FIBCD1 Modulation of the Epithelial Immune Response Elicited by Chitin

Mark Hammond, Anders Schlosser, Theresa Helene Bak-Thomsen, Grith Lykke Sørensen, Uffe Holmskov

Research output: Contribution to conference without publisher/journalConference abstract for conferenceResearchpeer-review

Abstract

Background:
FIBCD1 is a type II transmembrane protein located on the brush border of intestinal epithelial cells. FIBCD1 binds specifically to acetylated compounds
such as chitin through the C-terminal fibrinogen-related domain. Chitin is a highly acetylated homopolymeric b-1,4-N-acetylglucosamine carbohydrate, which next to cellulose is the most abundant biopolymer found in nature, eg in fungi and parasites. It was recently demonstrated that chitin induces the accumulation in tissue of IL-4-expressing innate immune cells in vivo and it was
suggested that chitin thus could be a recognition element implicated in allergic and helminth immunity. However, very little is known about how chitin-induced immune signalling is initiated or propagated.
Aim:
The aim of this project is to investigate the hypothesis that chitin immune signalling may be initiated by the FIBCD1 chitin receptor through activation of
NF-jB signalling and downstream synthesis of mucosal epithelial-derived cytokines, TSLP and IL-33, which shapes the local accumulation and activation of Th2 responses.
Results:
Initial experiments have focused on the establishment of stable FIBCD1 overexpression in HEK293, HCT-116 and A549 epithelial cell lines. Chitin fragments obtained from shrimp shells were produced by brief sonication followed by filtration through 100, 70 and 40 lm filters respectively. Size distribution was determined by fluorescence-activated cell sorting. Cell lines will now be exposed to chitin fragments of varying size or the model ligand acetylated BSA, at different time intervals anddoses and using a luciferase reporter system detection of NFjB activation will be performed and cytokine expression will be quantified via qRT-PCR.
Perspectives:
Improved understanding of epithelialimmune and inflammatory modulation in response to chitin may provide new strategies for therapeutic intervention of allergic or parasitic disease.
Original languageEnglish
Publication date2010
Number of pages1
Publication statusPublished - 2010

Cite this

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title = "FIBCD1 Modulation of the Epithelial Immune Response Elicited by Chitin",
abstract = "Background: FIBCD1 is a type II transmembrane protein located on the brush border of intestinal epithelial cells. FIBCD1 binds specifically to acetylated compoundssuch as chitin through the C-terminal fibrinogen-related domain. Chitin is a highly acetylated homopolymeric b-1,4-N-acetylglucosamine carbohydrate, which next to cellulose is the most abundant biopolymer found in nature, eg in fungi and parasites. It was recently demonstrated that chitin induces the accumulation in tissue of IL-4-expressing innate immune cells in vivo and it wassuggested that chitin thus could be a recognition element implicated in allergic and helminth immunity. However, very little is known about how chitin-induced immune signalling is initiated or propagated.Aim: The aim of this project is to investigate the hypothesis that chitin immune signalling may be initiated by the FIBCD1 chitin receptor through activation ofNF-jB signalling and downstream synthesis of mucosal epithelial-derived cytokines, TSLP and IL-33, which shapes the local accumulation and activation of Th2 responses.Results: Initial experiments have focused on the establishment of stable FIBCD1 overexpression in HEK293, HCT-116 and A549 epithelial cell lines. Chitin fragments obtained from shrimp shells were produced by brief sonication followed by filtration through 100, 70 and 40 lm filters respectively. Size distribution was determined by fluorescence-activated cell sorting. Cell lines will now be exposed to chitin fragments of varying size or the model ligand acetylated BSA, at different time intervals anddoses and using a luciferase reporter system detection of NFjB activation will be performed and cytokine expression will be quantified via qRT-PCR.Perspectives: Improved understanding of epithelialimmune and inflammatory modulation in response to chitin may provide new strategies for therapeutic intervention of allergic or parasitic disease.",
author = "Mark Hammond and Anders Schlosser and Bak-Thomsen, {Theresa Helene} and S{\o}rensen, {Grith Lykke} and Uffe Holmskov",
year = "2010",
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FIBCD1 Modulation of the Epithelial Immune Response Elicited by Chitin. / Hammond, Mark; Schlosser, Anders; Bak-Thomsen, Theresa Helene; Sørensen, Grith Lykke; Holmskov, Uffe.

2010.

Research output: Contribution to conference without publisher/journalConference abstract for conferenceResearchpeer-review

TY - ABST

T1 - FIBCD1 Modulation of the Epithelial Immune Response Elicited by Chitin

AU - Hammond, Mark

AU - Schlosser, Anders

AU - Bak-Thomsen, Theresa Helene

AU - Sørensen, Grith Lykke

AU - Holmskov, Uffe

PY - 2010

Y1 - 2010

N2 - Background: FIBCD1 is a type II transmembrane protein located on the brush border of intestinal epithelial cells. FIBCD1 binds specifically to acetylated compoundssuch as chitin through the C-terminal fibrinogen-related domain. Chitin is a highly acetylated homopolymeric b-1,4-N-acetylglucosamine carbohydrate, which next to cellulose is the most abundant biopolymer found in nature, eg in fungi and parasites. It was recently demonstrated that chitin induces the accumulation in tissue of IL-4-expressing innate immune cells in vivo and it wassuggested that chitin thus could be a recognition element implicated in allergic and helminth immunity. However, very little is known about how chitin-induced immune signalling is initiated or propagated.Aim: The aim of this project is to investigate the hypothesis that chitin immune signalling may be initiated by the FIBCD1 chitin receptor through activation ofNF-jB signalling and downstream synthesis of mucosal epithelial-derived cytokines, TSLP and IL-33, which shapes the local accumulation and activation of Th2 responses.Results: Initial experiments have focused on the establishment of stable FIBCD1 overexpression in HEK293, HCT-116 and A549 epithelial cell lines. Chitin fragments obtained from shrimp shells were produced by brief sonication followed by filtration through 100, 70 and 40 lm filters respectively. Size distribution was determined by fluorescence-activated cell sorting. Cell lines will now be exposed to chitin fragments of varying size or the model ligand acetylated BSA, at different time intervals anddoses and using a luciferase reporter system detection of NFjB activation will be performed and cytokine expression will be quantified via qRT-PCR.Perspectives: Improved understanding of epithelialimmune and inflammatory modulation in response to chitin may provide new strategies for therapeutic intervention of allergic or parasitic disease.

AB - Background: FIBCD1 is a type II transmembrane protein located on the brush border of intestinal epithelial cells. FIBCD1 binds specifically to acetylated compoundssuch as chitin through the C-terminal fibrinogen-related domain. Chitin is a highly acetylated homopolymeric b-1,4-N-acetylglucosamine carbohydrate, which next to cellulose is the most abundant biopolymer found in nature, eg in fungi and parasites. It was recently demonstrated that chitin induces the accumulation in tissue of IL-4-expressing innate immune cells in vivo and it wassuggested that chitin thus could be a recognition element implicated in allergic and helminth immunity. However, very little is known about how chitin-induced immune signalling is initiated or propagated.Aim: The aim of this project is to investigate the hypothesis that chitin immune signalling may be initiated by the FIBCD1 chitin receptor through activation ofNF-jB signalling and downstream synthesis of mucosal epithelial-derived cytokines, TSLP and IL-33, which shapes the local accumulation and activation of Th2 responses.Results: Initial experiments have focused on the establishment of stable FIBCD1 overexpression in HEK293, HCT-116 and A549 epithelial cell lines. Chitin fragments obtained from shrimp shells were produced by brief sonication followed by filtration through 100, 70 and 40 lm filters respectively. Size distribution was determined by fluorescence-activated cell sorting. Cell lines will now be exposed to chitin fragments of varying size or the model ligand acetylated BSA, at different time intervals anddoses and using a luciferase reporter system detection of NFjB activation will be performed and cytokine expression will be quantified via qRT-PCR.Perspectives: Improved understanding of epithelialimmune and inflammatory modulation in response to chitin may provide new strategies for therapeutic intervention of allergic or parasitic disease.

M3 - Conference abstract for conference

ER -