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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. [1] It is one of three endorphins that are produced in humans, the others of which include α-endorphin and γ-endorphin .
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.
Prodynorphin, also known as proenkephalin B, is an opioid polypeptide hormone involved with chemical signal transduction and cell communication. The gene for prodynorphin is expressed in the endometrium and the striatum , and its gene map locus is 20pter-p12.
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]
Endogenous amines are produced in many different tissues (for example: adrenaline in adrenal medulla or histamine in mast cells and liver). Serotonin, an endogenous amine, is a neurotransmitter derived from the amino acid tryptophan. Serotonin is involved in regulating mood, sleep, appetite, and sexuality. [9]
Well, according to Wise, the brain is actually the most powerful sex organ there is—namely because genital stimulation produces so much muscle and nerve information that a tremendous boost in ...
Its receptor – the neurokinin type 1 – is distributed over cytoplasmic membranes of many cell types (neurons, glia, endothelia of capillaries and lymphatics, fibroblasts, stem cells, white blood cells) in many tissues and organs. SP amplifies or excites most cellular processes. [16] [17]
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 ...