Human odontoblasts express transient receptor protein and acid-sensing ion channel mechanosensor proteins

Diverse proteins of the denegerin/epithelial sodium channel (DEG/ENa+C) superfamily, in particular those belonging to the acid‐sensing ion channel (ASIC) family, as well as some members of the transient receptor protein (TRP) channel, function as mechanosensors or may be required for mechanosensatio...

Full description

Saved in:
Bibliographic Details
Published in:Microscopy research and technique Vol. 74; no. 5; pp. 457 - 463
Main Authors: Solé-Magdalena, Antonio, Revuelta, Enrique G., Menénez-Díaz, Ivan, Calavia, Marta G., Cobo, Teresa, García-Suárez, Olivia, Pérez-Piñera, Pablo, De Carlos, Felix, Cobo, Juan, Vega, Jose A.
Format: Journal Article
Language:English
Published: Hoboken Wiley Subscription Services, Inc., A Wiley Company 01-05-2011
Subjects:
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Diverse proteins of the denegerin/epithelial sodium channel (DEG/ENa+C) superfamily, in particular those belonging to the acid‐sensing ion channel (ASIC) family, as well as some members of the transient receptor protein (TRP) channel, function as mechanosensors or may be required for mechanosensation in a diverse range of species and cell types. Therefore, we investigated the putative mechanosensitive function of human odontoblasts using immunohistochemistry to detect ENa+C subunits (α, β, and γ) and ASIC (1, 2, 3, and 4) proteins, as well as TRPV4, in these cells. Positive and specific immunoreactivity in the odontoblast soma and/or processes was detected for all proteins studied except α‐ENa+C. The intensity of immunostaining was high for β‐ENa+C and ASIC2, whereas it was low for ASIC1, ASIC3, γ‐ENa+C, and TRPV4, being absent for α‐ENa+C and ASIC4. These results suggest that human odontoblasts in situ express proteins related to mechanosensitive channels that probably participate in the mechanisms involved in teeth sensory transmission. Microsc. Res. Tech., 2011. © 2010 Wiley‐Liss, Inc.
Bibliography:ark:/67375/WNG-WJK830F9-0
istex:27AB8DC7206BF89902CE9125E02E5E5ECAF0708B
ArticleID:JEMT20931
ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-1
content type line 23
ObjectType-Article-1
ObjectType-Feature-2
ISSN:1059-910X
1097-0029
1097-0029
DOI:10.1002/jemt.20931