Modulation of endopeptidase activity by calcitonin gene related peptide: a mechanism affecting substance P action?
Peptides with hormonal or neuronal activity are derived by enzymatic processing from pro-hormones, which by themselves are biologically inert. Processing and other enzymatic conversions may occur step-wise, leading to the formation of a cascade of biologically active (or inactive) peptides. The neur...
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Veröffentlicht in: | Biochimie 1988, Vol.70 (1), p.65-68 |
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Sprache: | eng |
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Zusammenfassung: | Peptides with hormonal or neuronal activity are derived by enzymatic processing from pro-hormones, which by themselves are biologically inert. Processing and other enzymatic conversions may occur step-wise, leading to the formation of a cascade of biologically active (or inactive) peptides.
The neurokin in substance P is known to be metabolically transformed both by amino- and endopeptidases. More N-terminal substance (1–7) hass been found than C-terminal (2–11 to 5–11) fragments in various CNS areas. The substance P (1–7) fragment also shows biological activity
e.g., providing analgesia, lowering blood pressure, inhibiting aggressive behavior and (in contrast to substance P) inhibiting grooming behavior. An endopeptidase generating substance P (1–7) and to a lesser extent, substance (1–8), has been isolated and characterized from human cerebrospinal fluid (CSF) and bovine spinal cord, as a metalloenzyme with essential SH-groups.
Substance P co-exists with calcitonin gene related peptide (CGRP) in a large population of non-myelinated primary afferent (‘pain’) fibers. Intrathecal injection of substance P causes behavioral and physiological responses which are potentiated and prolonged by CGRP. It was found that CGRP competes with substance P for the endopeptidase. It is suggested that the main action of CGRP in the spinal cord is to inhibit substance P degradation. |
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ISSN: | 0300-9084 1638-6183 |
DOI: | 10.1016/0300-9084(88)90159-9 |