Document Detail


Expression of neurexin, neuroligin, and their cytoplasmic binding partners in the pancreatic beta-cells and the involvement of neuroligin in insulin secretion.
MedLine Citation:
PMID:  18755801     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The composition of the beta-cell exocytic machinery is very similar to that of neuronal synapses, and the developmental pathway of beta-cells and neurons substantially overlap. beta-Cells secrete gamma-aminobutyric acid and express proteins that, in the brain, are specific markers of inhibitory synapses. Recently, neuronal coculture experiments have identified three families of synaptic cell-surface molecules (neurexins, neuroligins, and SynCAM) that drive synapse formation in vitro and that control the differentiation of nascent synapses into either excitatory or inhibitory fully mature nerve terminals. The inhibitory synapse-like character of the beta-cells led us to hypothesize that members of these families of synapse-inducing adhesion molecules would be expressed in beta-cells and that the pattern of expression would resemble that associated with neuronal inhibitory synaptogenesis. Here, we describe beta-cell expression of the neuroligins, neurexins, and SynCAM, and show that neuroligin expression affects insulin secretion in INS-1 beta-cells and rat islet cells. Our findings demonstrate that neuroligins and neurexins are expressed outside the central nervous system and help confer an inhibitory synaptic-like phenotype onto the beta-cell surface. Analogous to their role in synaptic neurotransmission, neurexin-neuroligin interactions may play a role in the formation of the submembrane insulin secretory apparatus.
Authors:
Arthur T Suckow; Davide Comoletti; Megan A Waldrop; Merrie Mosedale; Sonya Egodage; Palmer Taylor; Steven D Chessler
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2008-08-28
Journal Detail:
Title:  Endocrinology     Volume:  149     ISSN:  0013-7227     ISO Abbreviation:  Endocrinology     Publication Date:  2008 Dec 
Date Detail:
Created Date:  2008-11-21     Completed Date:  2009-03-31     Revised Date:  2013-03-14    
Medline Journal Info:
Nlm Unique ID:  0375040     Medline TA:  Endocrinology     Country:  United States    
Other Details:
Languages:  eng     Pagination:  6006-17     Citation Subset:  AIM; IM    
Affiliation:
Department of Medicine, Biomedical Sciences Graduate Program, University of California, San Diego, La Jolla, California 92093, USA.
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MeSH Terms
Descriptor/Qualifier:
Alternative Splicing
Animals
Blotting, Western
Brain / metabolism
Carrier Proteins / genetics,  metabolism
Cell Adhesion Molecules, Neuronal / genetics,  metabolism*
Cell Line, Tumor
Glycoproteins / genetics,  metabolism
Guanylate Kinase / genetics,  metabolism
Humans
Insulin / secretion*
Insulin-Secreting Cells / metabolism*
Membrane Proteins / genetics,  metabolism
Microscopy, Confocal
Nerve Tissue Proteins / genetics,  metabolism*
Neuropeptides / genetics,  metabolism
RNA Interference
Rats
Reverse Transcriptase Polymerase Chain Reaction
Grant Support
ID/Acronym/Agency:
5P30 AI36214/AI/NIAID NIH HHS; DK063491-4S1/DK/NIDDK NIH HHS; P30 NS047101/NS/NINDS NIH HHS; R01 DK080971-04/DK/NIDDK NIH HHS
Chemical
Reg. No./Substance:
0/Carrier Proteins; 0/Cell Adhesion Molecules, Neuronal; 0/Glycoproteins; 0/Insulin; 0/Membrane Proteins; 0/NLGN4X protein, human; 0/Nerve Tissue Proteins; 0/Neuropeptides; 0/gephyrin; 0/neurexin II; 0/neurexophilin; 0/neuroligin 1; 0/neuroligin 2; 0/neuroligin 3; 156532-79-5/neurexin IIIbeta; 156532-80-8/neurexin Ibeta; EC 2.7.4.-/CASK kinases; EC 2.7.4.8/Guanylate Kinase
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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