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Characterization of basal pseudopod-like processes in ileal and colonic PYY cells.

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Date
2011-02
Authors
Bohórquez, Diego V
Chandra, Rashmi
Samsa, Leigh Ann
Vigna, Steven R
Liddle, Rodger A
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Abstract
The peptide tyrosine tyrosine (PYY) is produced and secreted from L cells of the gastrointestinal mucosa. To study the anatomy and function of PYY-secreting L cells, we developed a transgenic PYY-green fluorescent protein mouse model. PYY-containing cells exhibited green fluorescence under UV light and were immunoreactive to antibodies against PYY and GLP-1 (glucagon-like peptide-1, an incretin hormone also secreted by L cells). PYY-GFP cells from 15 μm thick sections were imaged using confocal laser scanning microscopy and three-dimensionally (3D) reconstructed. Results revealed unique details of the anatomical differences between ileal and colonic PYY-GFP cells. In ileal villi, the apical portion of PYY cells makes minimal contact with the lumen of the gut. Long pseudopod-like basal processes extend from these cells and form an interface between the mucosal epithelium and the lamina propria. Some basal processes are up to 50 μm in length. Multiple processes can be seen protruding from one cell and these often have a terminus resembling a synapse that appears to interact with neighboring cells. In colonic crypts, PYY-GFP cells adopt a spindle-like shape and weave in between epithelial cells, while maintaining contact with the lumen and lamina propria. In both tissues, cytoplasmic granules containing the hormones PYY and GLP-1 are confined to the base of the cell, often filling the basal process. The anatomical arrangement of these structures suggests a dual function as a dock for receptors to survey absorbed nutrients and as a launching platform for hormone secretion in a paracrine fashion.
Type
Journal article
Subject
Animals
Colon
Enteroendocrine Cells
Glucagon-Like Peptide 1
Green Fluorescent Proteins
Ileum
Intestinal Mucosa
Mice
Mice, Transgenic
Peptide YY
Protein Transport
Pseudopodia
Permalink
https://hdl.handle.net/10161/9383
Published Version (Please cite this version)
10.1007/s10735-010-9302-6
Publication Info
Bohórquez, Diego V; Chandra, Rashmi; Samsa, Leigh Ann; Vigna, Steven R; & Liddle, Rodger A (2011). Characterization of basal pseudopod-like processes in ileal and colonic PYY cells. J Mol Histol, 42(1). pp. 3-13. 10.1007/s10735-010-9302-6. Retrieved from https://hdl.handle.net/10161/9383.
This is constructed from limited available data and may be imprecise. To cite this article, please review & use the official citation provided by the journal.
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Scholars@Duke

Bohorquez

Diego V. Bohorquez

Associate Professor in Medicine
I am a gut-brain neuroscientist. Though my initial studies focused on GI physiology and nutrition, my expertise evolved to include neuroscience following the many personal stories, which have carefully sharpened my career vision along the way.  While pursuing a Doctoral degree in Nutrition, a friend shared her struggles with obesity and gastric bypass surgery.  Surgery was a last resort but helped to reduced her body weight dramatically and resolved her diabe
Liddle

Rodger Alan Liddle

Professor of Medicine
Our laboratory has two major research interests:Enteroendocrine Cell Biology Enteroendocrine cells (EECs) are sensory cells of the gut that send signals throughout the body.  They have the ability to sense food and nutrients in the lumen of the intestine and secrete hormones into the blood.  Our laboratory has had a longstanding interest in two types of EECs that regulate satiety and signal the brain to stop eating.   Chole

Steven R. Vigna

Associate Professor of Cell Biology
We are interested in the mechanisms of signal transduction of neuropeptides and peptide hormones, mechanisms of receptor regulation, and the role of receptor regulation in health and disease. The major peptide of interest is the neurotransmitter substance P which is involved in gastrointestinal tract regulation, pain pathways, inflammation, and central nervous system functions. Our major focus is at the level of the receptors for this peptide. We are currently studying mechanisms of subst
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