Adenovirus-mediated transfer of a gene encoding acyloxyacyl hydrolase (AOAH) into mice increases tissue and plasma AOAH activity

Coulthard, M. G., Swindle, J., Munford, R. S., Gerard, R.D. and Meidell, R.S. (1996) Adenovirus-mediated transfer of a gene encoding acyloxyacyl hydrolase (AOAH) into mice increases tissue and plasma AOAH activity. Infection and Immunity, 64 5: 1510-1515.

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Author Coulthard, M. G.
Swindle, J.
Munford, R. S.
Gerard, R.D.
Meidell, R.S.
Title Adenovirus-mediated transfer of a gene encoding acyloxyacyl hydrolase (AOAH) into mice increases tissue and plasma AOAH activity
Journal name Infection and Immunity  (ERA 2012 Listed)    (ERA 2010 Rank A)   Check publisher's open access policy
Publication date 1996-05
Sub-type Article
Volume number 64
Issue number 5
ISSN 0019-9567
Start page 1510
End page 1515
Total pages 6
Place of publication United States
Publisher American Society for Microbiology
Language eng
Formatted abstract Although the host response to gram-negative bacterial infection follows largely from the interactions of bacterial lipopolysaccharides (LPS or endotoxin) with host cells, little information is available concerning the mechanisms by which the host eliminates or detoxifies LPS. Acyloxyacyl hydrolase (AOAH) is an enzyme, found in phagocytic cells, that catalyzes the enzymatic deacylation of the lipid A moiety of LPS. Enzymatically deacylated LPS is much less potent than LPS at inducing responses in human cells, and it can antagonize the ability of LPS to activate human macrophages, neutrophils, and endothelial cells. Despite these observations, the physiologic role of LPS deacylation remains undefined. To investigate the ability of AOAH to carry out LPS deacylation in vivo, we produced a recombinant adenovirus carrying a gene encoding AOAH (Ad.CMV-AOAH) and employed this vector to elicit transient overexpression of AOAH in mice. Mice infected with Ad.CMV- AOAH expressed high levels of the enzyme in plasma, liver, spleen, and kidney. Although adenovirus-induced hepatitis reduced hepatic uptake of intravenously injected [3H]LPS, animals expressing the transgene deacylated a larger fraction of the [3H]LPS taken up by their livers than did mice infected with a control adenovirus. These studies indicate that AOAH can catalyze the deacylation of LPS in vivo, and they provide evidence that the rates of hepatic LPS uptake and deacylation are not closely linked.
Keyword Adenovirus
Animal experiment
Animal tissue
Article
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article
Collection: School of Medicine Publications
 
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