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
AUTHORS (7)
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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