- 同
- PLC
WordNet
- the 3rd letter of the Roman alphabet (同)c
- (music) the keynote of the scale of C major
- a general-purpose programing language closely associated with the UNIX operating system
PrepTutorEJDIC
- carbonの化学記号
- cesiumの化学記号
- cadmiumの化学記号
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2013/06/13 12:34:25」(JST)
[Wiki en表示]
Cleavage sites of phospholipases. Phospholipase C enzymes cut just before the phosphate attached to the R
3 moiety.
Phospholipase C (PLC) is a class of enzymes that cleave phospholipids just before the phosphate group (see figure). It is most commonly taken to be synonymous with the human forms of this enzyme, which play an important role in eukaryotic cell physiology, in particular signal transduction pathways. Thirteen kinds of mammalian phospholipase C are classified into six isotypes (β, γ, δ, ε, ζ, η) according to structure.
Contents
- 1 Mammalian variants
- 1.1 Activation
- 1.2 Effects
- 2 In other organisms
- 3 See also
- 4 References
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Mammalian variants[edit]
- beta: PLCB1, PLCB2, PLCB3, PLCB4
- gamma: PLCG1, PLCG2
- delta: PLCD1, PLCD3, PLCD4
- epsilon: PLCE1
- eta: PLCH1, PLCH2
- zeta: PLCZ1
- phospholipase C-like: PLCL1, PLCL2
Activation[edit]
Receptors that activate this pathway are mainly G protein-coupled receptors coupled to the Gαq subunit, including:
- 5-HT2 serotonergic receptors
- α1 (Alpha-1) adrenergic receptors[1]
- Calcitonin receptors
- H1 histamine receptors
- Metabotropic glutamate receptors, Group I
- M1, M3, and M5 muscarinic receptors
- Thyroid Releasing Hormone receptor in anterior pituitary gland
Other, minor, activators than Gαq are:
- MAP kinase. Activators of this pathway include PDGF and FGF.[1]
- βγ-complex of heterotrimeric G-proteins, as in a minor pathway of growth hormone release by growth hormone-releasing hormone.[2]
Effects[edit]
PLC cleaves the phospholipid phosphatidylinositol 4,5-bisphosphate (PIP2) into diacyl glycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). DAG remains bound to the membrane, and IP3 is released as a soluble structure into the cytosol. IP3 then diffuses through the cytosol to bind to IP3 receptors, particular calcium channels in the smooth endoplasmic reticulum (ER). This causes the cytosolic concentration of calcium to increase, causing a cascade of intracellular changes and activity.[3] In addition, calcium and DAG together work to activate protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity.[3] End effects include taste, tumor promotion, etc.[3]
Further information: Calcium function in vertebrates, Function of protein kinase C
In other organisms[edit]
Other phospholipase C enzymes have been identified in bacteria and in trypanosomes, each with its own EC number
- Phosphoinositide phospholipase C EC 3.1.4.11 The main form found in eukaryotes, especially mammals.
- Zinc-dependent phospholipase C family of bacterial enzymes EC 3.1.4.3 that includes alpha toxins
- Phosphatidylinositol diacylglycerol-lyase EC 4.6.1.13 Another related bacterial enzyme
- Glycosylphosphatidylinositol diacylglycerol-lyase EC 4.6.1.14 A trypanosomal enzyme.
See also[edit]
References[edit]
- ^ a b Walter F., PhD. Boron (2003). Medical Physiology: A Cellular And Molecular Approaoch. Elsevier/Saunders. p. 1300. ISBN 1-4160-2328-3. Page 104
- ^ GeneGlobe -> GHRH Signaling Retrieved on May 31, 2009
- ^ a b c Alberts B, Lewis J, Raff M, Roberts K, Walter P (2002). Molecular biology of the cell (4th ed.). New York: Garland Science. ISBN 0-8153-3218-1.
Hydrolase: esterases (EC 3.1)
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3.1.1: Carboxylic ester hydrolases |
- Cholinesterase
- Acetylcholinesterase
- Butyrylcholinesterase
- Pectinesterase
- 6-phosphogluconolactonase
- PAF acetylhydrolase
- Lipase
- Bile salt-dependent
- Gastric/Lingual
- Pancreatic
- Lysosomal
- Hormone-sensitive
- Endothelial
- Hepatic
- Lipoprotein
- Monoacylglycerol
- Diacylglycerol
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3.1.2: Thioesterase |
- Palmitoyl protein thioesterase
- Ubiquitin carboxy-terminal hydrolase L1
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3.1.3: Phosphatase |
- Alkaline phosphatase
- Acid phosphatase (Prostatic)/Tartrate-resistant acid phosphatase/Purple acid phosphatases
- Nucleotidase
- Glucose 6-phosphatase
- Fructose 1,6-bisphosphatase
- Phosphoprotein phosphatase
- OCRL
- Pyruvate dehydrogenase phosphatase
- Fructose 6-P,2-kinase:fructose 2,6-bisphosphatase
- PTEN
- Phytase
- Inositol-phosphate phosphatase
- Phosphoprotein phosphatase: Protein tyrosine phosphatase
- Protein serine/threonine phosphatase
- Dual-specificity phosphatase
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3.1.4: Phosphodiesterase |
- Autotaxin
- Phospholipase
- Sphingomyelin phosphodiesterase
- PDE1
- PDE2
- PDE3
- PDE4A/PDE4B
- PDE5
- Lecithinase (Clostridium perfringens alpha toxin)
- Cyclic nucleotide phosphodiesterase
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3.1.6: Sulfatase |
- arylsulfatase
- Arylsulfatase A
- Arylsulfatase B
- Arylsulfatase E
- Steroid sulfatase
- Galactosamine-6 sulfatase
- Iduronate-2-sulfatase
- N-acetylglucosamine-6-sulfatase
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Nuclease (includes
deoxyribonuclease and
ribonuclease) |
3.1.11-16: Exonuclease |
Exodeoxyribonuclease |
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Exoribonuclease |
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3.1.21-31: Endonuclease |
Endodeoxyribonuclease |
- Deoxyribonuclease I
- Deoxyribonuclease II
- Deoxyribonuclease IV
- Restriction enzyme
- UvrABC endonuclease
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Endoribonuclease |
- RNase III
- RNase H
- RNase P
- RNase A
- RNase T1
- RNA-induced silencing complex
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either deoxy- or ribo- |
- Aspergillus nuclease S1
- Micrococcal nuclease
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- B
- enzm
- 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 2.7.10
- 2.7.11-12
- 3.1
- 4.1
- 5.1
- 6.1-3
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Metabolism: lipid metabolism - eicosanoid metabolism enzymes
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Precursor |
- Phospholipase C
- Diacylglycerol lipase
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Prostanoids |
- PGE synthase
- Prostaglandin-E2 9-reductase
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Leukotrienes |
- 5-Lipoxygenase activating protein/Arachidonate 5-lipoxygenase
- LTA4 hydrolase (B4 synthesis)
- LTC4 synthase
- Gamma-glutamyl transpeptidase
- DPEP2
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Ungrouped |
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mt, k, c/g/r/p/y/i, f/h/s/l/o/e, a/u, n, m
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k, cgrp/y/i, f/h/s/l/o/e, au, n, m, epon
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m (A16/C10), i (k, c/g/r/p/y/i, f/h/s/o/e, a/u, n, m)
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Metabolism: lipid metabolism - phospholipids
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Anabolism |
to diacylglycerol: Acyltransferase · Phosphatidate phosphatase (2C)
Choline kinase (CHKA, CHKB) · Choline-phosphate cytidylyltransferase
phosphatidylinositol glycan anchor biosynthesis: (PIGA, PIGB, PIGC, PIGF, PIGG, PIGH, PIGK, PIGL, PIGM, PIGN, PIGO, PIGP, PIGQ, PIGS, PIGT, PIGU, PIGV, PIGW, PIGX, PIGY, PIGZ)
cardiolipin: Tafazzin
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Catabolism |
Phospholipase C
Diacylglycerol kinase (DGKA, DGKB, DGKD, DGKE, DGKG, DGKH, DGKI, DGKK, DGKQ, DGKZ)
Phosphoric monoester hydrolases · Inositol-phosphate phosphatase
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mt, k, c/g/r/p/y/i, f/h/s/l/o/e, a/u, n, m
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k, cgrp/y/i, f/h/s/l/o/e, au, n, m, epon
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m (A16/C10), i (k, c/g/r/p/y/i, f/h/s/o/e, a/u, n, m)
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UpToDate Contents
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English Journal
- Transgenic labeling of higher order neuronal circuits linked to phospholipase C-β2-expressing taste bud cells in medaka fish.
- Ieki T, Okada S, Aihara Y, Ohmoto M, Abe K, Yasuoka A, Misaka T.SourceDepartment of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo, 113-8657, Japan.
- The Journal of comparative neurology.J Comp Neurol.2013 Jun 1;521(8):1781-802. doi: 10.1002/cne.23256.
- The sense of taste plays a pivotal role in the food-selecting behaviors of vertebrates. We have shown that the fish ortholog of the phospholipase C gene (plc-β2) is expressed in a subpopulation of taste bud cells that transmit taste stimuli to the central nervous system to evoke favorable and avers
- PMID 23124957
- Sex-specific response of rat costochondral cartilage growth plate chondrocytes to 17β-estradiol involves differential regulation of plasma membrane associated estrogen receptors.
- Elbaradie KB, Wang Y, Boyan BD, Schwartz Z.SourceSchool of Biology, Georgia Institute of Technology, Atlanta, GA, USA.
- Biochimica et biophysica acta.Biochim Biophys Acta.2013 May;1833(5):1165-72. doi: 10.1016/j.bbamcr.2012.12.022. Epub 2013 Jan 7.
- Both male and female rat growth plate chondrocytes express estrogen receptors (ERs); however 17β-estradiol (E2) induces membrane responses leading to activation of phospholipase A2 (PLA2), phospholipase C (PLC), prostaglandin E2 (PGE2) production, protein kinase C (PKC), and ultimately mitogen prot
- PMID 23305904
- The unique role of dietary L-arginine in the acceleration of peritoneal macrophage sensitivity to bacterial endotoxin.
- Pekarova M, Kubala L, Martiskova H, Papezikova I, Kralova S, Baldus S, Klinke A, Kuchta R, Kadlec J, Kuchtova Z, Kolarova H, Lojek A.SourceInstitute of Biophysics, Academy of Sciences of the Czech Republic v.v.i., Kralovopolska 135, 612 65, Brno, Czech Republic, pekarovam@ibp.cz.
- Immunologic research.Immunol Res.2013 May;56(1):73-84. doi: 10.1007/s12026-012-8379-2.
- It is known that cells and organisms can indirectly "sense" changes in L-arginine availability via changes in the activity of various metabolic pathways. However, the mechanism(s) by which genes can be directly regulated by L-arginine in mammalian cells have not yet been elucidated. We investigated
- PMID 23184235
Japanese Journal
- N-アシルエタノールアミンプラスマローゲンからのN-アシルホスファチジルエタノールアミン水解ホスホリパーゼD依存的および非依存的経路を介したN-アシルエタノールアミンの生合成
- 坪井 一人,岡本 安雄,池松 夏紀,井上 愛美,清水 嘉文,宇山 徹,王 俊,Deutsch Dale G.,Burns Matthew P.,Ulloa Nadine M.,徳村 彰,上田 夏生
- ビタミン 87(5・6), 267-270, 2013-06-25
- NAID 110009612886
- Phospholipase C Produced by Clostridium botulinum Types C and D:Comparison of Gene, Enzymatic, and Biological Activities with Those of Clostridium perfringens Alpha-toxin
- Fatmawati Ni Nengah Dwi,Sakaguchi Yoshihiko,Suzuki Tomonori,Oda Masataka,Shimizu Kenta,Yamamoto Yumiko,Sakurai Jun,Matsushita Osamu,Oguma Keiji
- Acta Medica Okayama 67(1), 9-18, 2013-02-00
- Clostridium botulinum type C and D strains recently have been found to produce PLC on egg yolk agar plates. To characterize the gene, enzymatic and biological activities of C. botulinum PLCs (Cb-PLCs) …
- NAID 120005232332
- Structural Characteristics and Evolution of the Protobothrops elegans Pancreatic Phospholipase A? Gene in Contrast with Those of Protobothrops Genus Venom Phospholipase A? Genes
- CHIJIWA Takahito,NAKASONE Hideto,IRIE Sakiko [他]
- Bioscience, Biotechnology, and Biochemistry 77(1), 97-102, 2013-01-00
- NAID 40019561827
Related Links
- phos·pho·lip·ase C Clostridium welchii α-toxin; C. oedematiens β- and γ-toxins; an enzyme that catalyzes the hydrolysis of phosphatidylcholine (and possibly other phospholipids) to produce choline phosphate and 1,2-diacylglycerol ...
- F5807 FIPI hydrochloride hydrate ≥98% (HPLC), powder FIPI is a potent Phospholipase D (PLD) inhibitor. The signaling enzyme Phospholipase D (PLD) and the lipid second messenger phosphatidic acid (PA) generated by PLD are ...
Related Pictures
★リンクテーブル★
[★]
[★]
- 関
- phosphoinositide phospholipase C、phospholipase C、PLC
[★]
- 英
- phospholipase C, PLC
- 関
- ホスホリパーゼ
[★]
グリコシルホスファチジルイノシトール特異的ホスホリパーゼC
- 関
- glycosylphosphatidylinositol diacylglycerol-lyase、GPI-PLC
[★]
- 関
- phospholipase C、PLC、type C phospholipase
[★]
ホスホリパーゼCγ
- 関
- PLC-gamma
[★]
[★]
セシウム, caesium, cesium
[★]
カドミウム
- 関
- cadmium
[★]