scholarly journals N‐formyl peptide receptor‐1 is important for homeostasis of intestinal epithelial cells

2012 ◽  
Vol 26 (S1) ◽  
Author(s):  
Ashfaqul Alam ◽  
Giovanna Leoni ◽  
Christy Wentworth ◽  
Asma Nusrat ◽  
Andrew Neish
Keyword(s):  
Epithelial Cells ◽  
Intestinal Epithelial Cells ◽  
Formyl Peptide Receptor ◽  
Intestinal Epithelial ◽  
Peptide Receptor ◽  
Formyl Peptide

scholarly journals Salmonella typhimurium attachment to human intestinal epithelial monolayers: transcellular signalling to subepithelial neutrophils.

1993 ◽  
Vol 123 (4) ◽  
pp. 895-907 ◽  
Author(s):  
B A McCormick ◽  
S P Colgan ◽  
C Delp-Archer ◽  
S I Miller ◽  
J L Madara
Keyword(s):  
Epithelial Cells ◽  
Salmonella Typhimurium ◽  
Apical Membrane ◽  
Coli Strain ◽  
Formyl Peptide Receptor ◽  
Human Neutrophils ◽  
Classical Pathway ◽  
Intestinal Epithelial ◽  
Formyl Peptide

In human intestinal disease induced by Salmonella typhimurium, transepithelial migration of neutrophils (PMN) rapidly follows attachment of the bacteria to the epithelial apical membrane. In this report, we model those interactions in vitro, using polarized monolayers of the human intestinal epithelial cell, T84, isolated human PMN, and S. typhimurium. We show that Salmonella attachment to T84 cell apical membranes did not alter monolayer integrity as assessed by transepithelial resistance and measurements of ion transport. However, when human neutrophils were subsequently placed on the basolateral surface of monolayers apically colonized by Salmonella, physiologically directed transepithelial PMN migration ensued. In contrast, attachment of a non-pathogenic Escherichia coli strain to the apical membrane of epithelial cells at comparable densities failed to stimulate a directed PMN transepithelial migration. Use of the n-formyl-peptide receptor antagonist N-t-BOC-1-methionyl-1-leucyl-1- phenylalanine (tBOC-MLP) indicated that the Salmonella-induced PMN transepithelial migration response was not attributable to the classical pathway by which bacteria induce directed migration of PMN. Moreover, the PMN transmigration response required Salmonella adhesion to the epithelial apical membrane and subsequent reciprocal protein synthesis in both bacteria and epithelial cells. Among the events stimulated by this interaction was the epithelial synthesis and polarized release of the potent PMN chemotactic peptide interleukin-8 (IL-8). However, IL-8 neutralization, transfer, and induction experiments indicated that this cytokine was not responsible for the elicited PMN transmigration. These data indicate that a novel transcellular pathway exists in which subepithelial PMN respond to lumenal pathogens across a functionally intact epithelium. Based on the known unique characteristics of the intestinal mucosa, we speculate that IL-8 may act in concert with an as yet unidentified transcellular chemotactic factor(s) (TCF) which directs PMN migration across the intestinal epithelium.

scholarly journals Expression and localization of VPAC1, the major receptor of vasoactive intestinal peptide along the length of the intestine

2017 ◽  
Vol 313 (1) ◽  
pp. G16-G25 ◽  
Author(s):  
Dulari Jayawardena ◽  
Grace Guzman ◽  
Ravinder K. Gill ◽  
Waddah A. Alrefai ◽  
Hayat Onyuksel ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Vasoactive Intestinal Peptide ◽  
Intestinal Epithelial Cells ◽  
Mrna Levels ◽  
Intestinal Epithelial ◽  
Peptide Receptor ◽  
Mouse Colon ◽  
Mouse Intestine ◽  
Vasoactive Intestinal Peptide Receptor ◽  
Apical Localization

Vasoactive intestinal peptide (VIP) is an endogenous neuropeptide with a broad array of physiological functions in many organs including the intestine. Its actions are mediated via G protein-coupled receptors, and vasoactive intestinal peptide receptor 1 (VPAC1) is the key receptor responsible for majority of VIP’s biological activity. The distribution of VPAC1 along the length of the gastrointestinal tract and its subcellular localization in intestinal epithelial cells have not been fully characterized. The current studies were undertaken to determine VPAC1 distribution and localization so that VIP-based therapies can be targeted to specific regions of the intestine. The results indicated that the mRNA levels of VPAC1 showed an abundance pattern of colon > ileum > jejunum in the mouse intestine. In parallel, the VPAC1 protein levels were higher in the mouse colon, followed by the ileum and jejunum. Immunofluorescence studies in mouse colon demonstrated that the receptor was specifically localized to the luminal surface, as was evident by colocalization with the apical marker villin but not with the basolateral marker Na+/K+-ATPase. In the human intestine, VPAC1 mRNA expression exhibited a distribution similar to that in mouse intestine and was highest in the sigmoid colon. Furthermore, in the human colon, VPAC1 also showed predominantly apical localization. The physiological relevance of the expression and apical localization of VPAC1 remains elusive. We speculate that apical VPAC1 in intestinal epithelial cells may have relevance in recognizing secreted peptides in the intestinal lumen and therefore supports the feasibility of potential therapeutic and targeting use of VIP formulations via oral route to treat gastrointestinal diseases. NEW & NOTEWORTHY These studies for the first time present comprehensive data on the relative characterization of vasoactive intestinal peptide (VIP) receptors in the intestinal mucosa. Vasoactive intestinal peptide receptor 1 (VPAC1) was identified as the predominant receptor with higher levels in the colon compared with the small intestine and was mainly localized to the apical membrane. In addition, the findings in the human tissues were consistent with VPAC1 expression in the mouse intestine and open possibilities to target colonic tissues with VIP for treating diseases such as inflammatory bowel disease.

scholarly journals Formyl Peptide Receptor Ligands Promote Wound Closure in Lung Epithelial Cells

2011 ◽  
Vol 44 (3) ◽  
pp. 264-269 ◽  
Author(s):  
Guohong Shao ◽  
Mark W. Julian ◽  
Shengying Bao ◽  
Meghan K. McCullers ◽  
Ju-Ping Lai ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Wound Closure ◽  
Lung Epithelial Cells ◽  
Formyl Peptide Receptor ◽  
Receptor Ligands ◽  
Peptide Receptor ◽  
Lung Epithelial ◽  
Formyl Peptide

Three-dimensional organization and functional relationships of endocytotic compartments in pig intestinal epithelial cells

1992 ◽  
Vol 50 (1) ◽  
pp. 576-577
Author(s):  
Julian P. Heath ◽  
Buford L. Nichols ◽  
László G. Kömüves
Keyword(s):  
Electron Microscopy ◽  
Epithelial Cells ◽  
Intestinal Epithelial Cells ◽  
Three Dimensional ◽  
Intestinal Epithelial ◽  
Cell Surfaces ◽  
Basal Surface ◽  
Functional Relationships

The newborn pig intestine is adapted for the rapid and efficient absorption of nutrients from colostrum. In enterocytes, colostral proteins are taken up into an apical endocytotic complex of channels that transports them to target organelles or to the basal surface for release into the circulation. The apical endocytotic complex of tubules and vesicles clearly is a major intersection in the routes taken by vesicles trafficking to and from the Golgi, lysosomes, and the apical and basolateral cell surfaces.Jejunal tissues were taken from piglets suckled for up to 6 hours and prepared for electron microscopy and immunocytochemistry as previously described.

Human and mouse intestinal epithelial cells (IEC) present glycolipid antigens to natural killer (NK)-T cells in a CD1d-restricted manner

2001 ◽  
Vol 120 (5) ◽  
pp. A37-A37
Author(s):  
Y VANDEWAL ◽  
R PITMAN ◽  
R HERSHBERG ◽  
S COLGAN ◽  
S BEHAR ◽  
...  
Keyword(s):  
T Cells ◽  
Epithelial Cells ◽  
Natural Killer ◽  
Intestinal Epithelial Cells ◽  
Intestinal Epithelial ◽  
Nk T Cells ◽  
Human And Mouse

Thrombin enhances migration of intestinal epithelial cells

2001 ◽  
Vol 120 (5) ◽  
pp. A504-A504
Author(s):  
A NEUMANN ◽  
M DEPKAPRONDZINSKI ◽  
C WILHELM ◽  
K FELGENHAUER ◽  
T CASPRITZ ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Intestinal Epithelial Cells ◽  
Intestinal Epithelial
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