endogenous opioid peptides a endorphin b endorphin and g endorphin 23 The endorphins are all synthesized from the precursor protein proopiomelanocortin and all contain a Met enkephalin motif at their N terminus Tyr Gly Gly Phe Met 12 a endorphin and g endorphin result from proteolytic cleavage of b endorphin between the Thr 16 Leu 17 residues and Leu 17 Phe 18 respectively 24 a endorphin has the shortest sequence and b endorphin has the longest sequence a endorphin and g endorphin are primarily found in the anterior and intermediate pituitary 25 While b endorphin is studied for its opioid activity a endorphin and g endorphin both lack affinity for opiate receptors and thus do not affect the body in the same way that b endorphin does Some studies have characterized a endorphin activity as similar to that of psychostimulants and g endorphin activity to that of neuroleptics separately 25 Name Sequence Referencea endorphin Tyr Gly Gly Phe Met Thr Ser Glu Lys Ser Gln Thr Pro Leu Val Thr OH 26 12 b endorphin 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 27 28 g endorphin Tyr Gly Gly Phe Met Thr Ser Glu Lys Ser Gln Thr Pro Leu Val Thr Leu OH 26 12 Synthesis editEndorphin precursors are primarily produced in the pituitary gland 29 30 31 All three types of endorphins are fragments of the precursor protein proopiomelanocortin POMC At the trans Golgi network POMC binds to a membrane bound protein carboxypeptidase E CPE 32 CPE facilitates POMC transport into immature budding vesicles 33 In mammals pro peptide convertase 1 PC1 cleaves POMC into adrenocorticotropin ACTH and beta lipotropin b LPH 32 b LPH a pituitary hormone with little opiate activity is then continually fragmented into different peptides including a endorphin b endorphin and g endorphin 28 34 35 Peptide convertase 2 PC2 is responsible for cleaving b LPH into b endorphin and g lipotropin 12 Formation of a endorphin and g endorphin results from proteolytic cleavage of b endorphin 24 Regulation editNoradrenaline has been shown to increase endorphins production within inflammatory tissues resulting in an analgesic effect 36 the stimulation of sympathetic nerves by electro acupuncture is believed to be the cause of its analgesic effects 37 Mechanism of action editEndorphins are released from the pituitary gland typically in response to pain and can act in both the central nervous system CNS and the peripheral nervous system PNS In the PNS b endorphin is the primary endorphin released from the pituitary gland Endorphins inhibit transmission of pain signals by binding m receptors of peripheral nerves which block their release of neurotransmitter substance P The mechanism in the CNS is similar but works by blocking a different neurotransmitter gamma aminobutyric acid GABA In turn inhibition of GABA increases the production and release of dopamine a neurotransmitter associated with reward learning 27 38 Functions editEndorphins play a major role in the body s inhibitory response to pain Research has demonstrated that meditation by trained individuals can be used to trigger endorphin release 39 failed verification Laughter may also stimulate endorphin production and elevate one s pain threshold 40 Endorphin production can be triggered by vigorous aerobic exercise The release of b endorphin has been postulated to contribute to the phenomenon known as runner s high 41 42 However several studies have supported the hypothesis that the runner s high is due to the release of endocannabinoids rather than that of endorphins 43 Endorphins may contribute to the positive effect of exercise on anxiety and depression 44 The same phenomenon may also play a role in exercise addiction Regular intense exercise may cause the brain to downregulate the production of endorphins in periods of rest to maintain homeostasis causing a person to exercise more intensely in order to receive the same feeling 45 References edit Stefano GB Ptacek R Kuzelova H Kream RM 1515 Endogenous morphine up to date review 2011 PDF Folia Biologica 58 2 49 56 PMID 22578954 Positive evolutionary pressure has apparently preserved the ability to synthesize chemically authentic morphine albeit in homeopathic concentrations throughout animal phyla The apparently serendipitous finding of an opiate alkaloid sensitive opioid peptide insensitive µ3 opiate receptor subtype expressed by invertebrate immunocytes human blood monocytes macrophage cell lines and human blood granulocytes provided compelling validating evidence for an autonomous role of endogenous morphine as a biologically important cellular signalling molecule Stefano et al 1993 Cruciani et al 1994 Stefano and Scharrer 1994 Makman et al 1995 Human white blood cells have the ability to make and release morphine m receptor IUPHAR BPS Guide to PHARMACOLOGY International Union of Basic and Clinical Pharmacology 15 March 2017 Retrieved 28 December 2017 Comments b Endorphin is the highest potency endogenous ligand Morphine occurs endogenously Poeaknapo C Schmidt J Brandsch M Drager B Zenk MH September 2004 Endogenous formation of morphine in human cells Proceedings of the National Academy of Sciences of the United States of America 101 39 14091 14096 Bibcode 2004PNAS 10114091P doi 10 1073 pnas 0405430101 PMC 521124 PMID 15383669 Pilozzi A Carro C Huang X December 2020 Roles of b Endorphin in Stress Behavior Neuroinflammation and Brain Energy Metabolism International Journal of Molecular Sciences 22 1 338 doi 10 3390 ijms22010338 PMC 7796446 PMID 33396962 Howlett TA Tomlin S Ngahfoong L Rees LH Bullen BA Skrinar GS McArthur JW June 1984 Release of beta endorphin and met enkephalin during exercise in normal women response to training British Medical Journal 288 6435 1950 1952 doi 10 1136 bmj 288 6435 1950 PMC 1442192 PMID 6329401 Goldfarb AH Jamurtas AZ July 1997 Beta endorphin response to exercise An update Sports Medicine 24 1 8 16 doi 10 2165 00007256 199724010 00002 PMID 9257407 S2CID 72824962 Endorphins What They Are and How to Boost Them Cleveland Clinic Retrieved 25 March 2023 Role of endorphins discovered PBS Online A Science Odyssey People and Discoveries Public Broadcasting System 1 January 1998 Retrieved 15 October 2008 Hughes J Smith TW Kosterlitz HW Fothergill LA Morgan BA Morris HR December 1975 Identification of two related pentapeptides from the brain with potent opiate agonist activity Nature 258 5536 577 580 Bibcode 1975Natur 258 577H doi 10 1038 258577a0 PMID 1207728 S2CID 95411 Berezniuk I Fricker LD 2011 Endogenous Opioids In Pasternak GW ed The Opiate Receptors The Receptors Totowa NJ Humana Press pp 93 120 doi 10 1007 978 1 60761 993 2 5 ISBN 978 1 60761 993 2 a b c Corbett AD Henderson G McKnight AT Paterson SJ January 2006 75 years of opioid research the exciting but vain quest for the Holy Grail British Journal of Pharmacology 147 Suppl 1 S153 S162 doi 10 1038 sj bjp 0706435 PMC 1760732 PMID 16402099 a b c d e f Purves D Fitzpatrick D Augustine GJ 2018 Neuroscience 6th ed New York Sunderland ISBN 9781605353807 OCLC 990257568 Simantov R Snyder SH July 1976 Morphine like peptides in mammalian brain isolation structure elucidation and interactions 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1373 PMC 3267132 PMID 21920973 Boecker H Sprenger T Spilker ME Henriksen G Koppenhoefer M Wagner KJ et al November 2008 The runner s high opioidergic mechanisms in the human brain Cerebral Cortex 18 11 2523 2531 doi 10 1093 cercor bhn013 PMID 18296435 Kolata G 27 March 2008 Yes Running Can Make You High The New York Times ISSN 0362 4331 Retrieved 26 May 2016 Reynolds G 10 March 2021 Getting to the Bottom of the Runner s High The New York Times ISSN 0362 4331 Retrieved 16 March 2021 Anderson E Shivakumar G 23 April 2013 Effects of exercise and physical activity on anxiety Frontiers in Psychiatry 4 27 doi 10 3389 fpsyt 2013 00027 PMC 3632802 PMID 23630504 Freimuth M Moniz S Kim SR October 2011 Clarifying exercise addiction differential diagnosis co occurring disorders and phases of addiction International Journal of Environmental Research and Public Health 8 10 4069 4081 doi 10 3390 ijerph8104069 PMC 3210598 PMID 22073029 External links editEndorphins at the U S National Library of Medicine Medical Subject Headings MeSH Retrieved from https en wikipedia org w index php title Endorphins amp oldid 1199060371, wikipedia, wiki, book, books, library,

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