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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).
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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]
The most important regulatory proteins for the MOR are the β-arrestins arrestin beta 1 and arrestin beta 2, [25] [26] [27] and the RGS proteins RGS4, RGS9-2, RGS14, and RGSZ2. [ 28 ] [ 29 ] Long-term or high-dose use of opioids may also lead to additional mechanisms of tolerance becoming involved.
All G protein α sub-units contain palmitate, which is a 16-carbon saturated fatty acid, that is attached near the N-terminus through a labile, reversible thioester linkage to a cysteine amino acid. It is this palmitoylation that allows the G protein to interact with membrane phospholipids due to the hydrophobic nature of the alpha sub-units.
This supersensitivity of α 2-adrenoceptor was postulated to decrease locus coeruleus (the main projection site of NA in the central nervous system, CNS) NA activity leading to depression. In addition to enhancing NA release, α 2 -adrenoceptor antagonism also increases serotonergic neurotransmission due to blockade of α 2 -adrenoceptors ...
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]
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