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Information on EC 3.1.4.11 - phosphoinositide phospholipase C and Organism(s) Rattus norvegicus and UniProt Accession P10686

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     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.4 Phosphoric-diester hydrolases
                3.1.4.11 phosphoinositide phospholipase C
IUBMB Comments
These enzymes form some of the cyclic phosphate Ins(cyclic1,2)P(4,5)P2 as well as Ins(1,4,5)P3. They show activity towards phosphatidylinositol, i.e., the activity of EC 4.6.1.13, phosphatidylinositol diacylglycerol-lyase, in vitro at high [Ca2+]. Four beta-isoforms regulated by G-proteins, two gamma-forms regulated by tyrosine kinases, four delta-forms regulated at least in part by calcium and an epsilon-form, probably regulated by the oncogene ras, have been found.
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This record set is specific for:
Rattus norvegicus
UNIPROT: P10686
Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The taxonomic range for the selected organisms is: Rattus norvegicus
Synonyms
1-phosphatidyl-D-myo-inositol 4,5-bisphosphate inositoltrisphosphohydrolase, 1-phosphatidyl-D-myo-inositol-4,5-bisphosphate inositoltrisphosphohydrolase, 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase, 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-1, AtPLC1, AtPLC2, AtPLC3, AtPLC4, AtPLC5, AtPLC6, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1-phosphatidyl-D-myo-inositol 4,5-bisphosphate inositoltrisphosphohydrolase
-
-
-
-
1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase
-
-
-
-
Ca2 +-dependent phosphatidylinositol phosphodiesterase
248
-
No receptor potential A protein
-
-
-
-
PH-PLCdelta1
248
-
phosphatidylinositol 4,5-bisphosphate phosphodiesterase
-
-
-
-
phosphatidylinositol phosphodiesterase
phosphatidylinositol-4,5-bisphosphate phosphodiesterase
-
-
-
-
phosphatidylinositol-4,5-bisphosphate phospholipase C
-
-
-
-
phosphatidylinositol-phosphodiesterase
248
-
phosphatidylinositol-specific phospholipase C
248
-
phosphodiesterase, triphosphoinositide
-
-
-
-
phosphoinositidase C
-
-
-
-
phosphoinositide specific phospholipase C
248
-
phosphoinositide-specific phospholipase C
282135
-
phosphoinositide-specific phospholipase C beta1
282135
-
phospholipase C
phospholipase C beta1
248
-
phospholipase C-beta1
248
-
phospholipase C-epsilon
248
-
phospholipase C-eta
248
-
phospholipase Cbeta1
282135
-
phosphotidylinositol 4,5-bisphosphate-specific phospholipase C
-
-
-
-
PI-PLC beta 1
282135
-
PI-PLC beta1
PI-PLC beta3
PI-PLC beta4
PI-PLC delta1
282143
-
PI-PLC delta3
248
-
PI-PLC delta4
282144
-
PI-PLC epsilon
274825
-
PI-PLC gamma1
PI-PLC gamma2
248
-
PI-PLC-beta1
248
-
PIC
-
-
-
-
PIP2 PDE
-
-
-
-
PIP2 phosphodiesterase
-
-
-
-
PIPLC
-
-
-
-
PLC beta1
PLC beta1b
248
-
PLC beta3
282140
-
PLC delta1
282143
-
PLC gamma1
282142
-
PLC-148
-
-
-
-
PLC-154
-
-
-
-
PLC-85
-
-
-
-
PLC-delta1
248
-
PLC-epsilon
248
-
PLC-gamma1
248
-
PLCbeta1
PLCdelta1
248
-
PLCdeta1
248
-
PLCgamma1
248
-
pleckstrin homology-phospholipase C-delta1
248
-
polyphosphoinositide phospholipase C
-
-
-
-
PtdIns phosphodiesterase
248
-
PtdIns(4,5)P2-directed phospholipase C
-
-
-
-
triphosphoinositide phosphodiesterase
-
-
-
-
additional information
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
1-phosphatidyl-1D-myo-inositol-4,5-bisphosphate inositoltrisphosphohydrolase
These enzymes form some of the cyclic phosphate Ins(cyclic1,2)P(4,5)P2 as well as Ins(1,4,5)P3. They show activity towards phosphatidylinositol, i.e., the activity of EC 4.6.1.13, phosphatidylinositol diacylglycerol-lyase, in vitro at high [Ca2+]. Four beta-isoforms regulated by G-proteins, two gamma-forms regulated by tyrosine kinases, four delta-forms regulated at least in part by calcium and an epsilon-form, probably regulated by the oncogene ras, have been found.
CAS REGISTRY NUMBER
COMMENTARY hide
37213-51-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
show the reaction diagram
-
-
-
-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
show the reaction diagram
arachidonoylphosphatidylinositol + H2O
myo-inositol 1-phosphate + 1,2-diarachidonoylglycerol
show the reaction diagram
-
-
-
?
phosphatidylinositol + H2O
1D-myo-inositol 1-phosphate
show the reaction diagram
phosphatidylinositol + H2O
1D-myo-inositol 1-phosphate + diacylglycerol
show the reaction diagram
phosphatidylinositol + H2O
1D-myo-inositol 1-phosphate + glycerophosphoinositol + phosphate
show the reaction diagram
-
-
ratio between products decreased with increasing pH, 1D-myo-inositol 1,2-cyclic phosphate is also formed
-
?
phosphatidylinositol + H2O
?
show the reaction diagram
phosphatidylinositol + H2O
diacylglycerol + 1D-myo-inositol 1-phosphate
show the reaction diagram
-
enzyme is specific for phosphatidylinositol
-
-
?
phosphatidylinositol 4,5-bisphosphate + H2O
?
show the reaction diagram
-
enzyme activities for phosphatidylinositol 4,5-bisphosphate are strongly dependent on the relative levels of calcium and pH in the assay buffer
-
-
?
phosphatidylinositol 4,5-bisphosphate + H2O
D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
show the reaction diagram
phosphatidylinositol 4-phosphate
?
show the reaction diagram
phosphatidylinositol 4-phosphate + H2O
1D-myo-inositol 4,5-bisphosphate + diacylglycerol
show the reaction diagram
-
-
-
-
?
phosphatidylinositol 4-phosphate + H2O
?
show the reaction diagram
-
PLC-delta1, structure of the catalytic domain
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
-
stimulates
NaCl
-
inhibits phosphatidylinositol hydrolysis of low molecular weight PLC. Conversely, PIP2 hydrolysis is stimulated by increasing concentrations of NaCl
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-O-octadecyl-2-O-methyl-sn-glycero-3-phosphorylcholine
-
histamine-induced elevation of plasma noradrenaline and adrenaline is dose-dependently reduced by ET-18-OCH3
aggregated amyloid beta protein
-
full-length Abeta 1-40, aggregated form inhibits Ca2+-regulated phosphoinositide degradation by cytosolic and membrane-bound PLC by 30-40%, inhibitor may interact with the Ca2+-binding site of enzyme, no inhibition by nonaggregated soluble full-length amyloid beta protein
-
ATP
-
1-5 mM
Blood lipoprotein
-
enzyme is strongly inhibited by blood plasma, serum and blood lipoproteins
-
Blood plasma
-
enzyme is strongly inhibited by blood plasma, serum and blood lipoproteins
-
Blood serum
-
enzyme is strongly inhibited by blood plasma, serum and blood lipoproteins
-
Ca2+
-
above 0.1 mM
choline plasmalogen
-
18.5% of choline plasmalogen is needed for 50% inhibition
lysocholine plasmalogen
-
8.5% of choline plasmalogen is needed for 50% inhibition
-
lysophosphatidylcholine
NaCl
-
inhibits phosphatidylinositol hydrolysis of low molecular weight PLC. Conversely, PIP2 hydrolysis is stimulated by increasing concentrations of NaCl
neomycin
-
-
oleoyl sphingomyelin
-
-
phosphatidylcholine
sphingomyelin
-
50% inhibition at low concentration, and 97% at high concentration
sphingosylphosphocholine
-
-
stearoyl sphingomyelin
-
-
U-73122
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
albumin
-
maximal activation of hydrolysis of phosphatidylinositol 4,5-diphosphate at 0.0125 mg/ml
-
Ca2+
-
requirement of all PLCs, the delta isoenzymes are most sensitive to Ca2+
cytochrome c
-
maximal activation of hydrolysis of phosphatidylinositol 4,5-diphosphate at 0.0125 mg/ml
decanoylglycerophosphate
-
only little activating effect
decanoyllysophosphatidylcholine
-
C10 lysophosphatidylcholine activates the reaction
deoxycholate
diacylglycerol
-
5-6fold stimulation of rat brain phosphatidylinositol phosphodiesterase. The addition of choline phospholipids containing two long hydrophobic chains or choline lysophospholipids containing one long hydrophobic chain produced a total inhibition of the activation which had been produced by diacylglycerol
dihexanoylglycerophosphocholine
-
-
Epidermal growth factor
stimulates PLCepsilon overexpressed in COS-7 cells
histone
-
maximal activation of hydrolysis of phosphatidylinositol 4,5-diphosphate at 0.0125 mg/ml
oleic acid
-
causes a marked stimulation of the enzyme activity when the membrane-bound substrate is used
oleoylglycerophosphate
-
activates the hydrolysis at a physiological pH
palmitoylglycerophosphate
-
activates the hydrolysis at a physiological pH
phosphatidic acid
-
activates the hydrolysis at a physiological pH
phosphatidylethanolamine
-
activates the hydrolysis. Human platelet phosphatidylinositol phosphodiesterase
Q61L H-Ras
constitutively active Q61L H-Ras stimulates PLCepsilon co-expressed in COS-7 cells in parallel with Ras binding
-
RhoA
-
PLC-epsilon is a direct downstream efector for RhoA. RhA-dependent activation of PLC-epsilon depends on a unique insert within the catalytic core of the phospholipase
soluble amyloid beta protein fragment 25-35
-
activates PI-PLC
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.006
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
-
25°C, pH 7.4
0.012 - 0.035
phosphatidylinositol
0.058 - 0.182
phosphatidylinositol 4,5-bisphosphate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.1
-
isoenzyme PLC-gamma
11.4
-
isoenzyme PLC-beta1
28.97
-
phosphatidylinositol as substrate, last purification step
204.1
-
phosphatidylinositol 4,5-bisphosphate as substrate, last purification step
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 5.5
5
-
high molecular PLC (157 kDa), phosphatidylinositol as substrate
5.6
-
when (NH4)2SO4 fractionation (30-50%) of the brain supernatant is carried out, the phosphodiesterase preparation obtained shows an optimum at pH 5.6
6
-
at the higher calcium concentration the pH optimum for phosphatidylinositol 4,5-bisphosphate hydrolysis is 6.0
6.5 - 7
-
hydrolysis of phosphatidylinositol, isoenzyme PLC-beta1 in presence of 0.6 mg/ml sodium deoxycholate, isoenzyme PLC-gamma in presence of 0.4 mg/ml sodium deoxycholate
6.8
-
brain enzyme
7 - 8.5
7.5
-
hydrolysis of phosphatidylinositol 4,5-diphosphate, in presence of 0.1 mM CaCl2
7.8
-
assay at, phosphatidylinositol as substrate
additional information
-
activity at higher pH values requires higher calcium concentrations and disappears on purification of the soluble enzyme by ammonium sulfate fractionation
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 7.5
-
pH 4.5: about 25% of maximal activity, pH 7.5: about 55% of maximal activity, hydrolysis of phosphatidylinositol 4,5-diphosphate
5.3 - 7.7
-
about 45% of maximal activity at pH 5.3 and pH 7.7
6 - 11
-
pH: 6.0: about 10% of maximal activity, pH 11.0: about 40% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.8 - 4.2
-
4 peaks of phosphodiesterase activity are found at pl ranges 7.2-7.4 , 5.8-6.0, 4.4-4.8 and 3.8-4.2, pH 5.5
4.4 - 4.8
-
4 peaks of phosphodiesterase activity are found at pl ranges 7.2-7.4 , 5.8-6.0, 4.4-4.8 and 3.8-4.2, pH 5.5
4.6
-
when assayed at pH 7.0 and pH 8.0, 1 mM Ca2+
5.86
-
4 peaks of phosphodiesterase activity are found at pl ranges 7.2-7.4 , 5.8-6.0, 4.4-4.8 and 3.8-4.2, pH 5.5
7.2 - 7.4
-
4 peaks of phosphodiesterase activity are found at pl ranges 7.2-7.4 , 5.8-6.0, 4.4-4.8 and 3.8-4.2, pH 5.5
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SWissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
PLC delta3 and delta4
Manually annotated by BRENDA team
-
PI-PLC expression pattern, overview
Manually annotated by BRENDA team
-
frontal cortex, single inescapable shock reduces PI-PLC activity in the frontal cortex and hippocampus of learned helplessness rats. Repeated inescapable shock not only reduced PI-PLC activity but also selectively decreases the expression of PLCbeta1 and PLCgamma1 isozymes
Manually annotated by BRENDA team
-
PLC delta3 and delta4
Manually annotated by BRENDA team
-
C6Bu-1 rat glioma cell, isoenzyme PI-PLC-beta1
Manually annotated by BRENDA team
-
rapidly growing hepatoma 3924A
Manually annotated by BRENDA team
-
single inescapable shock reduces PI-PLC activity in the frontal cortex and hippocampus of learned helplessness rats. Repeated inescapable shock not only reduced PI-PLC activity but also selectively decreases the expression of PLCbeta1 and PLCgamma1 isozymes
Manually annotated by BRENDA team
-
C2C12 rat myoblast, isoenzyme PI-PLC-beta1
Manually annotated by BRENDA team
neonatal rat ventricular myocyte, NRVM
Manually annotated by BRENDA team
-
expression of PLC delta
Manually annotated by BRENDA team
expression of PLCepsilon
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PLCbeta1b targets to the sarcolemma and is enriched in caveolae
Manually annotated by BRENDA team
-
the PH domain of PLC-delta1 may tether the enzyme to the cell membrane by specific binding to phosphatidylinositol 4,5-bisphosphate
-
Manually annotated by BRENDA team
-
PLC-delta1
Manually annotated by BRENDA team
PLCbeta1b targets to the sarcolemma and is enriched in caveolae
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
isoforms of PI-PLC family display different expression and/or sub cellular distribution under non-physiological conditions such as the rat astrocytes activation during neurodegeneration, the tumoural progression of some neoplasms and the inflammatory cascade activation after lipopolysaccharide administration. PI-PLC beta3 and PI-PLC gamma2 isoforms, whose expression and sub cellular localization significantly differ after U73122 inhibitor treatment
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
PLCG1_RAT
1290
0
148548
Swiss-Prot
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
135000
-
Western blot analysis
58000
-
SDS-PAGE, low molecular weight PLC hydrolyzes both phosphatidylinositol and phosphatidylinositol 4,5-bisphosphate has a molecular mass of 58 kDa. Cloning techniques have tentatively identified the low molecular weight peak as PLC-alpha
66000
-
low molecular PLC by size exclusion chromatography
85000
-
Western blot analysis
140000
two splice variants, PLCbeta1a (150 kDa) and PLCbeta1b (140 kDa). Western Blot
145000
-
high molecular PLC shows much greater activity against phosphatidylinositol than phosphatidylinositol 4,5-bisphosphate and is active at lower calcium concentrations
150000
157000
-
high molecular PLC by size exclusion chromatography
255000
x * 255000, PLCepsilon, calculated from the amino acid sequence and Western blot analysis
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 255000, PLCepsilon, calculated from the amino acid sequence and Western blot analysis
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
-
an early increase in PLC-beta1b activity (6 h after partial hepatectomy) in nuclear matrix is associated with serine phosphorylation of the enzyme; the increase in the PLC-gamma1 activity measured at 6 h and 20 h after partial hepatectomy is associated with tyrosine phosphorylation of the enzyme
side-chain modification
-
rat brain protein kinase C phosphorylates phosphoinositidase gamma but not phosphoinositidase beta1
CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
2.4 A structure of phospholipase Cdelta1
-
of phosphatidylinositide-specific phospholipase deltaDELTA1-134
-
PLC-delta1 complexed with inositol 1,4,5-trisphosphate
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H503A
-
mutant enzyme shows reduced affinity for phosphoinositide binding and reduced hydrolysis of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
K2150A
mutation in the Ras-binding domain 2 of PLCepsilon, reduced binding of Q61L H-Ras
K2150E
mutation in the Ras-binding domain 2 of PLCepsilon, reduced binding of Q61L H-Ras
K2152A
mutation in the Ras-binding domain 2 of PLCepsilon, reduced binding of Q61L H-Ras
K2152E
mutation in the Ras-binding domain 2 of PLCepsilon, reduced binding of Q61L H-Ras
P500A
-
mutant enzyme shows reduced affinity for phosphoinositide binding and reduced hydrolysis of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
additional information
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Partially purified PLC can be stored in buffer C at -80°C for several months without appreciable loss of activity. However, repeated freezing and thawing has a deleterious effect on enzyme activity. More purified PLC (Mono Q and size exclusion fractions) can be stored at 4°C for 5-7 days with a gradual loss of activity
-
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
enzyme form beta3; enzyme subtype beta1 and beta 3 from brain, enzyme subtype beta2 from HL60 cells
-
partially purified, DEAE-cellulose and heparin-Sepharose chromatographies followed by Mono Q and size exclusion HPLC
-
preparation of nuclei, method development
recombinant PLCepsilon
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
enzyme expression in Escherichia coli strain BL21 (DE3)
-
expression in COS-7 cells
-
PLCepsilon, expression in Sf-9 cells and in COS-7 cells
transfection of C2C12 cells with expression vectors containing PLC beta1 and with small interfering RNAs from regions of the PLC beta1 gene
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Divecha, N.; Rhee, S.G.; Letcher, A.J.; Irvine, R.F.
Phosphoinositide signalling enzymes in rat liver nuclei: phosphoinoeitidase C isoform beta1 is specifically, but not predominantly located in the nucleus
Biochem. J.
289
617-620
1993
Rattus norvegicus
-
Manually annotated by BRENDA team
Irvine, R.F.; Letcher, A.J.; Dawson, R.M.C.
Phosphatidylinositol-4,5-bisphosphate phosphodiesterase and phosphomonoesterase activities of rat brain. Some properties and possible control mechanisms
Biochem. J.
218
177-185
1984
Rattus norvegicus
Manually annotated by BRENDA team
Yang, H.; Shen, F.; Herenyiova, M.; Weber, G.
Phospholipase C (EC 3.1.4.11): A malignancy linked signal transduction enzyme
Anticancer Res.
18
1399-1404
1998
Rattus norvegicus
Manually annotated by BRENDA team
Downes, C.P.; Michell, R.H.
The polyphosphoinositide phosphodiesterase of erythrocyte membranes
Biochem. J.
198
133-140
1981
Homo sapiens, Oryctolagus cuniculus, Rattus norvegicus
Manually annotated by BRENDA team
Mazzoni, M.; Bertagnolo, V.; Neri, L.M.; Carini, C.; Marchisio, M.; Milani, D.; Manzoli, F.A.; Capitani, S.
Discrete subcellular localization of phosphoinositidase C beta, gamma and delta in PC12 rat pheochromocytoma cells
Biochem. Biophys. Res. Commun.
187
114-120
1992
Rattus norvegicus
Manually annotated by BRENDA team
Marker, A.J.; Galloway, E.; Palmer, S.; Nakamura, T.; Gould, G.W.; MacSween, R.N.M.; Bushfield, M.
Role of the adenylate cyclase, phosphoinositidase C and receptor tyrosyl kinase systems in the control of hepatocyte proliferation by hepatocyte growth factor
Biochem. Pharmacol.
44
1037-1043
1992
Rattus norvegicus
Manually annotated by BRENDA team
Blank, J.L.; Foster, K.A.; Hawthorne, J.N.
Purification, properties, and phosphorylation by protein kinase C of two phosphoinositidase C isoenzymes from rat brain
J. Neurochem.
57
15-21
1991
Rattus norvegicus
Manually annotated by BRENDA team
Sawaki, K.; Hiramatsu, Y.; Baum, B.J.; Ambudkar, I.S.
Involvement of GalphaQ/11 in m3-muscarinic receptor stimulation of phosphotidylinositol 4,5-bisphosphate-specific phospholipase C in rat parotid gland membranes
Arch. Biochem. Biophys.
305
546-550
1993
Rattus norvegicus
Manually annotated by BRENDA team
Smreka, A.V.; Sternweis, P.C.
Regulation of purified subtypes of phosphatidylinositol-specific phospholipase C beta by G protein alpha and betagamma subunits
J. Biol. Chem.
268
9667-9674
1993
Rattus norvegicus
Manually annotated by BRENDA team
Griendling, K.K.; Taubman, M.B.; Akers, M.; Mendlowitz, M.; Alexander, R.W.
Characterization of phosphatidylinositol-specific phospholipase C from cultured vascular smooth muscle cells
J. Biol. Chem.
266
15498-15504
1991
Rattus norvegicus
Manually annotated by BRENDA team
Grobler, J.A.; Hurley, J.H.
Expression, characterization, and crystallization of the catalytic core of rat phosphatidylinositide-specific phospholipase C delta1
Protein Sci.
5
680-686
1996
Rattus norvegicus
Manually annotated by BRENDA team
Essen, L.O.; Perisic, O.; Cheung, R.; Katan, M.; Williams, R.L.
Crystal structure of a mammalian phosphoinositide-specific phospholipase Cdelta
Nature
18
595-602
1996
Rattus norvegicus
Manually annotated by BRENDA team
Dawson, R.M.C.; Hemington, N.; Irvine, R.F.
The inhibition of diacylglycerol-stimulated intracellular phospholipases by phospholipids with a phosphocholine-containing polar group. A possible physiological role for sphingomyelin
Biochem. J.
230
61-68
1985
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Shute, J.K.; Smith, M.E.
Phosphatidylinositol phosphodiesterase in isolated plasma membranes of rodent skeletal muscle
Biochem. Soc. Trans.
13
193-194
1985
Mus musculus, Mus musculus C57BL, Rattus norvegicus, Rattus norvegicus Sprague-Dawley
-
Manually annotated by BRENDA team
Shute, J.K.; Smith, M.E.
Soluble phosphatidylinositol phosphodiesterase in normal and denervated fast and slow muscles of the rat
Biochem. J.
222
299-305
1984
Rattus norvegicus
Manually annotated by BRENDA team
Schwertz, D.W.; Kreisberg, J.I.; Venkatachalam, M.A.
Characterization of rat kidney proximal tubule brush border membrane-associated phosphatidylinositol phosphodiesterase
Arch. Biochem. Biophys.
224
555-567
1983
Rattus norvegicus
Manually annotated by BRENDA team
Hirasawa, K.; Irvine, R.F.; Dawson, R.M.C.
Heterogeneity of the calcium-dependent phosphatidylinositol phosphodiesterase in rat brain
Biochem. J.
205
437-442
1982
Rattus norvegicus
Manually annotated by BRENDA team
Hirasawa, K.; Irvine, R.F.; Dawson, R.M.C.
The catabolism of phosphatidylinisitol by an EDTA-insensitive phospholipase A1 and calcium-dependent phosphatidylinositol phosphodiesterase in rat brain
Eur. J. Biochem.
120
53-58
1981
Rattus norvegicus
Manually annotated by BRENDA team
Dawson, R.M.C.; Hemington, N.; Irvine, R.F.
The inhibition and activation of Ca2+-dependent phosphatidylinositol phosphodiesterase by phospholipids and blood plasma
Eur. J. Biochem.
112
33-38
1980
Rattus norvegicus
Manually annotated by BRENDA team
Quinn, P.J.; Barenholz, Y.
A comparison of the activity of phosphatidylinositol phosphodiesterase against substrate in dispersions and as monolayers at the air-water interface
Biochem. J.
149
199-208
1975
Rattus norvegicus
Manually annotated by BRENDA team
Ochocka, A.M.; Pawelczyk, T.
Isozymes delta of phosphoinositide-specific phospholipase C and their role in signal transduction in the cell
Acta Biochim. Pol.
50
1097-1110
2003
Bos taurus, Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Rhee, S.G.
Regulation of phosphoinositide-specific phospholipase C
Annu. Rev. Biochem.
70
281-312
2001
Homo sapiens, Mammalia, Rattus norvegicus, Rattus norvegicus PLC-delta1
Manually annotated by BRENDA team
Kelley, G.G.; Reks, S.E.; Ondrako, J.M.; Smrcka, A.V.
Phospholipase C(epsilon): a novel Ras effector
EMBO J.
20
743-754
2001
Rattus norvegicus (Q99P84), Rattus norvegicus PLCepsilon (Q99P84)
Manually annotated by BRENDA team
Zambrzycka, A.; Strosznajder, R.P.; Strosznajder, J.B.
Aggregated beta amyloid peptide 1-40 decreases Ca2+- and cholinergic receptor-mediated phosphoinositide degradation by alteration of membrane and cytosolic phospholipase C in brain cortex
Neurochem. Res.
25
189-196
2000
Rattus norvegicus
Manually annotated by BRENDA team
Rebecchi, M.J.; Pentyala, S.N.
Structure, function, and control of phosphoinositide-specific phospholipase C
Physiol. Rev.
80
1291-1335
2000
Arabidopsis thaliana, Dictyostelium discoideum, Drosophila sp. (in: Insecta), Homo sapiens, Mus musculus, Rattus norvegicus, Saccharomyces cerevisiae, Saccharomyces cerevisiae PLC1p
Manually annotated by BRENDA team
Crljen, V.; Visnjic, D.; Banfic, H.
Presence of different phospholipase C isoforms in the nucleus and their activation during compensatory liver growth
FEBS Lett.
571
35-42
2004
Rattus norvegicus
Manually annotated by BRENDA team
Martelli, A.M.; Fiume, R.; Faenza, I.; Tabellini, G.; Evangelista, C.; Bortul, R.; Follo, M.Y.; Fala, F.; Cocco, L.
Nuclear phosphoinositide specific phospholipase C (PI-PLC)-beta 1: a central intermediary in nuclear lipid-dependent signal transduction
Histol. Histopathol.
20
1251-1260
2005
Cricetulus griseus, Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Kim, S.K.; Wee, S.M.; Chang, J.S.; Kwon, T.K.; Min do, S.; Lee, Y.H.; Suh, P.G.
Point mutations in the split PLC-gamma1 PH domain modulate phosphoinositide binding
J. Biochem. Mol. Biol.
37
720-725
2004
Rattus norvegicus
Manually annotated by BRENDA team
Thore, S.; Dyachok, O.; Tengholm, A.
Oscillations of phospholipase C activity triggered by depolarization and Ca2+ influx in insulin-secreting cells
J. Biol. Chem.
279
19396-19400
2004
Rattus norvegicus
Manually annotated by BRENDA team
Seifert, J.P.; Wing, M.R.; Snyder, J.T.; Gershburg, S.; Sondek, J.; Harden, T.K.
RhoA activates purified phospholipase C-epsilon by a guanine nucleotide-dependent mechanism
J. Biol. Chem.
279
47992-47997
2004
Rattus norvegicus
Manually annotated by BRENDA team
Hains, M.D.; Wing, M.R.; Maddileti, S.; Siderovski, D.P.; Harden, T.K.
G{alpha}12/13- and Rho-dependent activation of phospholipase C-{epsilon} by lysophosphatidic acid and thrombin receptors
Mol. Pharmacol.
69
2068-2075
2006
Rattus norvegicus
Manually annotated by BRENDA team
Dwivedi, Y.; Mondal, A.C.; Rizavi, H.S.; Shukla, P.K.; Pandey, G.N.
Single and repeated stress-induced modulation of phospholipase C catalytic activity and expression: role in LH behavior
Neuropsychopharmacology
30
473-483
2005
Rattus norvegicus
Manually annotated by BRENDA team
Rogel, A.; Bromberg, Y.; Sperling, O.; Zoref-Shani, E.
Phospholipase C is involved in the adenosine-activated signal transduction pathway conferring protection against iodoacetic acid-induced injury in primary rat neuronal cultures
Neurosci. Lett.
373
218-221
2005
Rattus norvegicus
Manually annotated by BRENDA team
Cai, Y.; Stafford, L.J.; Bryan, B.A.; Mitchell, D.; Liu, M.
G-protein-activated phospholipase C-beta, new partners for cell polarity proteins Par3 and Par6
Oncogene
24
4293-4300
2005
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Cocco, L.; Faenza, I.; Fiume, R.; Billi, A.M.; Gilmour, R.S.; Manzoli, F.A.
Phosphoinositide-specific phospholipase C (PI-PLC) beta 1 and nuclear lipid-dependent signaling
Biochim. Biophys. Acta
1761
509-521
2006
Mus musculus (Q9Z1B3), Rattus norvegicus (P10687)
Manually annotated by BRENDA team
Faenza, I.; Ramazzotti, G.; Bavelloni, A.; Fiume, R.; Gaboardi, G.C.; Follo, M.Y.; Gilmour, R.S.; Martelli, A.M.; Ravid, K.; Cocco, L.
Inositide-dependent phospholipase C signaling mimics insulin in skeletal muscle differentiation by affecting specific regions of the cyclin D3 promoter
Endocrinology
148
1108-1117
2007
Rattus norvegicus
Manually annotated by BRENDA team
Shimizu, T.; Yamaguchi, N.; Okada, S.; Lu, L.; Sasaki, T.; Yokotani, K.
Roles of brain phosphatidylinositol-specific phospholipase C and diacylglycerol lipase in centrally administered histamine-induced adrenomedullary outflow in rats
Eur. J. Pharmacol.
571
138-144
2007
Rattus norvegicus
Manually annotated by BRENDA team
Lo Vasco, V.R.; Fabrizi, C.; Artico, M.; Cocco, L.; Billi, A.M.; Fumagalli, L.; Manzoli, F.A.
Expression of phosphoinositide-specific phospholipase C isoenzymes in cultured astrocytes
J. Cell. Biochem.
100
952-959
2007
Rattus norvegicus (P10686), Rattus norvegicus (P10687), Rattus norvegicus (P10688), Rattus norvegicus (Q62711), Rattus norvegicus (Q99JE6), Rattus norvegicus (Q99P84), Rattus norvegicus (Q9QW07), Rattus norvegicus
Manually annotated by BRENDA team
Stewart, A.J.; Morgan, K.; Farquharson, C.; Millar, R.P.
Phospholipase C-eta enzymes as putative protein kinase C and Ca2+ signalling components in neuronal and neuroendocrine tissues
Neuroendocrinology
86
243-248
2007
Chlorocebus aethiops, Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Grubb, D.R.; Vasilevski, O.; Huynh, H.; Woodcock, E.A.
The extreme C-terminal region of phospholipase Cbeta1 determines subcellular localization and function; the b splice variant mediates alpha1-adrenergic receptor responses in cardiomyocytes
FASEB J.
22
2768-2774
2008
Rattus norvegicus (P10687)
Manually annotated by BRENDA team
Nelson, C.P.; Nahorski, S.R.; Challiss, R.A.
Temporal profiling of changes in phosphatidylinositol 4,5-bisphosphate, inositol 1,4,5-trisphosphate and diacylglycerol allows comprehensive analysis of phospholipase C-initiated signalling in single neurons
J. Neurochem.
107
602-615
2008
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Singal, T.; Dhalla, N.S.; Tappia, P.S.
Regulation of c-Fos and c-Jun gene expression by phospholipase C activity in adult cardiomyocytes
Mol. Cell. Biochem.
327
229-239
2009
Rattus norvegicus (P10686), Rattus norvegicus (P10687), Rattus norvegicus (P10688), Rattus norvegicus (Q99JE6)
Manually annotated by BRENDA team
Baumann, M.K.; Swann, M.J.; Textor, M.; Reimhult, E.
Pleckstrin homology-phospholipase C-delta1 interaction with phosphatidylinositol 4,5-bisphosphate containing supported lipid bilayers monitored in situ with dual polarization interferometry
Anal. Chem.
83
6267-6274
2011
Rattus norvegicus
Manually annotated by BRENDA team
Lo Vasco, V.R.; Fabrizi, C.; Panetta, B.; Fumagalli, L.; Cocco, L.
Expression pattern and sub-cellular distribution of phosphoinositide specific phospholipase C enzymes after treatment with U-73122 in rat astrocytoma cells
J. Cell. Biochem.
110
1005-1012
2010
Rattus norvegicus
Manually annotated by BRENDA team
Fiume, R.; Teti, G.; Faenza, I.; Cocco, L.
Phosphoinositide-specific phospholipase C beta1 signal transduction in the nucleus
Methods Mol. Biol.
645
143-164
2010
Homo sapiens, Homo sapiens (Q9NQ66), Mus musculus (Q9Z1B3), Rattus norvegicus (P10687)
Manually annotated by BRENDA team
Fukami, K.; Inanobe, S.; Kanemaru, K.; Nakamura, Y.
Phospholipase C is a key enzyme regulating intracellular calcium and modulating the phosphoinositide balance
Prog. Lipid Res.
49
429-437
2010
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
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