Intracellular and extracellular enzymatic deacylation of bacterial endotoxin during localized inflammation induced by Escherichia coli

C. M. McDermott, James S Cullor, B. W. Fenwick

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

Acyloxyacyl hydrolase (AOAH), an enzyme that removes the secondary acyl chains of gram-negative bacterial lipid A (endotoxin), has been identified previously in human neutrophils and mouse macrophages. We report here that bovine leukocytes also contain AOAH activity. Although bovine AOAH deacylates bacterial lipopolysaccharide in a manner similar to human AOAH, it is active in vitro over a broader pH range, from 4.0 to 7.0. By using Escherichia coli infection of the bovine mammary gland as a model of localized gram-negative bacterial disease and associated tissue inflammation, AOAH activity per leukocyte increased. In addition, AOAH activity increased in the cell-free portion of infected mammary secretions. These data indicate that AOAH activity increases in leukocytes associated with inflammation induced by gram-negative bacteria and provide additional evidence of its potential involvement in the defense against the effects of bacterial endotoxin.

Original languageEnglish (US)
Pages (from-to)478-485
Number of pages8
JournalInfection and Immunity
Volume59
Issue number2
StatePublished - 1991
Externally publishedYes

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Endotoxins
Escherichia coli
Inflammation
Leukocytes
Escherichia coli Infections
Lipid A
Human Mammary Glands
acyloxyacyl hydrolase
Gram-Negative Bacteria
Breast
Neutrophils
Macrophages
Enzymes

ASJC Scopus subject areas

  • Immunology

Cite this

Intracellular and extracellular enzymatic deacylation of bacterial endotoxin during localized inflammation induced by Escherichia coli. / McDermott, C. M.; Cullor, James S; Fenwick, B. W.

In: Infection and Immunity, Vol. 59, No. 2, 1991, p. 478-485.

Research output: Contribution to journalArticle

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