RGD Reference Report - Role of naofen, a novel WD repeat-containing protein, in reducing nitric oxide-induced relaxation. - Rat Genome Database

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Role of naofen, a novel WD repeat-containing protein, in reducing nitric oxide-induced relaxation.

Authors: Feng, GG  Yamada, M  Wongsawatkul, O  Li, C  Huang, L  An, J  Komatsu, T  Fujiwara, Y  Naohisa, I 
Citation: Feng GG, etal., Clin Exp Pharmacol Physiol. 2008 Dec;35(12):1447-53. doi: 10.1111/j.1440-1681.2008.05008.x. Epub 2008 Jul 29.
RGD ID: 11553926
Pubmed: PMID:18671723   (View Abstract at PubMed)
DOI: DOI:10.1111/j.1440-1681.2008.05008.x   (Journal Full-text)

1. Naofen, a novel WD40 repeat domain-containing protein, has recently been found in the intracellular compartment. The aim of the present study was to determine whether naofen affects thoracic aortic vascular reactivity in normotensive and hypertensive rats and whether naofen is present in the thoracic aorta. In addition, we examined whether naofen modulates acetylcholine (ACh)-stimulated nitric oxide (NO) release from the endothelium. 2. Immunohistochemistry showed greater naofen expression in endothelial cells in the DOCA-salt group compared with controls. There was increased naofen mRNA expression in deoxycorticosterone acetate (DOCA)-salt hypertensive rats compared with normotensive rats. 3. Acetylcholine-induced relaxation of rat aortic strips was decreased in DOCA-salt hypertensive rats compared with normotensive rats. Naofen-N- but not naofen-C-terminal protein caused a significant decrease in ACh-induced relaxation of aortic strips from normotensive rats. 4. Using a nitrite assay in a murine aortic endothelial cell line demonstrated that naofen-N-terminal protein, but not naofen-C-terminal protein, significantly reduced ACh-induced NO production, suggesting that naofen interferes with NO production. 5. Administration of naofen-N-terminal protein, but not naofen-C-terminal protein, significantly inhibited cyclohydrolase (GCH) I mRNA expression in a murine aortic endothelial cell line, suggesting that naofen-N-terminal protein interferes with NO synthesis by inhibiting GCH I mRNA expression. 6. The results of the present study suggest that naofen is present in vascular endothelial cells and has an inhibitory effect on ACh-induced relaxation under normotensive conditions. The findings reinforce the functional significance of naofen-N-terminal protein on rat vascular reactivity.



Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Wdr35Ratnegative regulation of gene expression  IDA Gch1RGD 
Wdr35Ratnegative regulation of nitric oxide biosynthetic process  IDA  RGD 
Wdr35Ratpositive regulation of vasoconstriction  IDA  RGD 

Objects Annotated

Genes (Rattus norvegicus)
Wdr35  (WD repeat domain 35)


Additional Information