| Predicate | Object |
|---|---|
| rdf:type | |
| biopax3:comment |
Phospholipase C enzymes (PLCs) catalyze the cleavage of |FRAME: PHOSPHATIDYL-MYO-INOSITOL-45-BISPHOSPHA "phosphatidylinositol-4,5-bisphosphate"| and result in the release of |FRAME: DIACYLGLYCEROL "1,2-diacylglycerol"| (DAG) and |FRAME: INOSITOL-1-4-5-TRISPHOSPHATE| (IP3 ) from membranes in response to receptor activation. This in turn results in activation of protein kinase C and the release of |FRAME: CA+2| from intracellular stores. Several distinct classes of PLCs that specifically react with phosphatidylinositols are known to exist in mammals. They have ben named the β γ. δ, ε, ζ and η classes |CITS:[11395409][12117804][17895620]|. As of 2007, thirteen isoforms have been described |CITS: [17895620]|. The delta-type phospholipase C is thought to be the least evolved form in the mammalian PLC family. The enzyme binds to its substrates with a high affinity via its pleckstrin homology (PH) domain. Several mutant forms of the proteins have been generated |CITS: [9588182][7890667]|. Inhibition of PKC-δ-mediated signaling by a dominant negative mutant or the PKC-δ inhibitor rottlerin blocked most of the estrogen-induced activation of mitogen-activated protein kinase (Erk/MAPK) |CITS: [11960991]|. The |FRAME: HS07195| gene encoding this enzyme has been mapped to chromosome 3, and its structure has been described |CITS: [9345909]|.
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| biopax3:dataSource | |
| biopax3:displayName |
phospholipase Cδ1
|
| biopax3:name |
PLC-δ-1,
PLC-III,
phospholipase C, delta 1
|
| biopax3:entityReference | |
| biopax3:standardName |
phospholipase Cδ1
|