Cargando…

ESTERASES OF THE POLYMORPHONUCLEAR LEUKOCYTE CAPABLE OF HYDROLYZING ACETYL DL-PHENYL-ALANINE β-NAPHTHYL ESTER : RELATIONSHIP TO THE ACTIVATABLE ESTERASE OF CHEMOTAXIS

Previous published work has led to the hypothesis that the activatable esterase of chemotaxis is a serine esterase of the rabbit polymorphonuclear leukocyte existing in an inert, phosphonate insusceptible form, which after activation is capable of hydrolyzing aromatic amino acid esters and being inh...

Descripción completa

Detalles Bibliográficos
Autores principales: Becker, Elmer L., Ward, Peter A.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1969
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2138612/
https://www.ncbi.nlm.nih.gov/pubmed/5812915
_version_ 1782143603946029056
author Becker, Elmer L.
Ward, Peter A.
author_facet Becker, Elmer L.
Ward, Peter A.
author_sort Becker, Elmer L.
collection PubMed
description Previous published work has led to the hypothesis that the activatable esterase of chemotaxis is a serine esterase of the rabbit polymorphonuclear leukocyte existing in an inert, phosphonate insusceptible form, which after activation is capable of hydrolyzing aromatic amino acid esters and being inhibited by phosphonates. In the present study, directed to the testing of this hypothesis, we have shown that rabbit peritoneal polymorphonuclear leukocytes contain three esterases capable of hydrolyzing the aromatic amino acid ester, acetyl DL-phenylalanine β-naphthyl ester. Two of these esterases, esterase 1 and esterase 2, are inhibited by various p-nitrophenyl ethyl phosphonate esters. The inhibition of each esterase is irreversible and progressive with time. When the logarithm of the esterase activity remaining after cell and inhibitor have been in contact for a constant time is plotted against the concentration of inhibitor, a straight line results. These results support the conclusion that both esterases are serine esterases. The third esterase, esterase 3, differs from the other two by its inability to be inactivated by any of the phosphonates no matter how high the concentration of phosphonate or prolonged the period of incubation of cell with phosphonate. The activity of esterase 1 is at least 10,000 times more easily inhibited by phosphonates than is that of esterase 2; incubating rabbit polymorphonuclear leukocytes for 15 min at 27°C with 10(–9)–10(–8) M concentrations of various phosphonates inactivates esterase 1, but it required 10(–6)–10(–4) M concentrations of the same phosphonates to inhibit esterase 2. The inhibition profiles of esterase 1 are distinctly different from those of esterase 2 when the two esterases are tested with the phenylalkylphosphonates, chloroalkylphosphonates, and alkylphosphonates. The inhibition profile of esterase 1 is essentially the same as that of the activatable esterase of chemotaxis obtained previously when the same three homologous series of phosphonates were tested for their ability to protect against deactivation by the chemotactic factor or give chemotactic-dependent inhibition. It is tentatively concluded that esterase 1 of the rabbit peritoneal neutrophil is the activated form of the activatable esterase of chemotaxis.
format Text
id pubmed-2138612
institution National Center for Biotechnology Information
language English
publishDate 1969
publisher The Rockefeller University Press
record_format MEDLINE/PubMed
spelling pubmed-21386122008-04-17 ESTERASES OF THE POLYMORPHONUCLEAR LEUKOCYTE CAPABLE OF HYDROLYZING ACETYL DL-PHENYL-ALANINE β-NAPHTHYL ESTER : RELATIONSHIP TO THE ACTIVATABLE ESTERASE OF CHEMOTAXIS Becker, Elmer L. Ward, Peter A. J Exp Med Article Previous published work has led to the hypothesis that the activatable esterase of chemotaxis is a serine esterase of the rabbit polymorphonuclear leukocyte existing in an inert, phosphonate insusceptible form, which after activation is capable of hydrolyzing aromatic amino acid esters and being inhibited by phosphonates. In the present study, directed to the testing of this hypothesis, we have shown that rabbit peritoneal polymorphonuclear leukocytes contain three esterases capable of hydrolyzing the aromatic amino acid ester, acetyl DL-phenylalanine β-naphthyl ester. Two of these esterases, esterase 1 and esterase 2, are inhibited by various p-nitrophenyl ethyl phosphonate esters. The inhibition of each esterase is irreversible and progressive with time. When the logarithm of the esterase activity remaining after cell and inhibitor have been in contact for a constant time is plotted against the concentration of inhibitor, a straight line results. These results support the conclusion that both esterases are serine esterases. The third esterase, esterase 3, differs from the other two by its inability to be inactivated by any of the phosphonates no matter how high the concentration of phosphonate or prolonged the period of incubation of cell with phosphonate. The activity of esterase 1 is at least 10,000 times more easily inhibited by phosphonates than is that of esterase 2; incubating rabbit polymorphonuclear leukocytes for 15 min at 27°C with 10(–9)–10(–8) M concentrations of various phosphonates inactivates esterase 1, but it required 10(–6)–10(–4) M concentrations of the same phosphonates to inhibit esterase 2. The inhibition profiles of esterase 1 are distinctly different from those of esterase 2 when the two esterases are tested with the phenylalkylphosphonates, chloroalkylphosphonates, and alkylphosphonates. The inhibition profile of esterase 1 is essentially the same as that of the activatable esterase of chemotaxis obtained previously when the same three homologous series of phosphonates were tested for their ability to protect against deactivation by the chemotactic factor or give chemotactic-dependent inhibition. It is tentatively concluded that esterase 1 of the rabbit peritoneal neutrophil is the activated form of the activatable esterase of chemotaxis. The Rockefeller University Press 1969-02-28 /pmc/articles/PMC2138612/ /pubmed/5812915 Text en Copyright © 1969 by The Rockefeller University Press 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
Becker, Elmer L.
Ward, Peter A.
ESTERASES OF THE POLYMORPHONUCLEAR LEUKOCYTE CAPABLE OF HYDROLYZING ACETYL DL-PHENYL-ALANINE β-NAPHTHYL ESTER : RELATIONSHIP TO THE ACTIVATABLE ESTERASE OF CHEMOTAXIS
title ESTERASES OF THE POLYMORPHONUCLEAR LEUKOCYTE CAPABLE OF HYDROLYZING ACETYL DL-PHENYL-ALANINE β-NAPHTHYL ESTER : RELATIONSHIP TO THE ACTIVATABLE ESTERASE OF CHEMOTAXIS
title_full ESTERASES OF THE POLYMORPHONUCLEAR LEUKOCYTE CAPABLE OF HYDROLYZING ACETYL DL-PHENYL-ALANINE β-NAPHTHYL ESTER : RELATIONSHIP TO THE ACTIVATABLE ESTERASE OF CHEMOTAXIS
title_fullStr ESTERASES OF THE POLYMORPHONUCLEAR LEUKOCYTE CAPABLE OF HYDROLYZING ACETYL DL-PHENYL-ALANINE β-NAPHTHYL ESTER : RELATIONSHIP TO THE ACTIVATABLE ESTERASE OF CHEMOTAXIS
title_full_unstemmed ESTERASES OF THE POLYMORPHONUCLEAR LEUKOCYTE CAPABLE OF HYDROLYZING ACETYL DL-PHENYL-ALANINE β-NAPHTHYL ESTER : RELATIONSHIP TO THE ACTIVATABLE ESTERASE OF CHEMOTAXIS
title_short ESTERASES OF THE POLYMORPHONUCLEAR LEUKOCYTE CAPABLE OF HYDROLYZING ACETYL DL-PHENYL-ALANINE β-NAPHTHYL ESTER : RELATIONSHIP TO THE ACTIVATABLE ESTERASE OF CHEMOTAXIS
title_sort esterases of the polymorphonuclear leukocyte capable of hydrolyzing acetyl dl-phenyl-alanine β-naphthyl ester : relationship to the activatable esterase of chemotaxis
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2138612/
https://www.ncbi.nlm.nih.gov/pubmed/5812915
work_keys_str_mv AT beckerelmerl esterasesofthepolymorphonuclearleukocytecapableofhydrolyzingacetyldlphenylalaninebnaphthylesterrelationshiptotheactivatableesteraseofchemotaxis
AT wardpetera esterasesofthepolymorphonuclearleukocytecapableofhydrolyzingacetyldlphenylalaninebnaphthylesterrelationshiptotheactivatableesteraseofchemotaxis