Fibronectin stimulates TRPV1 translocation in primary sensory neurons

Nathaniel A. Jeske, Amol M Patwardhan, Michael A. Henry, Stephen B. Milam

Research output: Contribution to journalArticle

17 Citations (Scopus)

Abstract

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 EC50 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 Ca2+ 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.

Original languageEnglish (US)
Pages (from-to)591-600
Number of pages10
JournalJournal of Neurochemistry
Volume108
Issue number3
DOIs
StatePublished - Feb 2009
Externally publishedYes

Fingerprint

Sensory Receptor Cells
Fibronectins
Neurons
Trigeminal Ganglion
Cell membranes
Extracellular Matrix
Phosphorylation
Capsaicin
Cell Membrane
Tyrosine
Modulation
Signal transduction
Molecules
Cell growth
Neuropeptides
Integrins
Modulators
Lysine
Fluorescent Antibody Technique
Cell Differentiation

Keywords

  • Fibronectin
  • Integrin
  • Pain
  • Src
  • Transient receptor potential family V type 1 receptor

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience

Cite this

Fibronectin stimulates TRPV1 translocation in primary sensory neurons. / Jeske, Nathaniel A.; Patwardhan, Amol M; Henry, Michael A.; Milam, Stephen B.

In: Journal of Neurochemistry, Vol. 108, No. 3, 02.2009, p. 591-600.

Research output: Contribution to journalArticle

Jeske, Nathaniel A. ; Patwardhan, Amol M ; Henry, Michael A. ; Milam, Stephen B. / Fibronectin stimulates TRPV1 translocation in primary sensory neurons. In: Journal of Neurochemistry. 2009 ; Vol. 108, No. 3. pp. 591-600.
@article{003051cde6494d0eace8ab07adbabece,
title = "Fibronectin stimulates TRPV1 translocation in primary sensory neurons",
abstract = "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 EC50 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 Ca2+ 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.",
keywords = "Fibronectin, Integrin, Pain, Src, Transient receptor potential family V type 1 receptor",
author = "Jeske, {Nathaniel A.} and Patwardhan, {Amol M} and Henry, {Michael A.} and Milam, {Stephen B.}",
year = "2009",
month = "2",
doi = "10.1111/j.1471-4159.2008.05779.x",
language = "English (US)",
volume = "108",
pages = "591--600",
journal = "Journal of Neurochemistry",
issn = "0022-3042",
publisher = "Wiley-Blackwell",
number = "3",

}

TY - JOUR

T1 - Fibronectin stimulates TRPV1 translocation in primary sensory neurons

AU - Jeske, Nathaniel A.

AU - Patwardhan, Amol M

AU - Henry, Michael A.

AU - Milam, Stephen B.

PY - 2009/2

Y1 - 2009/2

N2 - 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 EC50 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 Ca2+ 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.

AB - 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 EC50 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 Ca2+ 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.

KW - Fibronectin

KW - Integrin

KW - Pain

KW - Src

KW - Transient receptor potential family V type 1 receptor

UR - http://www.scopus.com/inward/record.url?scp=58149328528&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=58149328528&partnerID=8YFLogxK

U2 - 10.1111/j.1471-4159.2008.05779.x

DO - 10.1111/j.1471-4159.2008.05779.x

M3 - Article

C2 - 19012739

AN - SCOPUS:58149328528

VL - 108

SP - 591

EP - 600

JO - Journal of Neurochemistry

JF - Journal of Neurochemistry

SN - 0022-3042

IS - 3

ER -