Localization of the NO‐cGMP Signaling Pathway Molecules, NOS III‐Phosphorylation Sites, ERK1/2, and Akt/PKB in Osteoclasts

Male 0301 basic medicine Osteoclasts Protein Serine-Threonine Kinases Nitric Oxide Second Messenger Systems Rats 3. Good health Immunoenzyme Techniques 03 medical and health sciences Guanylate Cyclase Alveolar Process Animals Nitric Oxide Synthase Phosphorylation Rats, Wistar Cyclic GMP
DOI: 10.1902/jop.2004.75.8.1119 Publication Date: 2005-02-02T13:01:31Z
ABSTRACT
Background: Nitric oxide (NO) mediates different cellular functions by activating soluble guanylate cyclase (sGC) that converts guanosine‐5'‐ triphosphate (GTP) to cyclic guanosine‐3', 5'‐monophosphate (cGMP). Membrane‐bound GCs produce cGMP in response natriuretic peptides osteoblasts, but neither the NO‐target enzyme sGC, nor phosphorylation sites of NOS III, their regulation extracellular signalregulated kinases 1 and 2 (ERK1/2) Akt/protein kinase B (Akt/PKB) osteoclasts have been established. Methods: Rat molars with periodontium were perfusion‐ postfixed, decalcified, frozen‐sectioned. Free‐floating sections stained using nicotinamide adenine dinucleotide phosphate‐diaphorase (NADPH‐d) tartrate‐resistant acid phosphatase (TRAP) histochemical techniques immunoreacted antisera against NOsynthase (NOS) I‐III, III phoshorylated at Thr 495 , Serine 1177 (Ser ), ERK1/2, phosphorylated Akt/PKB, sGC (α /β cGMP. Results: NADPH‐d staining immunostaining Ser β ‐subunits), detected osteoclasts. Immunohistochemical reaction products for threonine (Thr ) ERK1/2 could not be identified Comparison TRAP activity ‐subunit revealed is only expressed a subpopulation Conclusions: NO likely generated I The inconstant expression II some may explained inducible upon physiological cell activation. Localization α ‐ ‐subunits compatible an involvement NO‐sGC signaling homeostasis site Akt/PKB are involved production under basal conditions. J Periodontol 2004;75:1119‐1125 .
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