Abstract
Previous and current research has revealed that most neuropeptides induce their actions on cellular systems through specific receptors located on the cell surface. These receptors are known as G-protein coupled receptors, which exert their effects through interaction with ion channels or enzymes located within the cell membrane. Following receptor stimulation and exerting their effects the peptides are inactivated by enzymatic degradation. However, in many cases the active neuropeptides are enzymatically converted to products with retained bioactivity. These bioactive fragments may mimic but also counteract the action of the parent peptide. Thus, the released fragment may serve as a modulator of the response of the original compound. This phenomenon has been found to occur in a number of peptide systems, including the opioid peptides, tachykinins, as well as peptides belonging to the renin-angiotensin system, such as angiotensin II. In some cases the conversion product interacts with the same receptor as the native compound but sometimes it appears that the released fragment interacts with receptors or binding sites distinct from those of the original peptide. This review is focused on peptide fragments released from opioid related peptides, substance P and angiotensin II, that have been shown to modulate the action of their parent compounds.
Keywords: Angiotensin, bioactive fragments, conversion, enzymes, G-protein (GPCR), opioid, peptides, receptors, substance P, tachykinins
Current Drug Targets
Title: Peptide Conversion - A Potential Pathway Modulating G-Protein Signaling
Volume: 8 Issue: 1
Author(s): F. Nyberg and M. Hallberg
Affiliation:
Keywords: Angiotensin, bioactive fragments, conversion, enzymes, G-protein (GPCR), opioid, peptides, receptors, substance P, tachykinins
Abstract: Previous and current research has revealed that most neuropeptides induce their actions on cellular systems through specific receptors located on the cell surface. These receptors are known as G-protein coupled receptors, which exert their effects through interaction with ion channels or enzymes located within the cell membrane. Following receptor stimulation and exerting their effects the peptides are inactivated by enzymatic degradation. However, in many cases the active neuropeptides are enzymatically converted to products with retained bioactivity. These bioactive fragments may mimic but also counteract the action of the parent peptide. Thus, the released fragment may serve as a modulator of the response of the original compound. This phenomenon has been found to occur in a number of peptide systems, including the opioid peptides, tachykinins, as well as peptides belonging to the renin-angiotensin system, such as angiotensin II. In some cases the conversion product interacts with the same receptor as the native compound but sometimes it appears that the released fragment interacts with receptors or binding sites distinct from those of the original peptide. This review is focused on peptide fragments released from opioid related peptides, substance P and angiotensin II, that have been shown to modulate the action of their parent compounds.
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Cite this article as:
Nyberg F. and Hallberg M., Peptide Conversion - A Potential Pathway Modulating G-Protein Signaling, Current Drug Targets 2007; 8 (1) . https://dx.doi.org/10.2174/138945007779315597
DOI https://dx.doi.org/10.2174/138945007779315597 |
Print ISSN 1389-4501 |
Publisher Name Bentham Science Publisher |
Online ISSN 1873-5592 |
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