Document Detail


Externalization of the leaderless cytokine IL-1F6 occurs in response to lipopolysaccharide/ATP activation of transduced bone marrow macrophages.
MedLine Citation:
PMID:  19717513     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
An interesting trait shared by many members of the IL-1 cytokine family is the absence of a signal sequence that can direct the newly synthesized polypeptides to the endoplasmic reticulum. As a result, these cytokines accumulate intracellularly. Recent studies investigating IL-1beta export established that its release is facilitated via activation of an intracellular multiprotein complex termed the inflammasome. The purpose of the current study was to explore the mechanism by which murine IL-1F6 is released from bone marrow-derived macrophages (BMDMs) and to compare this mechanism to that used by IL-1beta. BMDMs were engineered to overexpress IL-1F6 by retroviral transduction; cells overexpressing GFP also were generated to provide a noncytokine comparator. The transduced cells constitutively expressed IL-1F6 and GFP, but they did not constitutively release these polypeptides to the medium. Enhanced release of IL-1F6 was achieved by treating with LPS followed by ATP-induced activation of the P2X(7) receptor; GFP also was released under these conditions. No obvious proteolytic cleavage of IL-1F6 was noted following P2X(7) receptor-induced release. Stimulus-induced release of IL-1F6 and GFP demonstrated comparable susceptibility to pharmacological modulation. Therefore, transduced IL-1F6 is released in parallel with endogenous mature IL-1beta from LPS/ATP-treated BMDMs, but this externalization process is not selective for cytokines as a noncytokine (GFP) shows similar behavior. These findings suggest that IL-1F6 can be externalized via a stimulus-coupled mechanism comparable to that used by IL-1beta, and they provide additional insight into the complex cellular processes controlling posttranslational processing of the IL-1 cytokine family.
Authors:
Unja Martin; John Scholler; Jesse Gurgel; Blair Renshaw; John E Sims; Christopher A Gabel
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Publication Detail:
Type:  Journal Article     Date:  2009-08-28
Journal Detail:
Title:  Journal of immunology (Baltimore, Md. : 1950)     Volume:  183     ISSN:  1550-6606     ISO Abbreviation:  J. Immunol.     Publication Date:  2009 Sep 
Date Detail:
Created Date:  2009-09-03     Completed Date:  2009-09-23     Revised Date:  2010-01-14    
Medline Journal Info:
Nlm Unique ID:  2985117R     Medline TA:  J Immunol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  4021-30     Citation Subset:  AIM; IM    
Affiliation:
Department of Inflammation, Amgen, Seattle, WA 98119, USA.
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MeSH Terms
Descriptor/Qualifier:
Adenosine Triphosphate / pharmacology*
Animals
Bone Marrow Cells
Interleukin-1 / genetics,  metabolism*
Lipopolysaccharides / pharmacology*
Macrophages / metabolism
Mice
Mice, Inbred C57BL
Protein Transport / drug effects
Receptors, Purinergic P2 / metabolism
Transduction, Genetic
Chemical
Reg. No./Substance:
0/Interleukin-1; 0/Lipopolysaccharides; 0/Receptors, Purinergic P2; 0/interleukin 1F6, mouse; 0/purinergic P2X7 receptor; 56-65-5/Adenosine Triphosphate

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