PMID- 23640713
OWN - NLM
STAT- MEDLINE
DCOM- 20140501
LR  - 20211021
IS  - 1572-9702 (Electronic)
IS  - 0168-8162 (Print)
IS  - 0168-8162 (Linking)
VI  - 61
IP  - 3
DP  - 2013 Nov
TI  - Proteins and endotoxin in house dust mite extracts modulate cytokine secretion 
      and gene expression by dermal fibroblasts.
PG  - 311-25
LID - 10.1007/s10493-013-9703-9 [doi]
AB  - House dust mite extracts used for diagnostic tests and immunotherapy contain 
      bioreactive molecules including proteins and endotoxin. These extracts can 
      influence the cytokine secretion and adhesion molecule expression by cells in the 
      skin and lung airways. The aim of this study was to determine the role of 
      proteins and endotoxin in mite extracts in modulating gene expression and 
      cytokine secretion by human dermal fibroblasts. Cultured normal human dermal 
      fibroblasts were stimulated with whole mite extracts, mite extracts boiled to 
      denature proteins, or mite extracts treated with polymyxin B to inactivate 
      lipopolysaccharide. Gene expression and secretion of interleukin-6 (IL-6), IL-8, 
      and monocyte chemoattractant protein-1 (MCP-1) were determined after 6 h of 
      stimulation. Whole Dermatophagoides farinae, D. pteronyssinus and Euroglyphus 
      maynei extracts induced dose-dependent IL-6 and IL-8 secretion. In addition, D. 
      farinae and E. maynei induced secretion of MCP-1. Dermatophagoides farinae and E. 
      maynei also induced parallel cytokine gene expression. Cells stimulated with 
      boiled D. farinae extract showed moderate to marked reductions in IL-6 and IL-8 
      secretion. In contrast, boiled D. pteronyssinus and E. maynei extracts induced 
      equal or greater cytokine secretions than untreated extracts. The stimulating 
      properties were reduced for all three extracts following treatment with polymyxin 
      B. Our data suggest that both endotoxin and proteins in mite extracts modulate 
      the secretion of cytokines by dermal fibroblasts. The biological activities of D. 
      farinae, D. pteronyssinus, and E. maynei extracts are not equivalent. There 
      appears to be a lipopolysaccharide-binding protein in some mite extracts.
FAU - Rockwood, Jananie
AU  - Rockwood J
AD  - Department of Biological Sciences, Wright State University, 3640 Colonel Glenn 
      Highway, Dayton, OH, 45435, USA.
FAU - Morgan, Marjorie S
AU  - Morgan MS
FAU - Arlian, Larry G
AU  - Arlian LG
LA  - eng
GR  - R01 AI017252/AI/NIAID NIH HHS/United States
GR  - R21 AI017252/AI/NIAID NIH HHS/United States
GR  - AI017252/AI/NIAID NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
DEP - 20130503
PL  - Netherlands
TA  - Exp Appl Acarol
JT  - Experimental & applied acarology
JID - 8507436
RN  - 0 (Cytokines)
RN  - 0 (Endotoxins)
RN  - 0 (Proteins)
SB  - IM
MH  - Animals
MH  - Cells, Cultured
MH  - Cytokines/*metabolism
MH  - Endotoxins/*pharmacology
MH  - Fibroblasts/*drug effects/metabolism
MH  - Gene Expression Regulation/*drug effects
MH  - Humans
MH  - Proteins/*pharmacology
MH  - Pyroglyphidae/chemistry/*metabolism
PMC - PMC3762948
MID - NIHMS475416
EDAT- 2013/05/04 06:00
MHDA- 2014/05/03 06:00
PMCR- 2014/11/01
CRDT- 2013/05/04 06:00
PHST- 2013/02/11 00:00 [received]
PHST- 2013/04/23 00:00 [accepted]
PHST- 2013/05/04 06:00 [entrez]
PHST- 2013/05/04 06:00 [pubmed]
PHST- 2014/05/03 06:00 [medline]
PHST- 2014/11/01 00:00 [pmc-release]
AID - 10.1007/s10493-013-9703-9 [doi]
PST - ppublish
SO  - Exp Appl Acarol. 2013 Nov;61(3):311-25. doi: 10.1007/s10493-013-9703-9. Epub 2013 
      May 3.