Please use this identifier to cite or link to this item: http://ahro.austin.org.au/austinjspui/handle/1/12217
Title: Inhibition of angiotensin converting enzyme by N-terminal fragments of substance P.
Authors: Rogerson, F M;Livett, B G;Scanlon, D;Mendelsohn, Frederick AO
Affiliation: Department of Medicine, Austin Hospital, Heidelberg, Victoria, Australia.
Issue Date: 12-Nov-1989
Citation: Neuropeptides; 14(4): 213-7
Abstract: A range of N-terminal fragments of substance P (SP) were evaluated for inhibitory activity against angiotensin converting enzyme (ACE) from rat lung and brain (striatum). SP inhibited the enzyme from both sources in a concentration dependent manner (IC50 30 microM). The N-terminal fragments SP[1-7], SP[1-6], SP[1-4] and SP[3-4] were equipotent with SP for both sources of the enzyme. However, SP[1-3] showed a difference in its activity, being more active than SP (IC50 10 microM) in inhibiting the brain enzyme, but inactive against lung ACE. These results suggest that the inhibitory action of SP on ACE resides in the N-terminus of the peptide. The difference in reactivity towards SP[1-3] lends support to the idea that lung and brain ACE are different isozymes.
Internal ID Number: 2482949
URI: http://ahro.austin.org.au/austinjspui/handle/1/12217
URL: http://www.ncbi.nlm.nih.gov/pubmed/2482949
Type: Journal Article
Subjects: Angiotensin-Converting Enzyme Inhibitors
Animals
Corpus Striatum.enzymology
Dose-Response Relationship, Drug
Lung.enzymology
Male
Peptide Fragments.chemical synthesis.pharmacology
Rats
Rats, Inbred Strains
Substance P.pharmacology
Appears in Collections:Journal articles

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