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Information on EC 3.1.4.11 - phosphoinositide phospholipase C and Organism(s) Homo sapiens and UniProt Accession P51178

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EC Tree
     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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Homo sapiens
UNIPROT: P51178
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
pi-plc, phosphatidylinositol-specific phospholipase c, plc-gamma, plc-gamma1, plcgamma1, plc-beta, plcgamma, phosphoinositide-specific phospholipase c, plcgamma2, phospholipase c-gamma1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospholipase C-delta1
-
1-phosphatidyl-D-myo-inositol 4,5-bisphosphate inositoltrisphosphohydrolase
-
-
-
-
1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase
-
-
-
-
low molecular weight PI-PLC
-
-
No receptor potential A protein
-
-
-
-
phosphatidylinosite-specific phospholipase C
-
phosphatidylinositol 4,5-bisphosphate phosphodiesterase
-
-
-
-
phosphatidylinositol phosphodiesterase
-
-
phosphatidylinositol specific phospholipase C
-
-
phosphatidylinositol-4,5-bisphosphate phosphodiesterase
-
-
-
-
phosphatidylinositol-4,5-bisphosphate phospholipase C
-
-
-
-
phosphatidylinositol-specific phospholipase C
-
-
phosphatidylinositol-specific phospholipase C-beta
-
phosphatidylinositol-specific phospholipases C
-
-
phosphodiesterase, triphosphoinositide
-
-
-
-
phosphoinositidase C
-
-
-
-
phosphoinositide-phospholipase C
-
phosphoinositide-phospholipase C beta1
-
phosphoinositide-specific phospholipase C
-
-
phosphoinositide-specific phospholipase C beta1
-
phospholipase C
phospholipase C beta1
-
phospholipase C beta3
-
phospholipase C epsilon
-
phospholipase C-beta 2
-
phospholipase C-beta2
-
phospholipase C-beta3
-
-
phospholipase C-epsilon
-
-
phospholipase C-eta
-
-
phospholipase C-eta1a
-
phospholipase C-eta1b
-
phospholipase C-gamma1
-
phospholipase C-gamma2
phospholipase Cepsilon
-
-
phospholipase Cgamma1
-
-
phosphotidylinositol 4,5-bisphosphate-specific phospholipase C
-
-
-
-
PI-PLC
PI-PLC-ß1
-
-
PI-PLCbeta1
PI-PLCbeta2
-
isoform
PI-PLCbeta3
-
isoform
PI-PLCbeta4
-
PI-PLCc
-
-
PI-PLCdelta1
-
isoform
PI-PLCdelta3
-
isoform
PI-PLCepsilon
-
isoform
PI-PLCeta
-
isoform
PI-PLCgamma
-
isoform
PI-PLCgamma1
-
PI-PLCm
-
-
PI-PLCzeta
-
isoform
PI-specific phospholipase C
PIC
-
-
-
-
PIP2 PDE
-
-
-
-
PIP2 phosphodiesterase
-
-
-
-
PIPLC
-
-
-
-
PL-C
-
-
PLC beta1
-
-
PLC epsilon
-
PLC epsilon1a
PLC epsilon splice variant
PLC epsilon1b
PLC epsilon splice variant
PLC gamma1
-
-
PLC-148
-
-
-
-
PLC-154
-
-
-
-
PLC-85
-
-
-
-
PLC-beta1b
-
-
PLC-beta2
PLC-epsilon
-
-
PLC-eta1
-
-
PLC-eta2
-
-
PLC-gamma
-
-
PLC-gamma1
phospho-nephrin-binding protein
PLC-gamma2
-
PLCbeta1
PLCbeta2
-
isoform
PLCbeta3
-
isoform
PLCbeta4
-
isoform
PLCdelta1
PLCdelta3
-
isoform
PLCdelta4
-
isoform
PLCepsilon
PLCeta1
-
isoform
PLCeta2
-
isoform
PLCgamma
-
-
PLCgamma1
PLCgamma2
-
isoform
polyphosphoinositide phospholipase C
-
-
-
-
PtdIns(4,5)P2-directed phospholipase C
-
-
-
-
triphosphoinositide phosphodiesterase
-
-
-
-
additional information
-
four major types of PLC: beta, gamma, delta and epsilon
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -
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-acyl-2-arachidonoylphosphatidylinositol + H2O
?
show the reaction diagram
-
-
-
-
?
1-acyl-2-linoleoylphosphatidylinositol + H2O
?
show the reaction diagram
-
-
-
-
?
1-phosphatidyl-1D-myo-inositol + H2O
1D-myo-inositol 1-phosphate + diacylglycerol
show the reaction diagram
-
-
in almost equal amounts with 1D-myo-inositol 1,2-cyclic phosphate
-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1D-myo-inositol 1,4,5-triphosphate + 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
1-phosphatidyl-1D-myo-inositol 4-phosphate + H2O
1D-myo-inositol 1,4-bisphosphate + diacylglycerol
show the reaction diagram
-
-
-
-
?
1D-myo-inositol 1,4,5-trisphosphate fluorescent derivative WH-15 + H2O
1D-myo-inositol 1,4,5-trisphosphate + quinomethide + 6-aminoquinoline + ?
show the reaction diagram
-
-
-
-
ir
arachidonoyl-phosphatidylinositol + H2O
1,2-diarachidonoyl-sn-glycerol + 1D-myo-inositol 1-phosphate
show the reaction diagram
-
-
-
-
?
phosphatidylinositol + H2O
1D-myo-inositol 1-phosphate + diacylglycerol
show the reaction diagram
-
-
in vitro myo-inositol 1,2-cyclic phosphate also formed
-
?
phosphatidylinositol + H2O
1D-myo-inositol-1-phosphate + diacylglycerol
show the reaction diagram
-
-
in vitro 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
-
Pi-PLC (membrane) and Pi-PLC (cytosol) are specific for this substrate
-
-
?
phosphatidylinositol 4,5-bisphosphate
inositol 1,4,5-trisphosphate
show the reaction diagram
-
demonstration of the role of PLC in Ca2+-induced inactivation of TRPV6
-
-
?
phosphatidylinositol 4,5-bisphosphate + H2O
D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
show the reaction diagram
phosphatidylinositol 4-phosphate
?
show the reaction diagram
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-triphosphate + 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
1-phosphatidyl-1D-myo-inositol 4-phosphate + H2O
1D-myo-inositol 1,4-bisphosphate + diacylglycerol
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
(NH4)2SO4
-
high salt concentration, (NH4)2SO4, 2 M, dissociates the high molecular weight form yielding the low molecular form and increasing the specific activity
Mg2+
-
no requirement for the membrane enzyme solubilized with sodium cholate, activates the membrane enzyme after solubilization in octyl glucoside with maximal activity at 0.1 mM
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-(6-((17beta-3-methoxyestra-1,3,5(10)-trien-17-yl)amino)hexyl)-1H-pyrrole-2,5-dione
3beta,27-dihydroxyurs-12-en-28-oic acid
-
-
3beta,7'-diacetoxy-27- 4-(E)-coumaroyloxyurs-12-en-28-oic acid
-
-
3beta-4-(E)-coumaroyloxyurs-12-en-28-oic acid
-
-
3beta-hydroxy-27-(E)-feruloyloxyolea-12-en-28-oic acid
-
-
3beta-hydroxy-27-(E)-feruloyloxyurs-12-en-28-oic acid
-
-
3beta-hydroxy-27-(Z)-feruloyloxyolea-12-en-28-oic acid
-
-
3beta-hydroxy-27-(Z)-feruloyloxyurs-12-en-28-oic acid
-
-
3beta-hydroxy-27-4-(E)-2'-dihydrocoumaroyloxyurs-12-en-28-oic acid
-
-
3beta-hydroxy-27-4-(E)-coumaroyloxyolea-12-en-28-oic acid
-
-
3beta-hydroxy-27-4-(E)-coumaroyloxyurs-12-en-28-oic acid
-
-
3beta-hydroxy-27-4-(E)-coumaroyloxyurs-12-en-28-oic methyl ester
-
-
3beta-hydroxy-27-4-(Z)-coumaroyloxyolea-12-en-28-oic acid
-
-
3beta-hydroxy-27-4-(Z)-coumaroyloxyurs-12-en-28-oic acid
-
-
3beta-hydroxyurs-12-en-28-oic 4-(E)-coumaroyl ester
-
-
4-(E)-coumaric acid
-
-
48/80
-
compound 48/80, oligomeric mixture of condensation products of N-methyl-p-methoxyphenethylamine and formaldehyde
adriamycin
-
-
amentoflavone
-
-
Ba2+
-
-
camphor
-
inhibit the phospholipase C signaling
choline plasmalogen
-
18.5% of choline plasmalogen is needed for 50% inhibition
cinnamaldehyde
-
inhibit the phospholipase C signaling
deoxycholate
-
weak inhibition. Concentration of 2 mM inhibits the phospholipase C activity in all fractions by 20-30%
edelfosine
-
ET-18-OCH3, also inhibits Ca2+-induced inactivation of TRPV6
lysocholine plasmalogen
-
8.5% of choline plasmalogen is needed for 50% inhibition
-
lysophosphatidylcholine
-
50% inhibition is produced by 7% molar
menthol
-
inhibit the phospholipase C signaling
Mg2+
-
-
neomycin
oleoyl sphingomyelin
-
-
phosphatidylcholine
-
low effect, 50% inhibition is produced by 18% molar egg phosphatidylcholine
phosphatidylethanolamine
-
25% inhibition, in presence of 0.001 mM Ca2+
phosphatidylserine
-
50% inhibition, in presence of 0.001 mM Ca2+
putrescine
-
putrescine is less efficient than divalent cations in reducing isoform PLCbeta1 activity
spermidine
-
-
spermine
-
-
sphingomyelin
-
50% inhibition at 6.5% molar, and 97% at 20% molar
sphingosylphosphocholine
-
-
stearoyl sphingomyelin
-
-
U-73122
U-73343
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ARGHAP6
a GTPase-activating protein for RhoA. Activates PLC-gamma1 and increases the Vmax of PLC-beta1 and enhances its response to Ca2+ stimulation. ARHGAP6 protein binds to and up-regulates PLC-beta1 both under in vitro and in vivo conditions
-
2-nonenal
-
at 1-100 nM: activates PL-C in DMSO-differentiated HL-60 cells, at 1-10 nM: activates PL-C in undifferentiated HL-60 cells
4-hydroxynonenal
-
at 10-1000 nM, activates PL-C in both undifferentiated and DMSO-differentiated HL-60 cells
beta-estradiol
-
-
Ca2+
-
requirement of all PLCs, the delta isoenzymes are most sensitive to Ca2+
diacylglycerol
-
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
Epidermal growth factor
epidermal growth factor stimulates PI-PLC activity of both splice variants
G protein alpha12
-
activates PLC-epsilon
-
Gbetagamma
G protein betagamma subunits, the reconstituted enzymes, like wild-type PLC-beta2, are activated by Gbetagamma
-
phosphatidylethanolamine
phosphatidylserine
-
stimulation in presence of 1 mM Ca2+
PTEN
-
ubiquitously expressed tumor suppressor. PTEN overexpression results in changes in cellular phospholipid levels. Increased PTEN expression in unstimulated MCF-7 breast cancer cells results in a 51% increase in phosphatidic acid, with a decrease in phosphatidylcholine, PTEN activates also phospholipase D (PLD). PTEN induces translocation of PLC-gamma from the cytosol to the membrane
-
Ras
-
activator of PLC-epsilon
-
spermine
-
spermine potentiates the activity of isoform PLCgamma1
sphingosine 1-phosphate
sphingosine-1-phosphate stimulates PI-PLC activity of both splice variants
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0123 - 0.0391
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
0.1 - 0.15
1-phosphatidyl-1D-myo-inositol
-
-
0.143
phosphatidylinositol
-
-
0.031
phosphatidylinositol 4,5-bisphosphate
-
-
0.031
phosphatidylinositol 4-phosphate
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.001
phosphatidylserine
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.006
1-(6-((17beta-3-methoxyestra-1,3,5(10)-trien-17-yl)amino)hexyl)-1H-pyrrole-2,5-dione
Homo sapiens
-
significant inhibition of PLC-beta with IC50: 0.006 mM, little effect on PLC-beta1, PLC-beta3, or PLC-beta4
0.001 - 0.0666
3beta-hydroxy-27-(E)-feruloyloxyolea-12-en-28-oic acid
0.0028 - 0.0355
3beta-hydroxy-27-(E)-feruloyloxyurs-12-en-28-oic acid
0.0021 - 0.0503
3beta-hydroxy-27-(Z)-feruloyloxyolea-12-en-28-oic acid
0.0009 - 0.0441
3beta-hydroxy-27-(Z)-feruloyloxyurs-12-en-28-oic acid
0.0836
3beta-hydroxy-27-4-(E)-2'-dihydrocoumaroyloxyurs-12-en-28-oic acid
Homo sapiens
-
pH 7.0, 37°C
0.0008 - 0.0524
3beta-hydroxy-27-4-(E)-coumaroyloxyolea-12-en-28-oic acid
0.0009 - 0.0737
3beta-hydroxy-27-4-(E)-coumaroyloxyurs-12-en-28-oic acid
0.1213
3beta-hydroxy-27-4-(E)-coumaroyloxyurs-12-en-28-oic methyl ester
Homo sapiens
-
pH 7.0, 37°C
0.0017 - 0.059
3beta-hydroxy-27-4-(Z)-coumaroyloxyolea-12-en-28-oic acid
0.0014 - 0.0733
3beta-hydroxy-27-4-(Z)-coumaroyloxyurs-12-en-28-oic acid
0.0001 - 0.0246
adriamycin
0.029
amentoflavone
Homo sapiens
-
pH 7.0, 37°C
0.006 - 0.024
neomycin
0.4 - 4
spermine
additional information
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.5784
-
-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
-
hydrolysis of phosphatidylinositol 4,5-bisphosphate, in presence of sodium deoxycholate, enzyme from plasma membrane
6.7
assay at
6.8
-
hydrolysis of phosphatidylinositol 4,5-diphosphate
7 - 7.5
-
pH 7.0: about 30% of maximal activity, pH 7.5: about 75% of maximal activity, hydrolysis of phosphatidylinositol 4,5-diphosphate
7.3
-
hydrolysis of phosphatidylinositol 4,5-bisphosphate, in presence of sodium deoxycholate, enzyme from cytoplasm
7.4
-
platelet enzyme
7.8
-
assay at
8
-
Pi-PLC (membrane) solubilized with octyl glucoside
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.7 - 8
-
pH 5.7: about 70% of maximal activity, pH 8.0: about 50% of maximal activity
6 - 7
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.2
-
purified Pi-PLC (cytosol)
9 - 9.2
-
purified Pi-PLC (membrane)
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
highest expression level of PLCbeta1 in brain, especially in the amygdala, caudate nucleus and hippocampus
Manually annotated by BRENDA team
highest expression level of PLCbeta1 in brain, especially in the amygdala, caudate nucleus and hippocampus
Manually annotated by BRENDA team
-
isoenzyme PI-PLC-ß1
Manually annotated by BRENDA team
-
isoform PLCdelta4
Manually annotated by BRENDA team
-
W-138 fibroblasts, expression of PLC delta isoenzymes
Manually annotated by BRENDA team
-
TRPV6-expressing cell
Manually annotated by BRENDA team
PLC epsilon1b is enriched in
Manually annotated by BRENDA team
-
metastases
Manually annotated by BRENDA team
-
M1, M2 and unpolarized M0 macrophages
Manually annotated by BRENDA team
PLC-beta2 may be responsible, by modifying the phosphoinositide pools, for the changes of cytoskeleton architecture that take place during the acquisition of migration capability of differentiating promyelocytes
Manually annotated by BRENDA team
PLC epsilon1b is enriched in
Manually annotated by BRENDA team
only PLC epsilon1a, splice variant PLC epsilon1b can not be detected
Manually annotated by BRENDA team
-
isoform PI-PLCzeta
Manually annotated by BRENDA team
only PLC epsilon1a, splice variant PLC epsilon1b can not be detected
Manually annotated by BRENDA team
only PLC epsilon1a, splice variant PLC epsilon1b can not be detected
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
inner side, PLCbeta1
-
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PLCD1_HUMAN
756
0
85665
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
110000
-
gel filtration
115000
x * 115000, calculated from sequence
158500
-
gel filtration
18000
-
purified Pi-PLC (membrane) has a molecular weight of about 18000, SDS-PAGE or gel filtration
230000
-
x * 230000, x * 260000, two alternatively spliced PLC-epsilon forms
260000
-
x * 230000, x * 260000, two alternatively spliced PLC-epsilon forms
57000
-
purified Pi-PLC (cytosol), SDS-PAGE or gel filtration
additional information
-
PI-PLC, can be resolved into two peaks of activity of high M (60000-70000) and low M (16000-18000)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R257H
-
increased expression of mutant PLC delta1 in patients with coronary spastic angina
R564A/R672A
-
PLCgamma2 SH2 domain double mutant
T753F
PLCgamma2 mutant
T753F/T759F
T759F
PLCgamma2 mutant
Y1217F
phosphorylation site mutant
Y753F
phosphorylation site mutant
Y759F
phosphorylation site mutant
Y783F
-
PLC construct
additional information
-
constructs of PLCgamma2 containing either PLCdelta1 PH domain or the N-terminal tag of Lyn are targeted to the plasma membrane, recombinant wild-type PLCgamma2 not
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
both PI-PLC (membrane) and PI-PLC (cytosol) are fairly stable proteins when incubated for short periods of time (30 min) to a wide range of pH. PI-PLC (membrane) shows a fall of about 20-30% activity below pH 5.0 and is stable to alkaline pH up to 11
285237
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
confirmed by Coomassie blue staining after SDS-PAGE
-
enzyme from platelet membrane
-
preparation of nuclei, method development
recombinant PLCgamma2, expressed in Sf9 cells
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in COS-7 cells
expressed cDNA constructs encoding PLC-beta2 fragments of different lengths in COS-7 cell. Separate expression of amino- and C-terminal fragments of enzyme, requirements for reconstitution of enzyme activity and activation by Gbetagamma
expression in baculovirus-infected insect cells
-
expression in COS or HEK293 cells
expression in Escherichia coli
-
two distinct PLCbeta1 cDNAs, PLCbeta1a and b, generated through alternative splicing at their 3’ end, sequencing, overexpression in CHO and PC12 cells, gene structure, located on chromosome 20
wild-type and mutant PLCgamma2, expression in DT40 B-cells
-
wild-type and mutant PLCgamma2, expression in DT40 cells, A431 cells and in Sf9 cells
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
-
PLCgamma1 inhibitors may have potential therapeutic applications for the clinical treatment of tumor metastasis
medicine
pharmacology
-
showing that pharmacological inhibition of PLC enhances intestinal Ca2+ transport. This raises the possibility that pharmacological tools targeting PLC can be used to enhance intestinal Ca2+ absorption. Given the prevalence of osteoporosis, which generally comes with negative Ca2+ balance, PLC can be a clinically relevant pharmacological target in the future
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Banno, Y.; Nozawa, Y.
Characterization of partially purified phospholipase C from human platelet membranes
Biochem. J.
248
95-101
1987
Homo sapiens
Manually annotated by BRENDA team
Downes, C.P.; Michell, R.H.
The polyphosphoinositide phosphodiesterase of erythrocyte membranes
Biochem. J.
198
133-140
1981
Oryctolagus cuniculus, Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Maraldi, N.M.; Zini, N.; Santi, S.; Bavelloni, A.; Valmori, A.; Marmiroli, S.; Ognibene, A.
Phosphoinositidase C isozymes in SaOS-2 cells: immunocytochemical detection in nuclear and cytoplasmic compartments
Biol. Cell.
79
243-250
1993
Homo sapiens
Manually annotated by BRENDA team
Ginger, R.S.; Parker, P.J.
Expression, purification and characterisation of a functional phosphatidylinositol-specific phospholipase C-delta1 protein in Escherichia coli
Eur. J. Biochem.
210
155-160
1992
Homo sapiens
Manually annotated by BRENDA team
Carozzi, A.J.; Kriz, R.W.; Webster, C.; Parker, P.J.
Identification, purification and characterization of a novel phosphatidylinositol-specific phospholipase C, a third member of the beta subfamily
Eur. J. Biochem.
210
521-529
1992
Homo sapiens
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
Sies, W.; Lapetina, E.G.
Properties and distribution of phosphatidylinositol-specific phospholipase C in human and horse platelets
Biochim. Biophys. Acta
752
329-338
1983
Equus caballus, Homo sapiens
Manually annotated by BRENDA team
Mauco, G.; Chap, H.; Douste-Blazy, L.
Characterization and properties of a phosphatidylinositol phosphodiesterase (phospholipase C) from platelet cytosol
FEBS Lett.
100
367-370
1979
Homo sapiens
Manually annotated by BRENDA team
Roy, G.; Villar, L.M.; Lazaro, I.; Gonzalez, M.; Bootello, A.; Gonzalez-Porque, P.
Purification and properties of membrane and cytosolic phosphatidylinositol-specific phospholipase C from human spleen
J. Biol. Chem.
266
11495-11501
1991
Homo sapiens
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
Rodriguez, R.; Matsuda, M.; Storey, A.; Katan, M.
Requirements for distinct steps of phospholipase Cgamma2 regulation, membrane-raft-dependent targeting and subsequent enzyme activation in B-cell signalling
Biochem. J.
374
269-280
2003
Homo sapiens
Manually annotated by BRENDA team
Caricasole, A.; Sala, C.; Roncarati, R.; Formenti, E.; Terstappen, G.C.
Cloning and characterization of the human phosphoinositide-specific phospholipase C-beta 1 (PLCbeta1)
Biochim. Biophys. Acta
1517
63-72
2000
Homo sapiens (Q9NQ66), Homo sapiens
Manually annotated by BRENDA team
Rossi, M.A.; Dianzani, M.U.
Action of 2-nonenal and 4-hydroxynonenal on phosphoinositide-specific phospholipase C in undifferentiated and DMSO-differentiated HL-60 cells
Cell Biochem. Funct.
18
209-214
2000
Homo sapiens
Manually annotated by BRENDA team
Zhang, W.; Neer, E.J.
Reassembly of phospholipase C-b2 from separated domains: analysis of basal and G protein-stimulated activities
J. Biol. Chem.
276
2503-2508
2001
Homo sapiens (Q00722)
Manually annotated by BRENDA team
Rodriguez, R.; Matsuda, M.; Perisic, O.; Bravo, J.; Paul, A.; Jones, N.P.; Light, Y.; Swann, K.; Williams, R.L.; Katan, M.
Tyrosine residues in phospholipase Cgamma2 essential for the enzyme function in B-cell signaling
J. Biol. Chem.
276
47982-47992
2001
Homo sapiens (P16885), Homo sapiens
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, Saccharomyces cerevisiae, Dictyostelium discoideum, Drosophila sp. (in: flies), Homo sapiens, Mus musculus, Rattus norvegicus, Saccharomyces cerevisiae PLC1p
Manually annotated by BRENDA team
Hwang, J.I.; Oh, Y.S.; Shin, K.J.; Kim, H.; Ryu, S.H.; Suh, P.G.
Molecular cloning and characterization of a novel phospholipase C, PLC-eta
Biochem. J.
389
181-186
2005
Mus musculus (Q4KWH5), Mus musculus, Homo sapiens (Q4KWH8), Homo sapiens
Manually annotated by BRENDA team
Lukinovic-Skudar, V.; Donlagic, L.; Banfic, H.; Visnjic, D.
Nuclear phospholipase C-beta1b activation during G2/M and late G1 phase in nocodazole-synchronized HL-60 cells
Biochim. Biophys. Acta
1733
148-156
2005
Homo sapiens
Manually annotated by BRENDA team
vom Dorp, F.; Sari, A.Y.; Sanders, H.; Keiper, M.; Oude Weernink, P.A.; Jakobs, K.H.; Schmidt, M.
Inhibition of phospholipase C-epsilon by Gi-coupled receptors
Cell. Signal.
16
921-928
2004
Homo sapiens
Manually annotated by BRENDA team
Peng, H.H.; Hodgson, L.; Henderson, A.J.; Dong, C.
Involvement of phospholipase C signaling in melanoma cell-induced endothelial junction disassembly
Front. Biosci.
10
1597-1606
2005
Homo sapiens
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
Stewart, A.J.; Mukherjee, J.; Roberts, S.J.; Lester, D.; Farquharson, C.
Identification of a novel class of mammalian phosphoinositol-specific phospholipase C enzymes
Int. J. Mol. Med.
15
117-121
2005
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Piechulek, T.; Rehlen, T.; Walliser, C.; Vatter, P.; Moepps, B.; Gierschik, P.
Isozyme-specific stimulation of phospholipase C-gamma2 by Rac GTPases
J. Biol. Chem.
280
38923-38931
2005
Homo sapiens
Manually annotated by BRENDA team
Hou, C.; Kirchner, T.; Singer, M.; Matheis, M.; Argentieri, D.; Cavender, D.
In vivo activity of a phospholipase C inhibitor, 1-(6-((17beta-3-methoxyestra-1,3,5(10)-trien-17-yl)amino)hexyl)-1H-pyrrole-2,5-dione (U73122), in acute and chronic inflammatory reactions
J. Pharmacol. Exp. Ther.
309
697-704
2004
Homo sapiens
Manually annotated by BRENDA team
Kim, Y.J.; Sekiya, F.; Poulin, B.; Bae, Y.S.; Rhee, S.G.
Mechanism of B-cell receptor-induced phosphorylation and activation of phospholipase C-gamma2
Mol. Cell. Biol.
24
9986-9999
2004
Homo sapiens, Homo sapiens (P16885), Mus musculus, Mus musculus (Q8CIH5)
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
Sorli, S.C.; Bunney, T.D.; Sugden, P.H.; Paterson, H.F.; Katan, M.
Signaling properties and expression in normal and tumor tissues of two phospholipase C epsilon splice variants
Oncogene
24
90-100
2005
Homo sapiens, Homo sapiens (Q9P212)
Manually annotated by BRENDA team
Diaz Anel, A.M.
Phospholipase C beta3 is a key component in the Gbetagamma/PKCeta/PKD-mediated regulation of trans-Golgi network to plasma membrane transport
Biochem. J.
406
157-165
2007
Homo sapiens (Q01970)
Manually annotated by BRENDA team
Lukinovic-Skudar, V.; Matkovic, K.; Banfic, H.; Visnjic, D.
Two waves of the nuclear phospholipase C activity in serum-stimulated HL-60 cells during G(1) phase of the cell cycle
Biochim. Biophys. Acta
1771
514-521
2007
Homo sapiens
Manually annotated by BRENDA team
Bertagnolo, V.; Benedusi, M.; Brugnoli, F.; Lanuti, P.; Marchisio, M.; Querzoli, P.; Capitani, S.
Phospholipase C-beta 2 promotes mitosis and migration of human breast cancer-derived cells
Carcinogenesis
28
1638-1645
2007
Homo sapiens (Q00722), Homo sapiens
Manually annotated by BRENDA team
Brugnoli, F.; Bavelloni, A.; Benedusi, M.; Capitani, S.; Bertagnolo, V.
PLC-beta2 activity on actin-associated polyphosphoinositides promotes migration of differentiating tumoral myeloid precursors
Cell. Signal.
19
1701-1712
2007
Homo sapiens (Q00722)
Manually annotated by BRENDA team
Liu, X.; Zhao, Q.; Araki, S.; Zhang, S.; Miao, J.
Contrasting effects of phosphatidylinositol- and phosphatidylcholine-specific phospholipase C on apoptosis in cultured endothelial cells
Endothelium
13
205-211
2006
Homo sapiens
Manually annotated by BRENDA team
Faenza, I.; Bregoli, L.; Ramazzotti, G.; Gaboardi, G.; Follo, M.Y.; Mongiorgi, S.; Billi, A.M.; Manzoli, L.; Martelli, A.M.; Cocco, L.
Nuclear phospholipase C beta1 and cellular differentiation
Front. Biosci.
13
2452-2463
2008
Homo sapiens (Q01970), Homo sapiens (Q9NQ66), Mus musculus (Q9Z1B3)
Manually annotated by BRENDA team
Alvarez-Breckenridge, C.A.; Waite, K.A.; Eng, C.
PTEN regulates phospholipase D and phospholipase C
Hum. Mol. Genet.
16
1157-1163
2007
Homo sapiens
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
Ho, K.K.; Mann, D.J.
Nuclear signaling through phospholipase C and phosphatidylinositol 4,5-bisphosphate
Signal Transduction
6
92-100
2006
Homo sapiens, Mus musculus (Q8R3B1), Mus musculus (Q9Z1B3)
-
Manually annotated by BRENDA team
Kim, K.Y.; Bang, S.; Han, S.; Nguyen, Y.H.; Kang, T.M.; Kang, K.W.; Hwang, S.W.
TRP-independent inhibition of the phospholipase C pathway by natural sensory ligands
Biochem. Biophys. Res. Commun.
370
295-300
2008
Homo sapiens
Manually annotated by BRENDA team
Sala, G.; Dituri, F.; Raimondi, C.; Previdi, S.; Maffucci, T.; Mazzoletti, M.; Rossi, C.; Iezzi, M.; Lattanzio, R.; Piantelli, M.; Iacobelli, S.; Broggini, M.; Falasca, M.
Phospholipase Cgamma1 is required for metastasis development and progression
Cancer Res.
68
10187-10196
2008
Homo sapiens
Manually annotated by BRENDA team
Ochocka, A.M.; Grden, M.; Sakowicz-Burkiewicz, M.; Szutowicz, A.; Pawelczyk, T.
Regulation of phospholipase C-delta1 by ARGHAP6, a GTPase-activating protein for RhoA: possible role for enhanced activity of phospholipase C in hypertension
Int. J. Biochem. Cell Biol.
40
2264-2273
2008
Homo sapiens (P51178), Homo sapiens
Manually annotated by BRENDA team
Loreto, C.; Carnazza, M.L.; Cardile, V.; Libra, M.; Lombardo, L.; Malaponte, G.; Martinez, G.; Musumeci, G.; Papa, V.; Cocco, L.
Mineral fiber-mediated activation of phosphoinositide-specific phospholipase c in human bronchoalveolar carcinoma-derived alveolar epithelial A549 cells
Int. J. Oncol.
34
371-376
2009
Homo sapiens
Manually annotated by BRENDA team
Harita, Y.; Kurihara, H.; Kosako, H.; Tezuka, T.; Sekine, T.; Igarashi, T.; Ohsawa, I.; Ohta, S.; Hattori, S.
Phosphorylation of nephrin triggers Ca2+ signaling by recruitment and activation of phospholipase C-[gamma]1
J. Biol. Chem.
284
8951-8962
2009
Homo sapiens (P19174)
Manually annotated by BRENDA team
Hao, J.J.; Liu, Y.; Kruhlak, M.; Debell, K.E.; Rellahan, B.L.; Shaw, S.
Phospholipase C-mediated hydrolysis of PIP2 releases ERM proteins from lymphocyte membrane
J. Cell Biol.
184
451-462
2009
Homo sapiens
Manually annotated by BRENDA team
Follo, M.Y.; Finelli, C.; Clissa, C.; Mongiorgi, S.; Bosi, C.; Martinelli, G.; Baccarani, M.; Manzoli, L.; Martelli, A.M.; Cocco, L.
Phosphoinositide-phospholipase C beta1 mono-allelic deletion is associated with myelodysplastic syndromes evolution into acute myeloid leukemia
J. Clin. Oncol.
27
782-790
2009
Homo sapiens (P19174), Homo sapiens (Q15147), Homo sapiens (Q9NQ66), Homo sapiens
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
Thyagarajan, B.; Benn, B.S.; Christakos, S.; Rohacs, T.
Phospholipase C-mediated regulation of transient receptor potential vanilloid 6 channels: implications in active intestinal Ca2+ transport
Mol. Pharmacol.
75
608-616
2009
Homo sapiens
Manually annotated by BRENDA team
Lee, J.S.; Yoo, H.; Suh, Y.G.; Jung, J.K.; Kim, J.
Structure-activity relationship of pentacylic triterpene esters from Uncaria rhynchophylla as inhibitors of phospholipase Cgamma1
Planta Med.
74
1481-1487
2008
Homo sapiens, Mus musculus
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
Rattus norvegicus (P10687), Homo sapiens (Q9NQ66), Homo sapiens, Mus musculus (Q9Z1B3)
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
van Veen, M.; Mans, L.A.; Matas-Rico, E.; van Pelt, J.; Perrakis, A.; Moolenaar, W.H.; Haramis, A.G.
Glycerophosphodiesterase GDE2/GDPD5 affects pancreas differentiation in zebrafish
Int. J. Biochem. Cell Biol.
94
71-78
2018
Danio rerio (E9QG52), Danio rerio (X1WHY1), Homo sapiens (Q8WTR4)
Manually annotated by BRENDA team
Smrcka, A.V.
Regulation of phosphatidylinositol-specific phospholipase C at the nuclear envelope in cardiac myocytes
J. Cardiovasc. Pharmacol.
65
203-210
2015
Homo sapiens
Manually annotated by BRENDA team
Di Raimo, T.; Leopizzi, M.; Mangino, G.; Rocca, C.D.; Businaro, R.; Longo, L.; Lo Vasco, V.R.
Different expression and subcellular localization of phosphoinositide-specific phospholipase C enzymes in differently polarized macrophages
J. Cell Commun. Signal.
10
283-293
2016
Homo sapiens
Manually annotated by BRENDA team
Fais, P.; Leopizzi, M.; Di Maio, V.; Longo, L.; Della Rocca, C.; Tagliaro, F.; Bortolotti, F.; Lo Vasco, V.R.
Phosphoinositide-specific phospholipase C in normal human liver and in alcohol abuse
J. Cell. Biochem.
120
7907-7917
2018
Homo sapiens
Manually annotated by BRENDA team
Cocco, L.; Follo, M.Y.; Manzoli, L.; Suh, P.G.
Phosphoinositide-specific phospholipase C in health and disease
J. Lipid Res.
56
1853-1860
2015
Homo sapiens
Manually annotated by BRENDA team
Seo, J.B.; Jung, S.R.; Huang, W.; Zhang, Q.; Koh, D.S.
Charge shielding of PIP2 by cations regulates enzyme activity of phospholipase C
PLoS ONE
10
e0144432
2015
Homo sapiens
Manually annotated by BRENDA team