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Fibronectin stimulates TRPV1 translocation in primary sensory neurons
Author(s) -
Jeske Nathaniel A.,
Patwardhan Amol M.,
Henry Michael A.,
Milam Stephen B.
Publication year - 2009
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.2008.05779.x
Subject(s) - trpv1 , microbiology and biotechnology , fibronectin , tyrosine phosphorylation , signal transduction , chemistry , receptor , phosphorylation , tyrosine , integrin , capsaicin , transient receptor potential channel , biology , extracellular matrix , biochemistry
Extracellular matrix (ECM) molecules are highly variable in their composition and receptor recognition. Their ubiquitous expression profile has been linked to roles in cell growth, differentiation, and survival. Recent work has identified certain ECM molecules that serve as dynamic signal modulators, versus the more‐recognized role of chronic modulation of signal transduction. In this study, we investigated the role that fibronectin (FN) plays in the dynamic modulation of transient receptor potential family V type 1 receptor (TRPV1) translocation to the plasma membrane in trigeminal ganglia (TG) sensory neurons. Confocal immunofluorescence analyses identify co‐expression of the TRPV1 receptor with integrin subunits that bind FN. TG neurons cultured upon or treated with FN experienced a leftward shift in the EC 50 of capsaicin‐stimulated neuropeptide release. This FN‐induced increase in TRPV1 sensitivity to activation is coupled by an increase in plasma membrane expression of TRPV1, as well as an increase in tyrosine phosphorylation of TRPV1 in TG neurons. Furthermore, TG neurons cultured on FN demonstrated an increase in capsaicin‐mediated Ca 2+ accumulation relative to neurons cultured on poly‐ d ‐lysine. Data presented from these studies indicate that FN stimulates tyrosine‐phosphorylation‐dependent translocation of the TRPV1 receptor to the plasma membrane, identifying FN as a critical component of the ECM capable of sensory neuron sensitization.