Phospholipases of Mineralization Competent Cells and Matrix Vesicles: Roles in Physiological and Pathological Mineralizations
Abstract
:Contents
- 1. Introduction 5040
- 1.1. Bone Biology and Physiological Mineralization 5040
- 1.2. Ectopic Calcifications and Defective Mineralizations 5042
- 1.3. Matrix Vesicles and Early Stages of Mineralization 5043
- 1.4. Dietary Lipids and Bone Health 5044
- 1.5. Groups of Phospholipases and Possible Roles during Mineralization 5044
- 2. Phospholipases A1 5047
- 2.1. Groups, Subgroups and Specificity 5047
- 3. Phospholipases A2 5048
- 3.1. Groups, Subgroups and Specificity 5048
- 3.2. Presence of PLA2s in Chondrocytes and Possible Roles 5049
- 3.3 Presence of PLA2s in Osteoblasts and Possible Roles 5050
- 3.4. Presence of PLA2s in osteoclasts and Possible Roles 5051
- 3.5. Presence of PLA2s in Smooth Muscle Cells and Possible Roles 5052
- 3.6. The Expressions of PLA2s under Pathological Conditions 5052
- 3.7. Transgenic Knockout Animal for PLA2 Enzymes as Models for Bone Formation and Mineralization Diseases 5053
- 3.8. Inhibitors of PLA2 as Drug Therapy 5053
- 3.9. Effects Mediated by Arachidonic Acid and Its Pathways at Cellular Level 5054
- 3.9.1. Effects Mediated by PGE2 5055
- 3.9.2. Effects Mediated by PGF2α and PGD2 5056
- 3.10. Effects Mediated by Lysophospholipids and Their Pathways at Cellular Level 5057
- 3.11. The Effects of PLA Metabolites at Matrix Vesicle Level 5060
- 4. Non-Specific Phospholipase C 5060
- 4.1. Groups, Subgroups and Specificity 5060
- 4.2. Presence of PC-PLC in Chondrocytes and in Osteoblasts and Its Possible Role 5061
- 4.3. Presence of PC-PLC in Osteoclasts and Possible Roles 5061
- 4.4. Presence of PC-PLC in Smooth Muscle Cells and Possible Roles 5061
- 4.5. The Effect of PLC Metabolites in Matrix Vesicles 5061
- 5. PI-Specific Phospholipase C 5062
- 5.1. Groups, Subgroups and Specificity 5062
- 5.2. PI-PLC in Tissues 5063
- 5.3. Presence of PI-PLC in Chondrocytes and Possible Roles. 5064
- 5.4. Presence of PI-PLC in Osteoblasts 5065
- 5.4.1. Endothelin-1 Induced Signaling Pathway 5065
- 5.4.2. Basic FGF Induced Signaling Pathway 5066
- 5.4.3. Platelet-Derived Growth Factor Induced Signaling Pathway 5066
- 5.4.4. Parathyroid Hormone Induced Signaling Pathway 5066
- 5.4.5. PGD2 Induced-Signaling Pathway 5066
- 5.4.6. PGE2 Induced-Signaling Pathway 5067
- 5.4.7. PGF2 Induced-Signaling Pathway 5067
- 5.4.8. Vitamin D-Induced Signaling Pathway 5067
- 5.4.9. Interleukin-1-Induced Signaling Pathway 5067
- 5.4.10. Miscelanous Ligand Binding Stimulated PI-PLC in Osteoblasts 5068
- 5.4.11. Purinergic and Serotonin-2 B Receptors 5068
- 5.5. Presence of PI-PLC in Osteoclasts 5068
- 5.5.1. Calcitonin Induced Signaling Pathway 5069
- 5.5.2. Intracellular Ca2+ Induced Signaling Pathway 5069
- 5.5.3. Osteoprotegrin Induced Signaling Pathway 5070
- 5.5.4. RANK Induced Signaling Pathways 5071
- 5.5.5. Parathyroid Hormone Induced Signaling Pathway 5071
- 5.6. Presence of PI-PLC in Smooth Muscle Cells and Possible Roles 5072
- 5.7. Presence of PI-PLC in Odontoblasts and Possible Roles 5072
- 5.8. Genetic Models 5073
- 6. PLC-Related but Catalytically Inactive Protein 5073
- 7. Sphingomyelinase 5074
- 7.1. Groups, Subgroups and Specificity 5074
- 7.2. Presence of Sphingomyelinase in Chondrocytes and Possible Roles 5074
- 7.3. Presence of Sphingomyelinase in Osteoblasts and Possible Roles 5074
- 7.4. Presence of Sphyngomyelinase in Osteoclasts and Possible Roles 5075
- 7.5. Genetic Models 5075
- 7.6. Effects of Sphyngomyelinase Metabolites at Matrix Vesicle Level 5075
- 8. Phospholipase D 5076
- 8.1. Groups, Subgroups and Specificity 5076
- 8.2. Presence of PLD in Chondrocytes and Possible Roles 5077
- 8.3. Presence of PLD in Osteoblasts and Possible Roles 5079
- 8.4. Presence of PLD in Osteoclasts and Possible Roles 5080
- 8.5. Genetic Models 5080
- 8.6. Effects of PLD Metabolite at Matrix Vesicle Level 5080
- 9. Non-HKD Enzymes—GPI-PLD 5081
- 9.1. Groups, Subgroups and Specificity 5081
- 9.2. Presence of GPI-PLD in Chondrocytes and Possible Roles 5081
- 9.3. Presence of GPI-PLD in Osteoblasts and Possible Roles 5082
- 10. Non-HKD Enzymes—Autotaxin 5082
- 10.1. Groups, Subgroups and Specificity 5082
- 10.2. Presence of ATX in Chondrocytes and Possible Roles. 5083
- 10.3. Presence of ATX in Osteoblasts and Possible Roles 5083
- 10.4. Presence of ATX in Osteoclasts and Possible Roles. 5084
- 10.5. Presence of ATX in Smooth Muscle Cells and Possible Roles 5084
- 11. Concluding Remarks 5084
- Acknowledgments 5084
- References 5084
Abbreviations
1α,25-(OH)2D3 | 1α,25-dihydroxyvitamin D3 |
24R,25(OH)2D3 | 24R,25-dihydroxyvitamin D3 |
AA | arachidonic acid |
ATX | autotaxin |
BM | bone marrow |
Ca2+e | extracellular Ca2+ |
Ca2+i | intracellular Ca2+ |
CaR | calcium-sensing receptor |
CIA | collagen-induced arthritis |
cPLA2 | cytosolic Ca2+-dependent PLA2 |
COX | cyclooxygenase |
DAG | diacylglycerol |
DHT | 5α-dihydrotestosterone |
ECM | extracellular matrix |
ERK | extracellular signal-regulated kinase |
ET | endothelin |
FGF | fibroblast growth factor |
GPCR | G-protein-coupled receptor |
GPI-PLD | glycosyl-PI specific PLD |
HA | hydroxyapatite |
IL | interleukin |
IP3 | inositol 1,4,5-trisphosphate |
iPLA2 | Ca2+-independent PLA2 |
LOX | lipooxygenase |
LPA | lysophosphatidic acid |
LPC | lysophosphatidylcholine |
LPE | lysophosphatidylethanolamine |
LPG | lysophosphatidylglycerol |
LPI | lysophosphatidylinositol |
LPL | lysophospholipid |
LPS | lysophosphatidylserine |
LRRc17 | leucine-rich repeat-containing 17 |
MAP | mitogen activated protein |
MPP | metalloproteinase |
MV | matrix vesicle |
NF-κB | nuclear factor κB |
NFAT | nuclear factor of activated T cell |
NPP | ectonucleotide pyrophosphatase phosphodiesterase |
NSAID | non-steroidal anti-inflammatory drug |
OA | osteoarthritis |
OPG | osteoprotegerin |
PA | phosphatidic acid |
PAF | platelet-activating factor |
PAF-AH | PAF-acetylhydrolase |
PBMC | peripheral blood mononuclear cell |
PC | phosphatidylcholine |
PChol | phosphocholine |
PE | phosphatidylethanolamine |
PEA | phosphoethanolamine |
PGD2 | prostaglandin D2 |
PGE1 | prostaglandin E1 |
PGE2 | prostaglandin E2 |
PGF2 | prostaglandin F2 |
PH | pleckstrin homology |
PHOSPHO1 | phosphatase orphan 1 |
PI | phosphatidylinositol |
PI-PLC | PI-specific |
PIP2 | PI 4,5-bisphosphate |
PIP3 | PI 3,4,5-trisphosphate |
PKC | protein kinase C |
PLA1 | phospholipase A1 |
PLA2 | phospholipase A2 |
PLC | phospholipase C |
PLD | phospholipase D |
Pi | inorganic phosphate |
PPi | inorganic pyrophosphate |
PRIP | PLC-related but catalytically inactive protein |
PS | phosphatidylserine |
PS-PLA1 | PS-specific PLA1 |
PTH | parathyroid hormone |
PTX | pertussis toxin |
PUFA | polyunsaturated fatty acid |
RA | rheumatoid arthritis |
RANKL | receptor activator of nuclear factor κB ligand |
Runx2 | runt-related transcription factor 2 |
SH | src homology |
SM | sphingomyelin |
SMase | sphingomyelinase |
SMPD3 | sphingomyeline phosphodiesterase-3 |
sPLA2 | secreted PLA2 |
S1P | sphingosine-1-phosphate |
STAT | signal transducer and activator of transcription |
TNAP | tissue-non specific alkaline phosphatase |
TNF | tumor necrosis factor |
VSMC | vascular smooth muscle cell |
1. Introduction
1.1. Bone Biology and Physiological Mineralization
1.2. Ectopic Calcifications and Defective Mineralizations
1.3. Matrix Vesicles and Early Stages of Mineralization
1.4. Dietary Lipids and Bone Health
1.5. Groups of Phospholipases and Possible Roles during Mineralization
2. Phospholipases A1
2.1. Groups, Subgroups and Specificity
3. Phospholipases A2
3.1. Groups, Subgroups and Specificity
3.2. Presence of PLA2s in Chondrocytes and Possible Roles
3.3 Presence of PLA2s in Osteoblasts and Possible Roles
3.4. Presence of PLA2s in osteoclasts and Possible Roles
3.5. Presence of PLA2s in Smooth Muscle Cells and Possible Roles
3.6. The Expressions of PLA2s under Pathological Conditions
3.7. Transgenic Knockout Animal for PLA2 Enzymes as Models for Bone Formation and Mineralization Diseases
3.8. Inhibitors of PLA2 as Drug Therapy
3.9. Effects Mediated by Arachidonic Acid and Its Pathways at Cellular Level
3.9.1. Effects Mediated by PGE2
3.9.2. Effects Mediated by PGF2α and PGD2
3.10. Effects Mediated by Lysophospholipids and Their Pathways at Cellular Level
3.11. The Effects of PLA Metabolites at Matrix Vesicle Level
4. Non-Specific Phospholipase C
4.1. Groups, Subgroups and Specificity
4.2. Presence of PC-PLC in Chondrocytes and in Osteoblasts and Its Possible Role
4.3. Presence of PC-PLC in Osteoclasts and Possible Roles
4.4. Presence of PC-PLC in Smooth Muscle Cells and Possible Roles
4.5. The Effect of PLC Metabolites in Matrix Vesicles
5. PI-Specific Phospholipase C
5.1. Groups, Subgroups and Specificity
5.2. PI-PLC in Tissues
5.3. Presence of PI-PLC in Chondrocytes and Possible Roles
5.4. Presence of PI-PLC in Osteoblasts
5.4.1. Endothelin-1 Induced Signaling Pathway
5.4.2. Basic FGF Induced Signaling Pathway
5.4.3. Platelet-Derived Growth Factor Induced Signaling Pathway
5.4.4. Parathyroid Hormone Induced Signaling Pathway
5.4.5. PGD2 Induced-Signaling Pathway
5.4.6. PGE2 Induced-Signaling Pathway
5.4.7. PGF2 Induced-Signaling Pathway
5.4.8. Vitamin D-Induced Signaling Pathway
5.4.9. Interleukin-1-Induced Signaling Pathway
5.4.10. Miscelanous Ligand Binding Stimulated PI-PLC in Osteoblasts
5.4.11. Purinergic and Serotonin-2 B Receptors
5.5. Presence of PI-PLC in Osteoclasts
5.5.1. Calcitonin Induced Signaling Pathway
5.5.2. Intracellular Ca2+ Induced Signaling Pathway
5.5.3. Osteoprotegrin Induced Signaling Pathway
5.5.4. RANK Induced Signaling Pathways
5.5.5. Parathyroid Hormone Induced Signaling Pathway
5.6. Presence of PI-PLC in Smooth Muscle Cells and Possible Roles
5.7. Presence of PI-PLC in Odontoblasts and Possible Roles
5.8. Genetic Models
6. PLC-Related but Catalytically Inactive Protein
7. Sphingomyelinase
7.1. Groups, Subgroups and Specificity
7.2. Presence of Sphingomyelinase in Chondrocytes and Possible Roles
7.3. Presence of Sphingomyelinase in Osteoblasts and Possible Roles
7.4. Presence of Sphyngomyelinase in Osteoclasts and Possible Roles
7.5. Genetic Models
7.6. Effects of Sphyngomyelinase Metabolites at Matrix Vesicle Level
8. Phospholipase D
8.1. Groups, Subgroups and Specificity
8.2. Presence of PLD in Chondrocytes and Possible Roles
8.3. Presence of PLD in Osteoblasts and Possible Roles
8.4. Presence of PLD in Osteoclasts and Possible Roles
8.5. Genetic Models
8.6. Effects of PLD Metabolite at Matrix Vesicle Level
9. Non-HKD Enzymes—GPI-PLD
9.1. Groups, Subgroups and Specificity
9.2. Presence of GPI-PLD in Chondrocytes and Possible Roles
9.3. Presence of GPI-PLD in Osteoblasts and Possible Roles
10. Non-HKD Enzymes—Autotaxin
10.1. Groups, Subgroups and Specificity
10.2. Presence of ATX in Chondrocytes and Possible Roles
10.3. Presence of ATX in Osteoblasts and Possible Roles
10.4. Presence of ATX in Osteoclasts and Possible Roles
10.5. Presence of ATX in Smooth Muscle Cells and Possible Roles
11. Concluding Remarks
Acknowledgments
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% of Total lipid | |||||
---|---|---|---|---|---|
Chondrocytes | |||||
Lipid | Whole cartilage | Proliferating | Hypertrophic | Cell membranes | MVs |
SM | 8.6 ± 0.7 | 5.8 ± 0.4 | 8.0 ± 0.8 | 8.1 ± 0.8 | 13.4 ± 1.8 |
PC | 45.2 ± 1.9 | 47.6 ± 1.5 | 38.0 ± 1.5 | 53.2 ± 2.2 | 41.8 ± 2.5 |
LPC | 2.0 ± 0.6 | 1.9 ± 0.4 | 1.8 ± 0.4 | 3.5 ± 0.8 | 3.4 ± 0.8 |
PE | 17.6 ± 1.0 | 16.9 ± 0.7 | 14.7 ± 0.8 | 14.6 ± 1.8 | 14.9 ± 1.8 |
LPE | 2.0 ± 0.4 | 3.3 ± 0.7 | 2.4 ± 0.4 | 4.9 ± 1.2 | 6.5 ± 1.2 |
PS | 5.1 ± 0.8 | 3.3 ± 0.3 | 5.0 ± 1.0 | 5.4 ± 0.7 | 9.3 ± 1.1 |
LPS | 0.5 ± 0.2 | 0.2 ± 0.1 | 0.3 ± 0.2 | 2.2 ± 0.7 | 2.4 ± 0.8 |
PI | 7.2 ± 0.8 | 6.2 ± 0.8 | 6.4 ± 0.8 | 6.1 ± 0.8 | 6.6 ± 0.6 |
LPI | 1.1 ± 0.7 | 1.0 ± 0.6 | 0.5 ± 0.4 | 0.3 ± 0.2 | 1.1 ± 0.3 |
PA | 2.0 ± 0.5 | 0.8 ± 0.3 | 1.6 ± 0.5 | 1.1 ± 0.2 | 0.9 ± 0.3 |
PG | 1.2 ± 0.6 | 0.7 ± 0.3 | 1.2 ± 0.6 | 0.9 ± 0.2 | 1.3 ± 0.3 |
di-PG | 3.0 ± 0.6 | 2.5 ± 0.4 | 2.9 ± 0.6 | 1.7 ± 0.3 | 1.5 ± 1.4 |
Types of PLA1 | Groups | Origin |
---|---|---|
Extracellular PLA1 | PS-PLA1 | Human |
mPLA1α | Human | |
mPLA1β | Human | |
Hepatic lipase | Human | |
Endothelial lipase | Human | |
Pancreatic lipase-related protein 2 | Human | |
Intracellular PLA1 | iPLA1α | Human |
iPLA1β | Human | |
iPLA1γ | Human |
Type | Group | Subgroup | Origin or commun source |
---|---|---|---|
sPLA2 | I | A | Cobras and kraits |
I | B | Human/porcine pancreas | |
II | A | Rattlesnake/human synovial | |
II | B | Gaboon viper | |
II | C | Rat/murine testis | |
II | D | Human/murine pancreas/spleen | |
II | E | Human/murine brain/heart/uterus | |
II | F | Human/murine testis/embryo | |
III | Lizard/bee | ||
V | Human/murine heart/lung/macrophage | ||
IX | Snail venom | ||
X | Human spleen/thymus/leucocyte | ||
XI | A | Green rice shoots (PLA2-I) | |
XI | B | Green rice shoots (PLA2-II) | |
XII | A | Human/murine | |
XII | B | Human/murine | |
XIII | Parvovirus | ||
XIV | Symbiotic fungus/bacteria | ||
cPLA2 | IV | A(α) | Human macrophage-like U937 cells/Platelets/Raw 264.7/rat kidney, ubiquitous |
IV | B(β) | Human pancreas/liver/heart/brain/ubiquitous | |
IV | C(γ) | Human heart/skeletal muscle | |
IV | D(δ) | Murine placenta | |
IV | E(ɛ) | Murine heart/skeletal muscle/testis/thyroid | |
IV | F(η) | Murine thyroid/stomach | |
iPLA2 | VI | A(β) | Human/murine |
VI | B(γ) | Human/murine | |
VI | C(δ) | Human/murine | |
VI | D(ɛ) | Human | |
VI | E(ζ) | Human | |
VI | F(η) | Human | |
PAF-AH | VII | A(lipoprotein-associated-PLA2) | Human, murine, porcine, bovine |
VII | B(PAF-AH II) | Human, bovine | |
VIII | A(α1) | Human | |
VIII | B(α2) | Human | |
Lysosomal PLA2 | XV | Human, murine, bovine | |
Adipose PLA | XVI | Human,mouse |
Types of PLA2 | Expression levels | Diseases | References |
---|---|---|---|
sPLA2-IIA | Highly expressed in synovial fluid | RA | [123,126,165,166,169] |
sPLA2-IIA | Highly expressed in chondrocytes | RA | [126] |
sPLA2-IID | Overexpressed in synovial fluid | RA | [124] |
sPLA2-IIE | Overexpressed in synovial fluid | RA | [124] |
sPLA2-V | Overexpressed in synovial fluid | RA | [124] |
sPLA2-X | More or less expressed in synovial fluid | Active and inactive RA | [124] |
sPLA2-IIA | Overexpressed in synovial fluid | OA | [126,167,168] |
sPLA2-IIA | Overexpressed in VSMC | Infarctus heart | [164] |
sPLA2-V | Overexpressed in VSMC | Infarctus Heart | [164] |
cPLA2-α | cPLA2-α−/− mice loss in function | Prevention in collagen-induced arthritis | [174] |
iPLA2β | iPLA2-β−/− mice loss in function | Low bone mass | [121] |
Enzymes or products or animal models | Expression level or concentration | Physiological effects | Pathological effects | References |
---|---|---|---|---|
COX-2 | Increase in synovial fluid | RA | [38] | |
mPGES-1 | Increase in synovial fluid | RA | [38] | |
Mice deficient in COX2 | Null-COX | CIA reduction | [215] | |
Mice deficient in mPGES-1 | Null-PGES-1 | CIA reduction | [217] | |
PGE2 | High level in synovial fluid | RA | [239,240] | |
Prostaglandin | Stimulate bone formation | [233] | ||
Prostaglandin | Activate bone resorption in osteoporosis, RA, OA or in periodontis | [238] | ||
PGD2 | Stimulate osteoblast calcification | [249] | ||
PGF2α | Promote osteogenic differentiation | [251] | ||
15-Deoxy-Δ12,14- prostaglandin J2 | Prostaglandin D2 metabolite | Activates PPARγ and TNAP expression | [249] | |
n-3 PUFA or conjugated linoleic acid | Exogenous addition | Beneficial effects due to modulation of COX-2 | [59] |
Cox inhibitors | Physiological effects | Pathological effects | References |
---|---|---|---|
NSAIDS Ibuprofen Indomethacin | Inhibit fracture healing | [221–223] | |
Indomethacin | Decrease TNAP activity | [222] | |
NSAIDS | Decrease heterotopic calcification | [224–226] | |
Keterolac | Decrease in spinal fusion | [228] | |
COX-2 inhibitor | Decrease pain in RA | [231,241] |
Type | Group | Origin |
---|---|---|
Non-specific PLC | Mammalian | |
PI-specific | PLC-β PLCB1, PLCB2, PLCB3, PLCB4 | Mammalian |
PI-specific | PLC-γ PLCG1, PLCG2 | Mammalian |
PI-specific | PLC-δ PLCD1, PLCD3, PLCD4 | Mammalian |
PI-specific | PLC-ɛ PLCE1 | Mammalian |
PI-specific | PLC-η PLCH1, PLCH2 | Mammalian |
PI-specific | PLC-ζ PLCZ1 | Mammalian |
Phospholipase C-like | PLCL1, PLCL2 | Mammalian |
Zinc-dependent prokaryotic PLC | Bacterial | |
PI-DAG-lyase | Trypanosome | |
SMase | Neutral SMase1 | Mammalian |
Neutral SMase2 (SMPD3) | Mammalian | |
Neutral SMase3 | Mammalian | |
Lysosmal acid SMase | Mammalian | |
Secreted zinc-dependent acid SMase | Mammalian | |
Alkaline SMase | Mammalian |
Type | Variants | Origin |
---|---|---|
PLDs with HKD motif | ||
PLD1 | PLD1a, PLD1b, PLD1c, PLD1d | Mammalian |
PLD2 | PLD2a, PLD2b, PLD2c | Mammalian |
PLD3 | Mammalian | |
Endonuclease-like mitochondrial PLD | Mammalian | |
Non-HKD PLDs | ||
GPI-PLD | Mammalian | |
N-acyl PE-PLD | Mammalian | |
cytochrome P450 1A2 | Mammalian | |
cytochtome P450 2E1 | Mammalian | |
ATX | Mammalian |
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Mebarek, S.; Abousalham, A.; Magne, D.; Do, L.D.; Bandorowicz-Pikula, J.; Pikula, S.; Buchet, R. Phospholipases of Mineralization Competent Cells and Matrix Vesicles: Roles in Physiological and Pathological Mineralizations. Int. J. Mol. Sci. 2013, 14, 5036-5129. https://doi.org/10.3390/ijms14035036
Mebarek S, Abousalham A, Magne D, Do LD, Bandorowicz-Pikula J, Pikula S, Buchet R. Phospholipases of Mineralization Competent Cells and Matrix Vesicles: Roles in Physiological and Pathological Mineralizations. International Journal of Molecular Sciences. 2013; 14(3):5036-5129. https://doi.org/10.3390/ijms14035036
Chicago/Turabian StyleMebarek, Saida, Abdelkarim Abousalham, David Magne, Le Duy Do, Joanna Bandorowicz-Pikula, Slawomir Pikula, and René Buchet. 2013. "Phospholipases of Mineralization Competent Cells and Matrix Vesicles: Roles in Physiological and Pathological Mineralizations" International Journal of Molecular Sciences 14, no. 3: 5036-5129. https://doi.org/10.3390/ijms14035036