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Endomorphin-2 (EM-2) is an endogenous opioid peptide and one of the two endomorphins. [1] It has the amino acid sequence Tyr-Pro-Phe-Phe-NH 2.It is a high affinity, highly selective agonist of the μ-opioid receptor, and along with endomorphin-1 (EM-1), has been proposed to be the actual endogenous ligand of this receptor (that is, rather than the endorphins).
Alternately, endomorphin-2 is predominantly found in the spinal cord, specifically in presynaptic terminals of afferent neurons in the dorsal horn region. It has been found co-localized with calcitonin as well as the pain-conveying neurotransmitter, substance P. Neither endomorphin-1 or 2 have been identified in the amygdala or the hippocampus. [2]
[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]
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There are three well-characterized families of opioid peptides produced by the body: enkephalins, β-endorphin, and dynorphins.The met-enkephalin peptide sequence is coded for by the enkephalin gene; the leu-enkephalin peptide sequence is coded for by both the enkephalin gene and the dynorphin gene. [3]
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The α-neoendorphin is present in greater amounts in the brain than β-neoendorphin. Both are products of the dynorphin gene, which also expresses dynorphin A, dynorphin A-(1-8), and dynorphin B. [2] These opioid neurotransmitters are especially active in Central Nervous System receptors, whose primary function is pain sensation. [3]
Based on the results of dynorphin A 2-13, the authors proposed a mechanism in which dynorphin A activates bradykinin receptors and thus stimulates pain response. [ 8 ] According to this mechanism, dynorphin activates bradykinin receptors, which triggers the release of calcium ions into the cell through voltage-sensitive channels in the cell ...
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