| overview | endorphin (endorphin), also known as endorphin or endorphin, is an endogenous (secreted by the pituitary gland) Morphine-like biochemical compound hormone. It is an amino compound (peptide) secreted by the pituitary gland and the hypothalamus of vertebrates. It can bind to morphine receptors to produce the same analgesic effect and euphoria as morphine and opiates. It is equivalent to natural analgesics. The use of drugs can increase the secretion of endorphins. Endorphins are a class of morphine-like peptides originally isolated from brain tissue. In addition to the hypothalamus, the anterior lobe and the middle part of the pituitary gland secrete endorphins, and the gastrointestinal tract also has endorphins, which have a strong analgesic effect. |
| Physical and chemical properties | Endorphin has three main molecular forms, namely β-endorphin, α-endorphin and γ-endorphin, their structure is exactly the same as part of the sequence of pituitary lipotrophin. β-endorphin (β-endorphin,β-ENP) is a 31 peptide, which is a 61~91 amino acid residue of β-lipotrophin sequence and is a natural product. α-endorphin (α-endorphin,α-ENP) is a 16-peptide, which is a 61-76 amino acid residue of the β-lipotrophin sequence. β-endorphin has the highest affinity for μ1 opioid receptor (MOR1), slightly lower affinity for μ2(MOR2) and δ opioid receptor (DOR), and lower affinity for κ1 opioid receptor (KOR1). γ-endorphin is 17 peptide, which is 61~77 amino acid residue of β-lipotrophin sequence. Both α-endorphin and γ-endorphin are synthetic products, which are formed after being cut off by extracellular "proteolytic enzyme D. The CAS number of α-endorphin is 59004-96-5, and the molecular formula is C77H120N18O26S. |
| use | the endorphins commonly mentioned at present are all β-endorphins, and α-endorphins are rarely studied. Beta-endorphin is composed of 31 amino acids and can be synthesized by the hypothalamus of animals. Under normal circumstances, only a small amount is released into the blood. Under stress, the release into the blood increases, which plays an important role in anti-stress and pain suppression. Recently, it has been found that the immune system can also produce α-endorphin, which is mainly synthesized by peripheral blood mononuclear cells (PBMC). PBMC mainly includes monocytes and lymphocytes, and the content of endorphin in T-type memory cells is relatively high. Under the condition of inflammation or stress, the content of endorphin in PBMC will be significantly increased, but the content of endorphin in plasma will not change. Studies have shown that the content of endorphins in lymph nodes is significantly higher than that in plasma, indicating that endorphins are synthesized in immune cells and sent to lymph nodes. Endorphin is formed by the processing of POMC, the precursor of melanosin. It has been found in immune cells that there is a full-length expression of mRNA, but the mRNA is about 200 bp shorter than the mRNA in the pituitary gland, and there is no signal peptide sequence. Description-The secretion form of endorphins in PBMC is very similar to that of cytokines, and can be secreted and released without signal peptide precursors. Many endorphins in the hypothalamus of mice are biologically active. |
