Functional Role of Phospholipase D in Bone Metabolism
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Phospholipase D (PLD) proteins are major enzymes that regulate various cellular functions, such as cell growth, cell migration, membrane trafficking, and cytoskeletal dynamics. As they are responsible for such important biological functions, PLD proteins have been considered promising therapeutic targets for various diseases, including cancer and vascular and neurological diseases. Intriguingly, emerging evidence indicates that PLD1 and PLD2, 2 major mammalian PLD isoenzymes, are the key regulators of bone remodeling; this suggests that these isozymes could be used as potential therapeutic targets for bone diseases, such as osteoporosis and rheumatoid arthritis. PLD1 or PLD2 deficiency in mice can lead to decreased bone mass and dysregulated bone homeostasis. Although both mutant mice exhibit similar skeletal phenotypes, PLD1 and PLD2 play distinct and nonredundant roles in bone cell function. This review summarizes the physiological roles of PLD1 and PLD2 in bone metabolism, focusing on recent findings of the biological functions and action mechanisms of PLD1 and PLD2 in bone cells.
Abstract
Phospholipase D (PLD) proteins are major enzymes that regulate various cellular functions, such as cell growth, cell migration, membrane trafficking, and cytoskeletal dynamics. As they are responsible for such important biological functions, PLD proteins have been considered promising therapeutic targets for various diseases, including cancer and vascular and neurological diseases. Intriguingly, emerging evidence indicates that PLD1 and PLD2, 2 major mammalian PLD isoenzymes, are the key regulators of bone remodeling; this suggests that these isozymes could be used as potential therapeutic targets for bone diseases, such as osteoporosis and rheumatoid arthritis. PLD1 or PLD2 deficiency in mice can lead to decreased bone mass and dysregulated bone homeostasis. Although both mutant mice exhibit similar skeletal phenotypes, PLD1 and PLD2 play distinct and nonredundant roles in bone cell function. This review summarizes the physiological roles of PLD1 and PLD2 in bone metabolism, focusing on recent findings of the biological functions and action mechanisms of PLD1 and PLD2 in bone cells.
참고문헌 (57)
- Boyle WJ, "Osteoclast differentiation and activation", Nature, 423, pp.337~342 (2003)[DOI]
- Kim BJ, "Coupling factors involved in preserving bone balance", Cell Mol Life Sci, 76, pp.1243~1253 (2019)[DOI]
- Takayanagi H, "Osteoimmunology : Shared mechanisms and crosstalk between the immune and bone systems", Nat Rev Immunol, 7, pp.292~304 (2007)[DOI]
- Teitelbaum SL, "Bone resorption by osteoclasts", Science, 289, pp.1504~1508 (2000)[DOI]
- Kong YY, "OPGL is a key regulator of osteoclastogenesis, lymphocyte development and lymph-node organogenesis", Nature, 397, pp.315~323 (1999)[DOI]
- Lacey DL, "Osteoprotegerin ligand is a cytokine that regulates osteoclast differentiation and activation", Cell, 93, pp.165~176 (1998)[DOI]
- -related activation-induced cytokine), a new TNF family member predominantly expressed in T cells, is a dendritic cell-specific survival factor, "J Exp Med", 1997, 2075~2080, https:
- Yasuda H, "Osteoclast differentiation factor is a ligand for osteoprotegerin", osteoclastogenesis-inhibitory factor and is identical to TRANCE, Proc Natl Acad Sci U S A, pp.1998, 95[DOI]
- 박진희, "Current Understanding of RANK Signaling in Osteoclast Differentiation and Maturation", Molecules and Cells, 40(10), pp.706~713 (2017), 한국분자세포생물학회[DOI]
- Takayanagi H, "Induction and activation of the transcription factor NFATc1(NFAT2)integrate RANKL signaling in terminal differentiation of osteoclasts", Dev Cell, 3, pp.889~901 (2002)[DOI]
- 김정하, "Regulation of NFATc1 in Osteoclast Differentiation", 대한골대사학회지, 21(4), pp.233~241 (2014), 대한골대사학회[DOI]
- Feng X, "Osteoclasts : New insights", Bone Res, 1, pp.11~26 (2013)[DOI]
- Teitelbaum SL, "The osteoclast and its unique cytoskeleton", Ann N Y Acad Sci, 1240, pp.14~17 (2011)[DOI]
- Yoshida H, "The murine mutation osteopetrosis is in the coding region of the macrophage colony stimulating factor gene", Nature, 345, pp.442~444 (1990)[DOI]
- Pixley FJ, "CSF-1 regulation of the wandering macrophage : Complexity in action", Trends Cell Biol, 14, pp.628~638 (2004)[DOI]
- Brown HA, "Targeting phospholipase D in cancer, infection and neurodegenerative disorders", Nat Rev Drug Discov, 16, pp.351~367 (2017)[DOI]
- Ghim J, "Accumulating insights into the role of phospholipase D2 in human diseases", Adv Biol Regul, 61, pp.42~46 (2016)[DOI]
- Frohman MA, "The phospholipase D superfamily as therapeutic targets", Trends Pharmacol Sci, 36, pp.137~144 (2015)[DOI]
- Kodaki T, "Cloning, expression, and characterization of a novel phospholipase D complementary DNA from rat brain", J Biol Chem, 272, pp.11408~11413 (1997)[DOI]
- Hammond SM, "Human ADP-ribosylation factor-activated phosphatidylcholine-specific phospholipase D defines a new and highly conserved gene family", J Biol Chem, 270, pp.29640~29643 (1995)[DOI]
- Colley WC, "Phospholipase D2, a distinct phospholipase D isoform with novel regulatory properties that provokes cytoskeletal reorganization", Curr Biol, 7, pp.191~201 (1997)[DOI]
- Freyberg Z, "Intracellular localization of phospholipase D1 in mammalian cells", Mol Biol Cell, 12, pp.943~955 (2001)[DOI]
- Du G, "Regulation of phospholipase D1 subcellular cycling through coordination of multiple membrane association motifs", J Cell Biol, 162, pp.305~315 (2003)[DOI]
- Brown FD, "Phospholipase D1 localises to secretory granules and lysosomes and is plasma-membrane translocated on cellular stimulation", Curr Biol, 8, pp.835~838 (1998)[DOI]
- O’Luanaigh N, "Continual production of phosphatidic acid by phospholipase D is essential for antigen-stimulated membrane ruffling in cultured mast cells", Mol Biol Cell, 13, pp.3730~3746 (2002)[DOI]
- Du G, "Phospholipase D2 localizes to the plasma membrane and regulates angiotensin II receptor endocytosis", Mol Biol Cell, 15, pp.1024~1030 (2004)[DOI]
- Park JB, "Phospholipase signalling networks in cancer", Nat Rev Cancer, 12, pp.782~792 (2012)[DOI]
- Kang DW, "Functional regulation of phospholipase D expression in cancer and inflammation", J Biol Chem, 289, pp.22575~22582 (2014)[DOI]
- Jin JK, "Phospholipase D1 is up-regulated in the mitochondrial fraction from the brains of Alzheimer’s disease patients", Neurosci Lett, 407, pp.263~267 (2006)[DOI]
- Hong KW, "Non-synonymous single-nucleotide polymorphisms associated with blood pressure and hypertension", J Hum Hypertens, 24, pp.763~774 (2010)[DOI]
- Bae EJ, "Phospholipase D1 regulates autophagic flux and clearance of α-synuclein aggregates", Cell Death Differ, 21, pp.1132~1141 (2014)[DOI]
- Kim Hyun-Ju, "Phospholipase D2 controls bone homeostasis by modulating M-CSF-dependent osteoclastic cell migration and microtubule stability", Experimental and Molecular Medicine, 54, pp.1~10 (2022), 생화학분자생물학회[DOI]
- Kang DW, "Deletion of phospholipase D1 decreases bone mass and increases fat mass via modulation of Runx2, β-catenin-osteoprotegerin, PPAR-γ and C", EBPα signaling axis, 2021, pp.1867, 166084~
- Blackwell KA, "Prostaglandins in bone: bad cop, good cop?", Trends Endocrinol Metab, 21, pp.294~301 (2010)[DOI]
- Imamura Y, "Mechanism of phospholipase D activation induced by prostaglandin D2 in osteoblast-like cells : function of Ca2+", calmodulin, 1995, pp.7, 45~51
- Oiso Y, "Effect of prostaglandin E2 on phospholipase D activity in osteoblast-like MC3T3-E1 cells", J Bone Miner Res, 10, pp.1185~1190 (1995)[DOI]
- Kozawa O, "Prostaglandin F2 alpha activates phospholipase D independently from activation of protein kinase C in osteoblast-like cells", J Cell Biochem, 55, pp.373~379 (1994)[DOI]
- Sugiyama T, "Prostaglandin F2 alpha-stimulated phospholipase D activation in osteoblast-like MC3T3-E1 cells: involvement in sustained 1,2-diacylglycerol production", Biochem J, 298, pp.479~484 (1994)[DOI]
- Kozawa O, "Effect of platelet-derived growth factor on phosphatidylcholine-hydrolyzing phospholipase D in osteoblast-like cells", Endocrinology, 136, pp.4473~4478 (1995)[DOI]
- Suzuki A, "Basic fibroblast growth factor stimulates phosphatidylcholine-hydrolyzing phospholipase D in osteoblast-like cells", J Cell Biochem, 63, pp.491~499 (1996)[DOI]
- Carpio LC, "Activation of phospholipase D signaling pathway by epidermal growth factor in osteoblastic cells", J Bone Miner Res, 13, pp.1707~1713 (1998)[DOI]
- Carpio LC, "Phosphatidic acid effects on cytosolic calcium and proliferation in osteoblastic cells", Prostaglandins Leukot Essent Fatty Acids, 59, pp.101~109 (1998)[DOI]
- Singh AT, "Parathyroid hormone stimulates phosphatidylethanolamine hydrolysis by phospholipase D in osteoblastic cells", Lipids, 40, pp.1135~1140 (2005)[DOI]
- Singh AT, "G alpha12", G alpha13 subunits of heterotrimeric G proteins mediate parathyroid hormone activation of phospholipase D in UMR-106 osteoblastic cells, 2005, pp.146, 2171~2175
- Kim MJ, "Activation of phospholipase D1 by surface roughness of titanium in MG63 osteoblast-like cell", Biomaterials, 27, pp.5502~5511 (2006)[DOI]
- Abdallah D, "Effects of phospholipase D during cultured osteoblast mineralization and bone formation", J Cell Biochem, 120, pp.5923~5935 (2019)[DOI]
- Bendre MS, "Tumor-derived interleukin-8 stimulates osteolysis independent of the receptor activator of nuclear factor-kappaB ligand pathway", Cancer Res, 65, pp.11001~11009 (2005)[DOI]
- Hsu YL, "Phospholipase D signaling pathway is involved in lung cancer-derived IL-8 increased osteoclastogenesis", Carcinogenesis, 31, pp.587~596 (2010)[DOI]
- Wan Y, "PPAR-gamma regulates osteoclastogenesis in mice", Nat Med, 13, pp.1496~1503 (2007)[DOI]
- Chen W, "C", EBPα regulates osteoclast lineage commitment, 2013, pp.110, 7294~7299
- Han SW, "DICAM inhibits angiogenesis via suppression of AKT and p38 MAP kinase signalling", Cardiovasc Res, 98, pp.73~82 (2013)[DOI]
- Munugalavadla V, "The p85alpha subunit of class IA phosphatidylinositol 3-kinase regulates the expression of multiple genes involved in osteoclast maturation and migration", Mol Cell Biol, 28, pp.7182~7198 (2008)[DOI]
- Destaing O, "Podosomes display actin turnover and dynamic self-organization in osteoclasts expressing actin-green fluorescent protein", Mol Biol Cell, 14, pp.407~416 (2003)[DOI]
- Jurdic P, "Podosome and sealing zone : specificity of the osteoclast model", Eur J Cell Biol, 85, pp.195~202 (2006)[DOI]
- Hong JM, "Calpain-6, a target molecule of glucocorticoids, regulates osteoclastic bone resorption via cytoskeletal organization and microtubule acetylation", J Bone Miner Res, 26, pp.657~665 (2011)[DOI]
- Shinohara M, "Class IA phosphatidylinositol 3-kinase regulates osteoclastic bone resorption through protein kinase B-mediated vesicle transport", J Bone Miner Res, 27, pp.2464~2475 (2012)[DOI]
- Matsumoto T, "Regulation of bone resorption and sealing zone formation in osteoclasts occurs through protein kinase B-mediated microtubule stabilization", J Bone Miner Res, 28, pp.1191~1202 (2013)[DOI]
