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Reduction of acyloxyacyl hydrolase activity in circulating neutrophils from cows after parturition

Hilde Dosogne, Anthony Capuco UGent, Max Paape UGent, Eddy Roets, Christian Burvenich UGent and B Fenwick (1998) JOURNAL OF DAIRY SCIENCE. 81(3). p.672-677
abstract
Bovine neutrophils contain the enzyme acyloxyacyl hydrolase, which hydrolyzes the acyloxyacyl linkage of the two nonhydroxylated fatty acyl chains to two 3-hydroxy fatty acids in the highly conserved lipid A part of endotoxins with high specificity. This hydrolysis decreases the toxicity of lipid A, but the immunostimulatory capacity of endotoxins is largely maintained. In two trials, we studied the activity of acyloxyacyl hydrolase in neutrophils that had been isolated from the blood of 18 dairy cows around parturition. Between 10 and 26 d after parturition, the activity of acyloxyacyl hydrolase in neutrophils decreased approximately 20% below prepartum activity. At about 2 mo after parturition, acyloxyacyl hydrolase activity returned to prepartum values. Changes in acyloxyacyl hydrolase activity could not be attributed to changes in binding of lipopolysaccharides by the CD14 molecules on neutrophils or monocytes. We hypothesize that decreased acyloxyacyl hydrolase activity in neutrophils shortly after parturition is a factor that increases the susceptibility of dairy cows to coliform mastitis during early lactation.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
CD14, BINDING, neutrophils, mastitis, endotoxin, BACTERIAL LIPOPOLYSACCHARIDES, ESCHERICHIA-COLI MASTITIS, POLYMORPHONUCLEAR LEUKOCYTES, ENZYMATIC DEACYLATION, ENDOTOXIN, BOVINE MASTITIS, PROTEIN, INFLAMMATION
journal title
JOURNAL OF DAIRY SCIENCE
J. Dairy Sci.
volume
81
issue
3
pages
672-677 pages
Web of Science type
Article
Web of Science id
000072988100010
ISSN
0022-0302
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
177526
handle
http://hdl.handle.net/1854/LU-177526
alternative location
http://jds.fass.org/cgi/content/abstract/81/3/672
date created
2004-01-14 13:41:00
date last changed
2016-12-19 15:38:07
@article{177526,
  abstract     = {Bovine neutrophils contain the enzyme acyloxyacyl hydrolase, which hydrolyzes the acyloxyacyl linkage of the two nonhydroxylated fatty acyl chains to two 3-hydroxy fatty acids in the highly conserved lipid A part of endotoxins with high specificity. This hydrolysis decreases the toxicity of lipid A, but the immunostimulatory capacity of endotoxins is largely maintained. In two trials, we studied the activity of acyloxyacyl hydrolase in neutrophils that had been isolated from the blood of 18 dairy cows around parturition. Between 10 and 26 d after parturition, the activity of acyloxyacyl hydrolase in neutrophils decreased approximately 20\% below prepartum activity. At about 2 mo after parturition, acyloxyacyl hydrolase activity returned to prepartum values. Changes in acyloxyacyl hydrolase activity could not be attributed to changes in binding of lipopolysaccharides by the CD14 molecules on neutrophils or monocytes. We hypothesize that decreased acyloxyacyl hydrolase activity in neutrophils shortly after parturition is a factor that increases the susceptibility of dairy cows to coliform mastitis during early lactation.},
  author       = {Dosogne, Hilde and Capuco, Anthony and Paape, Max and Roets, Eddy and Burvenich, Christian and Fenwick, B},
  issn         = {0022-0302},
  journal      = {JOURNAL OF DAIRY SCIENCE},
  keyword      = {CD14,BINDING,neutrophils,mastitis,endotoxin,BACTERIAL LIPOPOLYSACCHARIDES,ESCHERICHIA-COLI MASTITIS,POLYMORPHONUCLEAR LEUKOCYTES,ENZYMATIC DEACYLATION,ENDOTOXIN,BOVINE MASTITIS,PROTEIN,INFLAMMATION},
  language     = {eng},
  number       = {3},
  pages        = {672--677},
  title        = {Reduction of acyloxyacyl hydrolase activity in circulating neutrophils from cows after parturition},
  url          = {http://jds.fass.org/cgi/content/abstract/81/3/672},
  volume       = {81},
  year         = {1998},
}

Chicago
Dosogne, Hilde, Anthony Capuco, Max Paape, Eddy Roets, Christian Burvenich, and B Fenwick. 1998. “Reduction of Acyloxyacyl Hydrolase Activity in Circulating Neutrophils from Cows After Parturition.” Journal of Dairy Science 81 (3): 672–677.
APA
Dosogne, Hilde, Capuco, A., Paape, M., Roets, E., Burvenich, C., & Fenwick, B. (1998). Reduction of acyloxyacyl hydrolase activity in circulating neutrophils from cows after parturition. JOURNAL OF DAIRY SCIENCE, 81(3), 672–677.
Vancouver
1.
Dosogne H, Capuco A, Paape M, Roets E, Burvenich C, Fenwick B. Reduction of acyloxyacyl hydrolase activity in circulating neutrophils from cows after parturition. JOURNAL OF DAIRY SCIENCE. 1998;81(3):672–7.
MLA
Dosogne, Hilde, Anthony Capuco, Max Paape, et al. “Reduction of Acyloxyacyl Hydrolase Activity in Circulating Neutrophils from Cows After Parturition.” JOURNAL OF DAIRY SCIENCE 81.3 (1998): 672–677. Print.