Metalloendopeptidases EC 3.4.24.15 and EC 3.4.24.16: potential roles in vascular physiology |
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Authors: | Norman M Ursula Smith A Ian Hickey Michael J |
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Institution: | (1) Baker Medical Research Institute, Prahran, Victoria, Australia;(2) Centre for Inflammatory Diseases, Monash University, Clayton, Victoria, Australia |
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Abstract: | Summary The zinc metalloendopeptidases EC 3.4.24.15 (EP 24.15) and EC 3.4.24.16 (EP 24.16) are closely related ubiquitous enzymes,
which have well-defined in vitro activities in generation and degradation of a range of specific peptide targets. Despite
this, little is known regarding their roles in whole animal physiology. One of the peptides degraded by these enzymes in vitro
is bradykinin, a mediator with potent effects on the vasculature at both systemic and local levels. This review summarises
the work that has examined the role of EP 24.15/24.16 in regulation of the vascular effects of bradykinin in vivo. This work
was made possible by the development of a specific stable inhibitor of these enzymes, JA-2. Use of this inhibitor has shown
that EP 24.15/24.16 are capable of regulating responses induced by exogenous bradykinin. This effect was observed at a systemic
level with an increase in the hypotensive effect of intravenous bradykinin. Further work is required to determine whether
these enzymes also regulate bradykinin produced endogenously. |
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Keywords: | Bradykinin zinc metalloendopeptidase EC 3 4 24 15 zinc metalloendopeptidase EC 3 4 24 16 vascular permeability |
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