Casomorphins and Hemorphins—Opioid Active Peptides Released by Partial Hydrolysis of Structural Proteins

摘要: ABSTRACT In addition to the classic opioid peptides (β-endorphin, dynorphins, and enkephalins), with N-terminal Tyr-Gly-Gly-Phe tetrapeptide sequence, active containing Tyr-Pro dipeptide residues in their sequence have been identified characterized. Other than endomorphins, these so-called atypical are derived by partial hydrolysis of endogenous existing functional proteins mainly produced peripheral tissues body fluids. Among endogenously β-casomorphins hemorphins. These formed through milk protein β-casein hemoglobin, respectively, many biological effects They less potent but share most typical effects. Moreover, detected concentrations hemorphins fluids highly exceed those β-endorphin enkephalins. Originally, were isolated from enzymatically treated bovine blood, respectively. Later they as naturally occurring compounds human plasma cerebrospinal fluid. This chapter gives a brief review past current research on regarding mechanisms for release, distribution, actions, pathophysiological roles.