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Background: The epithelial rests of Malassez (ERM) are derived from the Hertwig's epithelial root sheath during tooth development. The ERM contain endothelial nitric oxide synthase (eNOS), but the existence of phosphorylation site/s of eNOS in the ERM is unclear. Methods: Rat molars with periodontium were perfusion- and post-fixed, decalcified, and frozen-sectioned. Free-floating sections were incubated using antisera against total eNOS, eNOS phosphorylated at serine (Ser)1177 Ser116 and threonine (Thr)495. The signal intensities of t-eNOS, p-eNOS at Ser1177 and Ser116 in the ERM were measured by densitometry and statistically analyzed. Results: In the ERM, localization of total eNOS and the phosphorylation sites of eNOS at Ser1177 and Ser116 were detected, while a basal localization of eNOS phosphorylated at Thr495 in the ERM was undetectable. For p-eNOS at Ser116 regional differences in phosphorylation were detected. Conclusions: The basal production of NO by eNOS in the ERM is modulated by phosphorylation of eNOS at Ser1177 and Ser116 residues, while the basal activity of the eNOS is not influenced by phosphorylation of eNOS at Thr495 residue. This provides evidence that phosphorylation plays a key role for regulation of the catalytic activity of eNOS. [ABSTRACT FROM AUTHOR]

Korkmaz Y, Bloch W, Behrends S, Schröder H, Addicks K, Baumann MA. NO-cGMP signaling molecules in the rat epithelial rests of Malassez. Eur J Oral Sci 2004; 112: 55–60.© Eur J Oral Sci, 2004 The epithelial rests of Malassez (ERM) are derived from the disintegrating epithelial root sheath of Hertwig that guides root formation during tooth development. Low concentrations of nitric oxide (NO) produced by NO-synthase I (NOS I) and NOS III activate intracellular soluble guanylate cyclase (sGC) to produce intracellular cyclic guanosine 3′:5′-monophosphate (cGMP), which triggers rapid cellular responses such as cell proliferation, cell differentiation, and apoptosis under physiological conditions. The presence of NOS I–III, sGC (α2- and β1-subunits) and cGMP in the ERM was investigated by immunohistochemistry. Rat molars with periodontium were perfusion and postfixed, decalcified, frozen-sectioned, and sections were immunostained. NOS I, NOS III, sGC (α2- and β1-subunits) and cGMP were localized with different densities in the ERM. The presence of NOS II in the ERM varied. The localization of NOS I, NOS III, sGC and cGMP in the ERM indicates an involvement of NO and/or NO-cGMP signal pathway molecules in homeostasis of a variety of physiological processes in the ERM. These could include regulation of cell proliferation, cell differentiation and apoptosis. [ABSTRACT FROM AUTHOR]