肝性リパーゼ
WordNet
- pertaining to or affecting the liver; "hepatic ducts"; "hepatic cirrhosis"
- an enzyme secreted in the digestive tract that catalyzes the breakdown of fats into individual fatty acids that can be absorbed into the bloodstream
PrepTutorEJDIC
- 肝臓の;肝臓にきく,肝臓のような色の
- リパーゼ(脂肪分解酵素)
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2013/10/08 22:16:13」(JST)
[Wiki en表示]
Lipase, hepatic |
Identifiers |
Symbols |
LIPC; HDLCQ12; HL; HTGL; LIPH |
External IDs |
OMIM: 151670 MGI: 96216 HomoloGene: 199 ChEMBL: 2127 GeneCards: LIPC Gene |
EC number |
3.1.1.3 |
Gene Ontology |
Molecular function |
• phospholipase activity
• triglyceride lipase activity
• heparin binding
• low-density lipoprotein particle binding
• apolipoprotein binding
• retinyl-palmitate esterase activity
|
Cellular component |
• extracellular space
• high-density lipoprotein particle
|
Biological process |
• fatty acid biosynthetic process
• cholesterol metabolic process
• triglyceride catabolic process
• very-low-density lipoprotein particle remodeling
• intermediate-density lipoprotein particle remodeling
• low-density lipoprotein particle remodeling
• high-density lipoprotein particle remodeling
• chylomicron remnant clearance
• phosphatidylcholine catabolic process
• cholesterol homeostasis
• reverse cholesterol transport
• triglyceride homeostasis
|
Sources: Amigo / QuickGO |
|
RNA expression pattern |
|
More reference expression data |
Orthologs |
Species |
Human |
Mouse |
|
Entrez |
3990 |
15450 |
|
Ensembl |
ENSG00000166035 |
ENSMUSG00000032207 |
|
UniProt |
P11150 |
P27656 |
|
RefSeq (mRNA) |
NM_000236 |
NM_008280 |
|
RefSeq (protein) |
NP_000227 |
NP_032306 |
|
Location (UCSC) |
Chr 15:
58.7 – 58.86 Mb |
Chr 9:
70.8 – 70.93 Mb |
|
PubMed search |
[1] |
[2] |
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Hepatic lipase is a form of lipase. It is expressed in the liver and adrenal glands.[1]
One of the principal functions of hepatic lipase is to convert intermediate-density lipoprotein (IDL) to low-density lipoprotein (LDL).
LIPC encodes hepatic triglyceride lipase (HTGL), which is expressed in liver. LIPC has the dual functions of triglyceride hydrolase and ligand/bridging factor for receptor-mediated lipoprotein uptake.[2]
Contents
- 1 Clinical significance
- 2 Interactive pathway map
- 3 References
- 4 Further reading
- 5 External links
Clinical significance[edit]
Hepatic lipase deficiency is a rare, autosomal recessive disorder that results in elevated high density lipoprotein (HDL) cholesterol due to a mutation in the hepatic lipase gene. Clinical features are not well understood and there are no characteristic xanthomas. There is an association with a delay in atherosclerosis in an animal model.[3]
Interactive pathway map[edit]
Click on genes, proteins and metabolites below to link to respective articles. [§ 1]
- ^ The interactive pathway map can be edited at WikiPathways: "Statin_Pathway_WP430".
References[edit]
- ^ Dichek HL, Agrawal N, El Andaloussi N, Qian K (2006). "Attenuated corticosterone response to chronic ACTH stimulation in hepatic lipase-deficient mice: evidence for a role for hepatic lipase in adrenal physiology". Am. J. Physiol. Endocrinol. Metab. 290 (5): E908–15. doi:10.1152/ajpendo.00442.2005. PMID 16368783.
- ^ "Entrez Gene: LIPC lipase, hepatic".
- ^ Karackattu SL, Trigatti B, Krieger M (2006). "Hepatic lipase deficiency delays atherosclerosis, myocardial infarction, and cardiac dysfunction and extends lifespan in SR-BI/apolipoprotein E double knockout mice". Arterioscler. Thromb. Vasc. Biol. 26 (3): 548–54. doi:10.1161/01.ATV.0000202662.63876.02. PMID 16397139.
Further reading[edit]
- Santamarina-Fojo S, Haudenschild C, Amar M (1998). "The role of hepatic lipase in lipoprotein metabolism and atherosclerosis.". Curr. Opin. Lipidol. 9 (3): 211–9. doi:10.1097/00041433-199806000-00005. PMID 9645503.
- Jansen H, Verhoeven AJ, Sijbrands EJ (2003). "Hepatic lipase: a pro- or anti-atherogenic protein?". J. Lipid Res. 43 (9): 1352–62. doi:10.1194/jlr.R200008-JLR200. PMID 12235167.
- Zambon A, Deeb SS, Pauletto P, et al. (2003). "Hepatic lipase: a marker for cardiovascular disease risk and response to therapy.". Curr. Opin. Lipidol. 14 (2): 179–89. doi:10.1097/01.mol.0000064055.08840.77. PMID 12642787.
- Hegele RA, Tu L, Connelly PW (1993). "Human hepatic lipase mutations and polymorphisms.". Hum. Mutat. 1 (4): 320–4. doi:10.1002/humu.1380010410. PMID 1301939.
- Hegele RA, Vezina C, Moorjani S, et al. (1991). "A hepatic lipase gene mutation associated with heritable lipolytic deficiency.". J. Clin. Endocrinol. Metab. 72 (3): 730–2. doi:10.1210/jcem-72-3-730. PMID 1671786.
- Hegele RA, Little JA, Connelly PW (1991). "Compound heterozygosity for mutant hepatic lipase in familial hepatic lipase deficiency.". Biochem. Biophys. Res. Commun. 179 (1): 78–84. doi:10.1016/0006-291X(91)91336-B. PMID 1883393.
- Ameis D, Stahnke G, Kobayashi J, et al. (1990). "Isolation and characterization of the human hepatic lipase gene.". J. Biol. Chem. 265 (12): 6552–5. PMID 2324091.
- Datta S, Luo CC, Li WH, et al. (1988). "Human hepatic lipase. Cloned cDNA sequence, restriction fragment length polymorphisms, chromosomal localization, and evolutionary relationships with lipoprotein lipase and pancreatic lipase.". J. Biol. Chem. 263 (3): 1107–10. PMID 2447084.
- Cai SJ, Wong DM, Chen SH, Chan L (1990). "Structure of the human hepatic triglyceride lipase gene.". Biochemistry 28 (23): 8966–71. doi:10.1021/bi00449a002. PMID 2605236.
- Stahnke G, Sprengel R, Augustin J, Will H (1988). "Human hepatic triglyceride lipase: cDNA cloning, amino acid sequence and expression in a cultured cell line.". Differentiation 35 (1): 45–52. doi:10.1111/j.1432-0436.1987.tb00150.x. PMID 2828141.
- Martin GA, Busch SJ, Meredith GD, et al. (1988). "Isolation and cDNA sequence of human postheparin plasma hepatic triglyceride lipase.". J. Biol. Chem. 263 (22): 10907–14. PMID 2839510.
- Sparkes RS, Zollman S, Klisak I, et al. (1988). "Human genes involved in lipolysis of plasma lipoproteins: mapping of loci for lipoprotein lipase to 8p22 and hepatic lipase to 15q21.". Genomics 1 (2): 138–44. doi:10.1016/0888-7543(87)90005-X. PMID 3692485.
- Kounnas MZ, Chappell DA, Wong H, et al. (1995). "The cellular internalization and degradation of hepatic lipase is mediated by low density lipoprotein receptor-related protein and requires cell surface proteoglycans.". J. Biol. Chem. 270 (16): 9307–12. doi:10.1074/jbc.270.16.9543. PMID 7721852.
- Mori A, Takagi A, Ikeda Y, et al. (1996). "An AvaII polymorphism in exon 5 of the human hepatic triglyceride lipase gene.". Mol. Cell. Probes 10 (4): 309–11. doi:10.1006/mcpr.1996.0040. PMID 8865179.
- Takagi A, Ikeda Y, Mori A, et al. (1996). "Identification of a BstNI polymorphism in exon 9 of the human hepatic triglyceride lipase gene.". Mol. Cell. Probes 10 (4): 313–4. doi:10.1006/mcpr.1996.0041. PMID 8865180.
- Choi SY, Goldberg IJ, Curtiss LK, Cooper AD (1998). "Interaction between ApoB and hepatic lipase mediates the uptake of ApoB-containing lipoproteins.". J. Biol. Chem. 273 (32): 20456–62. doi:10.1074/jbc.273.32.20456. PMID 9685400.
- Cargill M, Altshuler D, Ireland J, et al. (1999). "Characterization of single-nucleotide polymorphisms in coding regions of human genes.". Nat. Genet. 22 (3): 231–8. doi:10.1038/10290. PMID 10391209.
- Tiebel O, Gehrisch S, Pietzsch J, et al. (2000). "18 bp insertion/duplication with internal missense mutation in human hepatic lipase gene exon 3. Mutations in brief no. 181. Online.". Hum. Mutat. 12 (3): 216. PMID 10660332.
- Yamakawa-Kobayashi K, Somekawa Y, Fujimura M, et al. (2002). "Relation of the -514C/T polymorphism in the hepatic lipase gene to serum HDL and LDL cholesterol levels in postmenopausal women under hormone replacement therapy.". Atherosclerosis 162 (1): 17–21. doi:10.1016/S0021-9150(01)00675-X. PMID 11947893.
External links[edit]
- hepatic lipase, human at the US National Library of Medicine Medical Subject Headings (MeSH)
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
- 3.1
- 4.1
- 5.1
- 6.1-3
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Lipids: lipoprotein particle metabolism
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Lipoprotein particle classes and subclasses |
- delivery of TGs: Chylomicron
- VLDL
- delivery of C and CE: IDL
- LDL
- lb LDL
- sd LDL
- Lp(a)
- HDL
|
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Apolipoproteins |
- APOA
- APOB
- APOC
- APOD
- APOE
- APOH
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Extracellular enzymes |
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Lipid transfer proteins |
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Cell surface receptors |
- IDL: LRP
- LRP1
- LRP1B
- LRP2
- LRP3
- LRP4
- LRP5
- LRP5L
- LRP6
- LRP8
- LRP10
- LRP11
- LRP12
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ATP-binding cassette transporter |
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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
|
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
- ADIPOQ single nucleotide polymorphism: Association with adiponectin and lipoproteins levels restricted to men.
- Tureck LV1, Leite N2, Souza RL1, da Silva Timossi L2, Osiecki AC2, Osiecki R2, Alle LF1.
- Meta gene.Meta Gene.2015 Jun 17;5:98-104. doi: 10.1016/j.mgene.2015.06.003. eCollection 2015.
- Adiponectin is an adipokine inversely correlated with obesity, which has beneficial effect on insulin resistance and lipid metabolism. Considering its potential as a therapeutic target in the metabolic disorder contexts, and in order to add knowledge in the area, our study evaluated the ADIPOQ 276G�
- PMID 26137445
- Cholestane-3β,5α,6β-triol in lipidosis: High levels in Niemann Pick type C, Cerebrotendinous Xanthomatosis and Lysosomal Acid Lipase deficiency.
- Pajares S1, Arias A1, Garcia-Villoria J1, Macias-Vidal J1, Ros E2, de Las Heras J3, Giros M1, Coll MJ1, Ribes A4.
- Journal of lipid research.J Lipid Res.2015 Aug 3. pii: jlr.M060343. [Epub ahead of print]
- Niemann-Pick type C (NPC) is a progressive neurodegenerative disease characterized by lysosomal/endosomal accumulation of unesterified cholesterol and glycolipids. Recent studies have shown that plasma cholestane-3b,5a,6b-triol (CT) and 7-ketocholesterol (7-KC) could be potential biomarkers for the
- PMID 26239048
- Plasma Apolipoprotein C-III Levels, Triglycerides, and Coronary Artery Calcification in Type 2 Diabetics.
- Qamar A1, Khetarpal SA1, Khera AV1, Qasim A1, Rader DJ2, Reilly MP2.
- Arteriosclerosis, thrombosis, and vascular biology.Arterioscler Thromb Vasc Biol.2015 Aug;35(8):1880-8. doi: 10.1161/ATVBAHA.115.305415. Epub 2015 Jun 11.
- OBJECTIVE: Triglyceride-rich lipoproteins have emerged as causal risk factors for developing coronary heart disease independent of low-density lipoprotein cholesterol levels. Apolipoprotein C-III (ApoC-III) modulates triglyceride-rich lipoprotein metabolism through inhibition of lipoprotein lipase a
- PMID 26069232
Japanese Journal
- 初代培養ラット肝細胞系におけるプラゾシンによる肝性リパーゼの分泌促進に対するロイコトリエン代謝系の関与
Related Links
- Hepatic lipase is a form of lipase. It is expressed in the liver and adrenal glands. One of the principal functions of hepatic lipase is to convert IDL to LDL. LIPC encodes hepatic triglyceride lipase (HTGL), which is expressed in liver. LIPC has the ...
Related Pictures
★リンクテーブル★
[★]
- 英
- hepatic triacylglycerol lipase, HTGL
- 同
- 肝性リパーゼ hepatic lipase
[★]
- 英
- hepatic lipase
- 関
- 肝性トリアシルグリセロールリパーゼ
[★]
- 関
- hepato、hepatogenic、liver