Neutrophil elastase-dependent cleavage of LTA4H alters its aminopeptidase activity in cystic fibrosis

The enzyme leukotriene A 4 hydrolase (LTA4H) is classically known for its epoxide hydrolase activity that converts leukotriene A 4 (LTA 4 ) to the neutrophil chemoattractant LTB 4 [1]. In 2010, our group published a study in Science that demonstrated that during an influenza model of acute airway in...

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Published inThe European respiratory journal Vol. 63; no. 3; p. 2301512
Main Authors Xu, Xin, Li, Jin-Dong, Green, Todd J, Wilson, Landon, Genschmer, Kristopher, Russell, Derek, Blalock, J Edwin, Gaggar, Amit
Format Journal Article
LanguageEnglish
Published England European Respiratory Society 01.03.2024
Subjects
Aminopeptidases - genetics
Cystic Fibrosis
Humans
Leukocyte Elastase
Neutrophils
Proteolysis
Research Letters
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Summary:The enzyme leukotriene A 4 hydrolase (LTA4H) is classically known for its epoxide hydrolase activity that converts leukotriene A 4 (LTA 4 ) to the neutrophil chemoattractant LTB 4 [1]. In 2010, our group published a study in Science that demonstrated that during an influenza model of acute airway inflammation, LTA4H was released from cells to degrade proline-glycine-proline (PGP), a non-canonical CXCR1 and -2 agonist of polymorphonuclear neutrophil (PMN) recruitment and activation [2], thereby attenuating PMN inflammation [3]. This study demonstrates that neutrophil elastase is a major enzyme responsible for the regulation of leukotriene A4 hydrolase (LTA4H) upon neutrophil activation, altering the aminopeptidase activity of LTA4H in the cystic fibrosis lung https://bit.ly/3SS1tKk
Bibliography:SourceType-Other Sources-1
content type line 63
ObjectType-Correspondence-1
ISSN:0903-1936
1399-3003
DOI:10.1183/13993003.01512-2023