The greatest binding potential exists between the beta-endorphins and the mu-receptors. Opioid receptors are broken down into four primary classes of G protein-coupled receptors: mu-receptors, delta-receptors, kappa-receptors, and nociceptin receptors. In the PNS, the perception of pain relief is produced beta-endorphins bind to opioid receptors. The mechanism of endorphins can be viewed through two different lenses through activity in the peripheral nervous system (PNS) and the CNS. Endorphins express functional duality as they fall into the category of either neurotransmitters or neuromodulators in the central nervous system (CNS) and hormones in the pituitary gland.
MY ENDORPHIN FULL
Research is ongoing on each type to further understand the full functional potential of each, along with how they can be used in a medically beneficial manner. Of the three endorphin types, beta-endorphins have been the most studied and prevalent, accounting for the majority of the functional properties of endorphins as generalized and understood as a whole. Additionally, endorphins have been found to be associated with states of pleasure, including such emotions brought upon by laughter, love, sex, and even appetizing food. β-endorphin (an endogenous opioid) is one of the neurochemicals involved with exercise-induced euphoria (runner's high).
The pain relief experienced as a result of the release of endorphins has been determined to be greater than that of morphine. In general, the release of endorphins is understood to be associated with the body’s response to pain. The function of endorphins can be stated in general terms as well as broken down specifically and observed per each endorphin type. This molecular configuration thereby allows these endorphins to be the agonist of opioid receptors, the same receptors to which chemicals derived from opium, such as morphine, bind to for triggering physiological responses. Thus, the sequences of beta-endorphins and gamma-endorphins essentially have the sequence of alpha-endorphins nested within them. The alpha-endorphins are amino acid chains comprised of the same first 16 amino acid sequence as the beta-endorphins (and consequently has the same sequence of the first 16 amino acids comprising the gamma-endorphins). Finally, the third and shortest type of endorphins about the amino acid chain sequence is the alpha-endorphins. The second-longest chain is the gamma-endorphins, consisting of a 17 amino acid chain the same as the first 17 amino acid chain sequence of the beta-endorphins.
This sequence corresponds to amino acids 104 to 134 in the sequence of beta-LPH. The beta-endorphins are the longest chain, containing 31 amino acids in the following sequence: 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. Endorphins are identified as three distinct peptides termed alpha-endorphins, beta-endorphins, and gamma-endorphins. Beta-LPH is cleaved via enzymes into beta-melanocyte-stimulating hormone and endorphins, amongst other molecule types. POMC consists of a 241 amino acid chain which is cleaved by enzyme (prohormone convertases) action into the 93 amino acid single-chain polypeptide beta-lipoprotein (beta-LPH). Recent studies have produced evidence suggesting that POMC may also be produced by the immune system and, consequently, also provide a base source for endorphin production. The origins of endorphins have been traced to the precursor pro-opiomelanocortin (POMC) polypeptide, which is synthesized in the pituitary gland.