NDLI: P2Y2 nucleotide receptor activation enhances the aggregation and self-organization of dispersed salivary epithelial cells.

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P2Y2 nucleotide receptor activation enhances the aggregation and self-organization of dispersed salivary epithelial cells.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	El-Sayed, Farid G. Camden, Jean M. Woods, Lucas T. Khalafalla, Mahmoud G. Petris, Michael J. Erb, Laurie Weisman, Gary A.
Description	Author Affiliation: El-Sayed FG ( Department of Biochemistry, University of Missouri, Columbia, Missouri); Camden JM ( Department of Biochemistry, University of Missouri, Columbia, Missouri); Woods LT ( Department of Biochemistry, University of Missouri, Columbia, Missouri); Khalafalla MG ( Department of Biochemistry, University of Missouri, Columbia, Missouri); Petris MJ ( Department of Biochemistry, University of Missouri, Columbia, Missouri); Erb L ( Department of Biochemistry, University of Missouri, Columbia, Missouri); Weisman GA ( Department of Biochemistry, University of Missouri, Columbia, Missouri)
Abstract	Hyposalivation resulting from salivary gland dysfunction leads to poor oral health and greatly reduces the quality of life of patients. Current treatments for hyposalivation are limited. However, regenerative medicine to replace dysfunctional salivary glands represents a revolutionary approach. The ability of dispersed salivary epithelial cells or salivary gland-derived progenitor cells to self-organize into acinar-like spheres or branching structures that mimic the native tissue holds promise for cell-based reconstitution of a functional salivary gland. However, the mechanisms involved in salivary epithelial cell aggregation and tissue reconstitution are not fully understood. This study investigated the role of the P2Y2 nucleotide receptor (P2Y2R), a G protein-coupled receptor that is upregulated following salivary gland damage and disease, in salivary gland reconstitution. In vitro results with the rat parotid acinar Par-C10 cell line indicate that P2Y2R activation with the selective agonist UTP enhances the self-organization of dispersed salivary epithelial cells into acinar-like spheres. Other results indicate that the P2Y2R-mediated response is dependent on epidermal growth factor receptor activation via the metalloproteases ADAM10/ADAM17 or the 5ß1 integrin/Cdc42 signaling pathway, which leads to activation of the MAPKs JNK and ERK1/2. Ex vivo data using primary submandibular gland cells from wild-type and P2Y2R(-/-) mice confirmed that UTP-induced migratory responses required for acinar cell self-organization are mediated by the P2Y2R. Overall, this study suggests that the P2Y2R is a promising target for salivary gland reconstitution and identifies the involvement of two novel components of the P2Y2R signaling cascade in salivary epithelial cells, the 5ß1 integrin and the Rho GTPase Cdc42.
File Format	HTM / HTML
ISSN	03636143
e-ISSN	15221563
DOI	10.1152/ajpcell.00380.2013
Journal	American Journal of Physiology - Cell Physiology
Issue Number	1
Volume Number	307
Language	English
Publisher	American Physiological Society
Publisher Date	2014-07-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Discipline Cell Biology Cell Aggregation Drug Effects Cell Movement Epithelial Cells Parotid Gland Purinergic P2y Receptor Agonists Pharmacology Receptors, Purinergic P2y2 Submandibular Gland Uridine Triphosphate Adam Proteins Antagonists & Inhibitors Metabolism Animals Cell Line Extracellular Signal-regulated Map Kinases Integrin Alpha5beta1 Jnk Mitogen-activated Protein Kinases Mice Mice, Inbred C57bl Mice, Knockout Cytology Phosphorylation Protease Inhibitors Protein Kinase Inhibitors Receptor, Epidermal Growth Factor Deficiency Genetics Transfection Cdc42 Gtp-binding Protein Research Support, N.i.h., Extramural
Content Type	Text
Resource Type	Article
Subject	Cell Biology Physiology

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