Histamine N-methyltransferase Modulates Human Bronchial Smooth Muscle Contraction

To elucidate the modulatory role of histamine-degrading enzymes in airway constrictor responses, human bronchial strips were studied under isometric conditions in vitro. Pretreatment of tissues with the histamine N-methyltransferase (HMT) inhibitor SKF 91488 specifically potentiated the contractile...

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Main Authors: J. Tamaoki, A. Chiyotani, E. Tagaya, K. Isono, K. Konno
Format: Article
Language:English
Published: Hindawi Limited 1994-01-01
Series:Mediators of Inflammation
Online Access:http://dx.doi.org/10.1155/S0962935194000153
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spelling doaj-1e966ef7267e477fb31d048c1aaebbef2020-11-24T23:41:33ZengHindawi LimitedMediators of Inflammation0962-93511466-18611994-01-013212512910.1155/S0962935194000153Histamine N-methyltransferase Modulates Human Bronchial Smooth Muscle ContractionJ. Tamaoki0A. Chiyotani1E. Tagaya2K. Isono3K. Konno4First Department of Medicine, Tokyo Women's Medical College, Tokyo 162, JapanFirst Department of Medicine, Tokyo Women's Medical College, Tokyo 162, JapanFirst Department of Medicine, Tokyo Women's Medical College, Tokyo 162, JapanFirst Department of Medicine, Tokyo Women's Medical College, Tokyo 162, JapanFirst Department of Medicine, Tokyo Women's Medical College, Tokyo 162, JapanTo elucidate the modulatory role of histamine-degrading enzymes in airway constrictor responses, human bronchial strips were studied under isometric conditions in vitro. Pretreatment of tissues with the histamine N-methyltransferase (HMT) inhibitor SKF 91488 specifically potentiated the contractile responses to histamine, causing a leftward displacement of the concentration response curves, whereas the diamine oxidase inhibitor aminoguanidine had no effect. This potentiation was attenuated by mechanical removal of the epithelium. The HMT activity was detected in the human bronchi, which was less in the epithelium-denuded tissues than the epithelium-intact tissues. These results suggest that HMT localized to the airway epithelium may play a protective role against histamine-mediated bronchoconstriction in humans.http://dx.doi.org/10.1155/S0962935194000153
collection DOAJ
language English
format Article
sources DOAJ
author J. Tamaoki
A. Chiyotani
E. Tagaya
K. Isono
K. Konno
spellingShingle J. Tamaoki
A. Chiyotani
E. Tagaya
K. Isono
K. Konno
Histamine N-methyltransferase Modulates Human Bronchial Smooth Muscle Contraction
Mediators of Inflammation
author_facet J. Tamaoki
A. Chiyotani
E. Tagaya
K. Isono
K. Konno
author_sort J. Tamaoki
title Histamine N-methyltransferase Modulates Human Bronchial Smooth Muscle Contraction
title_short Histamine N-methyltransferase Modulates Human Bronchial Smooth Muscle Contraction
title_full Histamine N-methyltransferase Modulates Human Bronchial Smooth Muscle Contraction
title_fullStr Histamine N-methyltransferase Modulates Human Bronchial Smooth Muscle Contraction
title_full_unstemmed Histamine N-methyltransferase Modulates Human Bronchial Smooth Muscle Contraction
title_sort histamine n-methyltransferase modulates human bronchial smooth muscle contraction
publisher Hindawi Limited
series Mediators of Inflammation
issn 0962-9351
1466-1861
publishDate 1994-01-01
description To elucidate the modulatory role of histamine-degrading enzymes in airway constrictor responses, human bronchial strips were studied under isometric conditions in vitro. Pretreatment of tissues with the histamine N-methyltransferase (HMT) inhibitor SKF 91488 specifically potentiated the contractile responses to histamine, causing a leftward displacement of the concentration response curves, whereas the diamine oxidase inhibitor aminoguanidine had no effect. This potentiation was attenuated by mechanical removal of the epithelium. The HMT activity was detected in the human bronchi, which was less in the epithelium-denuded tissues than the epithelium-intact tissues. These results suggest that HMT localized to the airway epithelium may play a protective role against histamine-mediated bronchoconstriction in humans.
url http://dx.doi.org/10.1155/S0962935194000153
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