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Literature summary for 3.1.4.4 extracted from

  • Park, S.Y.; Cho, J.H.; Ma, W.; Choi, H.J.; Han, J.S.
    Phospholipase D2 acts as an important regulator in LPS-induced nitric oxide synthesis in Raw 264.7 cells (2010), Cell. Signal., 22, 619-628.
    View publication on PubMed
Search for more literature for 3.1.4.4

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of PLD1, PLD2, and their dominant negative forms into Raw 264.7 cells Mus musculus

Protein Variants

Protein Variants Comment Organism
additional information transfection of PLD1, PLD2, and their dominant negative forms into Raw 264.7 cells, only PLD2 overexpression, but not that of PLD1, increases NO synthesis and iNOS expression. LPS-induced NO synthesis and iNOS expression are blocked by PLD2 siRNA, suggesting that LPS upregulates NO synthesis through PLD2. Knockdown of PLD2 with siRNA also decreases phosphorylation of S6K1, p42/44 MAPK and STAT3 induced by LPS Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
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-
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Source Tissue

Source Tissue Comment Organism Textmining
macrophage
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 Mus musculus
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RAW-264.7 cell
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 Mus musculus
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Synonyms

Synonyms Comment Organism
phospholipase D2
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 Mus musculus
PLD2
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 Mus musculus

General Information

General Information Comment Organism
physiological function importance and activating role of PLD2 for LPS-induced NO synthesis in Raw 264.7 cells with involvement of the S6K1-p42/44 MAPK-STAT3 pathway. Binding of transcription factor STAT3 to the iNOS promoter is mediated by PLD2 Mus musculus