Peptide conversion: a potential pathway modulating G-protein signaling
2007 (English)In: Current Drug Targets, ISSN 1389-4501, Vol. 8, no 1, 147-154 p.Article, review/survey (Refereed) Published
Previous and current research has revealed that most neuropeptides induce their actions on cellular systems through specificreceptors located on the cell surface. These receptors are known as G-protein coupled receptors, which exert their effects through interac-tion with ion channels or enzymes located within the cell membrane. Following receptor stimulation and exerting their effects the pep-tides are inactivated by enzymatic degradation. However, in many cases the active neuropeptides are enzymatically converted to productswith retained bioactivity. These bioactive fragments may mimic but also counteract the action of the parent peptide. Thus, the releasedfragment may serve as a modulator of the response of the original compound. This phenomenon has been found to occur in a number ofpeptide systems, including the opioid peptides, tachykinins, as well as peptides belonging to the renin-angiotensin system, such as angio-tensin II. In some cases the conversion product interacts with the same receptor as the native compound but sometimes it appears that thereleased fragment interacts with receptors or binding sites distinct from those of the original peptide. This review is focused on peptidefragments released from opioid related peptides, substance P and angiotensin II, that have been shown to modulate the action of their par-ent compounds.
Place, publisher, year, edition, pages
2007. Vol. 8, no 1, 147-154 p.
Angiotensin, bioactive fragments, conversion, enzymes, G-protein (GPCR), opioid, peptides, receptors, substance P, tachyki- nins
IdentifiersURN: urn:nbn:se:uu:diva-25299DOI: 10.2174/138945007779315597ISI: 000243632600013PubMedID: 17266538OAI: oai:DiVA.org:uu-25299DiVA: diva2:53073