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Hemorphin

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Title: Hemorphin  
Author: World Heritage Encyclopedia
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Subject: Valorphin, Hemorphin-4, Spinorphin, Met-enkephalin, Opioid peptides
Collection: Opioid Peptides
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Hemorphin

Hemorphins are a class of naturally occurring, endogenous opioid peptides which are found in the bloodstream, and are derived from the β-chain of hemoglobin.[1][2] They have antinociceptive effects via activation of the opioid receptors,[2][3] and some may also play a role in blood pressure through inihibition of the angiotensin-converting enzyme (ACE),[4] as well as cause an elevation of endogenous enkephalin levels.[5] Some examples of hemorphins include hemorphin-4, spinorphin, and valorphin.

See also

References

  1. ^ Brantl V, Gramsch C, Lottspeich F, Mertz R, Jaeger KH, Herz A (June 1986). "Novel opioid peptides derived from hemoglobin: hemorphins". European Journal of Pharmacology 125 (2): 309–10.  
  2. ^ a b Davis TP, Gillespie TJ, Porreca F (1989). "Peptide fragments derived from the beta-chain of hemoglobin (hemorphins) are centrally active in vivo". Peptides 10 (4): 747–51.  
  3. ^ Liebmann C, Schrader U, Brantl V (August 1989). "Opioid receptor affinities of the blood-derived tetrapeptides hemorphin and cytochrophin". European Journal of Pharmacology 166 (3): 523–6.  
  4. ^ Lantz I, Glämsta EL, Talbäck L, Nyberg F (August 1991). "Hemorphins derived from hemoglobin have an inhibitory action on angiotensin converting enzyme activity". FEBS Letters 287 (1-2): 39–41.  
  5. ^ Benuck M, Berg MJ, Marks N (1982). "Separate metabolic pathways for Leu-enkephalin and Met-enkephalin-Arg(6)-Phe(7) degradation by rat striatal synaptosomal membranes". Neurochemistry International 4 (5): 389–96.  


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