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COMPLEMENT AS A MEDIATOR OF INFLAMMATION : ENHANCEMENT OF VASCULAR PERMEABILITY BY PURIFIED HUMAN C'1 ESTERASE

Purified preparations of the esterase derived from the first component of complement (C'1 esterase) increased vascular permeability in guinea pig skin, an effect inhibited by triprolidine, an antihistaminic agent, but not by soy bean trypsin inhibitor. The permeability-increasing and esterolyti...

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Detalles Bibliográficos
Autores principales: Ratnoff, Oscar D., Lepow, Irwin H.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1963
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2137679/
https://www.ncbi.nlm.nih.gov/pubmed/14087615
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author Ratnoff, Oscar D.
Lepow, Irwin H.
author_facet Ratnoff, Oscar D.
Lepow, Irwin H.
author_sort Ratnoff, Oscar D.
collection PubMed
description Purified preparations of the esterase derived from the first component of complement (C'1 esterase) increased vascular permeability in guinea pig skin, an effect inhibited by triprolidine, an antihistaminic agent, but not by soy bean trypsin inhibitor. The permeability-increasing and esterolytic properties of C'1 esterase were inhibited in parallel by the serum inhibitor of C'1 esterase, diisopropylphosphofluoridate and extremes of temperature and pH. Moreover, the permeability-increasing and esterolytic properties evolved in parallel when C'1 esterase was generated from its subcomponents. How C'1 esterase induces changes in vascular permeability remains unexplained, although the possibility that its action is mediated through a histamine-like agent is attractive.
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spelling pubmed-21376792008-04-17 COMPLEMENT AS A MEDIATOR OF INFLAMMATION : ENHANCEMENT OF VASCULAR PERMEABILITY BY PURIFIED HUMAN C'1 ESTERASE Ratnoff, Oscar D. Lepow, Irwin H. J Exp Med Article Purified preparations of the esterase derived from the first component of complement (C'1 esterase) increased vascular permeability in guinea pig skin, an effect inhibited by triprolidine, an antihistaminic agent, but not by soy bean trypsin inhibitor. The permeability-increasing and esterolytic properties of C'1 esterase were inhibited in parallel by the serum inhibitor of C'1 esterase, diisopropylphosphofluoridate and extremes of temperature and pH. Moreover, the permeability-increasing and esterolytic properties evolved in parallel when C'1 esterase was generated from its subcomponents. How C'1 esterase induces changes in vascular permeability remains unexplained, although the possibility that its action is mediated through a histamine-like agent is attractive. The Rockefeller University Press 1963-10-31 /pmc/articles/PMC2137679/ /pubmed/14087615 Text en Copyright © 1963, by The Rockefeller Institute This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Article
Ratnoff, Oscar D.
Lepow, Irwin H.
COMPLEMENT AS A MEDIATOR OF INFLAMMATION : ENHANCEMENT OF VASCULAR PERMEABILITY BY PURIFIED HUMAN C'1 ESTERASE
title COMPLEMENT AS A MEDIATOR OF INFLAMMATION : ENHANCEMENT OF VASCULAR PERMEABILITY BY PURIFIED HUMAN C'1 ESTERASE
title_full COMPLEMENT AS A MEDIATOR OF INFLAMMATION : ENHANCEMENT OF VASCULAR PERMEABILITY BY PURIFIED HUMAN C'1 ESTERASE
title_fullStr COMPLEMENT AS A MEDIATOR OF INFLAMMATION : ENHANCEMENT OF VASCULAR PERMEABILITY BY PURIFIED HUMAN C'1 ESTERASE
title_full_unstemmed COMPLEMENT AS A MEDIATOR OF INFLAMMATION : ENHANCEMENT OF VASCULAR PERMEABILITY BY PURIFIED HUMAN C'1 ESTERASE
title_short COMPLEMENT AS A MEDIATOR OF INFLAMMATION : ENHANCEMENT OF VASCULAR PERMEABILITY BY PURIFIED HUMAN C'1 ESTERASE
title_sort complement as a mediator of inflammation : enhancement of vascular permeability by purified human c'1 esterase
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2137679/
https://www.ncbi.nlm.nih.gov/pubmed/14087615
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