Epithelial sodium channels (ENaCs) are a subfamily of ion channels within the degenerin/ENaC (DEG/ENaC) superfamily. Previous studies have shown the immunolocalization of ENaC in the neural elements of the cutaneous mechanoreceptors as well as dorsal root and trigeminal ganglion neurons, indicating the involvement of this molecule in mechanotransduction. The present study examined the expression of ENaCβ, a major component of ENaC protein, in the mechanoreceptive Ruffini endings in the periodontal ligament of the rat incisors by immunohistochemistry. The expression of ENaCβ in the trigeminal ganglion-which innervates the periodontal Ruffini endings-was also investigated at the mRNA and protein levels. Furthermore, double staining and a nerve injury experiment were applied to clarify its detailed localization in the periodontal Ruffini endings. ENaCβ immunoreaction in the trigeminal ganglion was recognizable in the comparatively large neurons which have been considered to mediate mechanotransduction. Immunohistochemistry for ENaCβ demonstrated dendritic ramifications of the Ruffini endings as well as the rounded cells in the periodontal ligament. Double staining with ENaCβ and either PGP9.5 or S-100 protein showed immunoreaction for ENaCβ in both the axonal and glial elements in the periodontal ligament. Some ENaCβ positive cells with rounded profiles were reactive to non-specific cholinesterase activity. Furthermore, a transection of the inferior alveolar nerve failed to eliminate the rounded cells with ENaCβ reaction, indicating that they were the terminal Schwann cells associated with the periodontal Ruffini endings. These findings suggest that ENaCβ is a key mechanotransducing channel in the periodontal Ruffini endings. Probably, the terminal Schwann cells together with the axon terminals regulate mechanotransduction in the periodontal endings.Epithelial sodium channels (ENaCs) are members of the degenerin/ENaC (DEG/ENaC) family of voltage-insensitive, amiloride-blockable cation channels (21, 25). They are generally composed of four subunits: ENaCα, β, γ and δ. These ENaC subunits have a conserved topology consisting of two membrane-spanning domains with intracellular N-and C-termini and a large glycosylated extracellular region. Of these channels, a heterotetramer containing two ENaCα, one ENaCβ and one ENaCγ shows high sensitivity to amiloride and its analogues (21,25). However, the function of ENaCδ remains unknown though this subunit can also form a functional ion channel. Many studies have shown a wide distribution of ENaCs in various tissues where their expression at the apical membrane mediates unidirectional absorption of Na + (9, 15). These ENaCs can also be regarded as key mechanotransducing channels came from the findings that the mutation
Removing water from these subjects would promote sustained sympathetic nervous overactivity. These findings indicate that the UFR during HD needs to be set at ≤15 ml/h/kg.
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