ホルモン感受性リパーゼ
WordNet
- responsive to physical stimuli; "a mimosas leaves are sensitive to touch"; "a sensitive voltmeter"; "sensitive skin"; "sensitive to light"
- hurting; "the tender spot on his jaw" (同)sore, raw, tender
- being susceptible to the attitudes, feelings, or circumstances of others; "sensitive to the local community and its needs"
- of or pertaining to classified information or matters affecting national security
- an enzyme secreted in the digestive tract that catalyzes the breakdown of fats into individual fatty acids that can be absorbed into the bloodstream
- the secretion of an endocrine gland that is transmitted by the blood to the tissue on which it has a specific effect (同)endocrine, internal_secretion
PrepTutorEJDIC
- (五感が)『敏感な』,感じやすい / 物事を非常に気にする,神経過敏な / 感光性の;(器械などが)感度のよい
- リパーゼ(脂肪分解酵素)
- ホルモン
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2013/06/15 06:30:29」(JST)
[Wiki en表示]
| Lipase, hormone-sensitive |
| Identifiers |
| Symbols |
LIPE; HSL; LHS |
| External IDs |
OMIM: 151750 MGI: 96790 HomoloGene: 3912 ChEMBL: 3590 GeneCards: LIPE Gene |
| EC number |
3.1.1.79 |
| Gene Ontology |
| Molecular function |
• triglyceride lipase activity
• protein binding
• protein kinase binding
• hormone-sensitive lipase activity
|
| Cellular component |
• lipid particle
• cytosol
• caveola
|
| Biological process |
• protein phosphorylation
• lipid metabolic process
• cholesterol metabolic process
• lipid catabolic process
• triglyceride catabolic process
• small molecule metabolic process
• diacylglycerol catabolic process
|
| Sources: Amigo / QuickGO |
|
| RNA expression pattern |
|
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| More reference expression data |
| Orthologs |
| Species |
Human |
Mouse |
|
| Entrez |
3991 |
16890 |
|
| Ensembl |
ENSG00000079435 |
ENSMUSG00000003123 |
|
| UniProt |
Q05469 |
P54310 |
|
| RefSeq (mRNA) |
NM_005357 |
NM_001039507 |
|
| RefSeq (protein) |
NP_005348 |
NP_001034596 |
|
| Location (UCSC) |
Chr 19:
42.91 – 42.93 Mb |
Chr 7:
25.38 – 25.4 Mb |
|
| PubMed search |
[1] |
[2] |
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| Hormone-sensitive lipase (HSL) N-terminus |
| Identifiers |
| Symbol |
HSL_N |
| Pfam |
PF06350 |
| InterPro |
IPR010468 |
| Available protein structures: |
| Pfam |
structures |
| PDB |
RCSB PDB; PDBe |
| PDBsum |
structure summary |
|
Hormone-sensitive lipase (EC 3.1.1.79, HSL) also previously known as cholesteryl ester hydrolase (CEH)[1] is an enzyme that, in humans, is encoded by the LIPE gene.[2]
HSL is an intracellular neutral lipase that is capable of hydrolyzing a variety of esters.[3] The enzyme has a long and a short form. The long form is expressed in steroidogenic tissues such as testis, where it converts cholesteryl esters to free cholesterol for steroid hormone production. The short form is expressed in adipose tissue, among others, where it hydrolyzes stored triglycerides to free fatty acids.[4]
|
Contents
- 1 Nomenclature
- 2 Function
- 3 Activation
- 4 References
- 5 Further reading
- 6 External links
|
Nomenclature[edit]
During fasting-state the increased free fatty acid secretion by adipocyte cells was attributed to epinephrine hormone. Hence the name "hormone-sensitive lipase".[5] Other hormones like catecholamines, adrenocorticotropic hormone (ACTH), and glucagon can also stimulate such responses. Such enzymatic action plays a key role in providing major source of energy for most cells.
Function[edit]
HSL functions to hydrolyze the first fatty acid from a triacylglycerol molecule, freeing a fatty acid and diglyceride. It is also known as triglyceride lipase, while the enzyme that cleaves the second fatty acid in the triglyceride is known as diglyceride lipase, and the third enzyme that cleaves the final fatty acid is called monoglyceride lipase. Only the initial enzyme is affected by hormones, hence its hormone-sensitive lipase name. The diglyceride and monoglyceride enzymes are tens to hundreds of times faster, hence HSL is the rate-limiting step in cleaving fatty acids from the triglyceride molecule.[6][7]
HSL is activated when the body needs to mobilize energy stores, and so responds positively to catecholamines, ACTH. It is inhibited by insulin. Previously, glucagon was thought to activate HSL, however the removal of insulin's inhibitory effects ("cutting the brakes") is the source of activation. The lipolytic effect of glucagon in adipose tissue is minimal in humans.[citation needed]
Another important role is the release of cholesterol from cholesterol esters for use in the production of steroids.[8]
Activation[edit]
It may be activated by two mechanisms.[9]
- In the first, phosphorylated perilipin A causes it to move to the surface of the lipid droplet, where it may begin hydrolyzing the lipid droplet.
- Also, it may be activated by a cAMP-dependent protein kinase (PKA). This pathway is significantly less effective than the first, which is necessary for lipid mobilization in response to cyclic AMP, which itself is provided by the activation of Gs protein-coupled receptors that promote cAMP production. Examples include beta adrenergic stimulation of the glucagon receptor and ACTH stimulation of the ACTH receptor in the adrenal cortex.
References[edit]
- ^ Aten RF, Kolodecik TR, Macdonald GJ, Behrman HR (November 1995). "Modulation of cholesteryl ester hydrolase messenger ribonucleic acid levels, protein levels, and activity in the rat corpus luteum". Biol. Reprod. 53 (5): 1110–7. doi:10.1095/biolreprod53.5.1110. PMID 8527515.
- ^ Langin D, Laurell H, Holst LS, Belfrage P, Holm C (June 1993). "Gene organization and primary structure of human hormone-sensitive lipase: possible significance of a sequence homology with a lipase of Moraxella TA144, an antarctic bacterium". Proc. Natl. Acad. Sci. U.S.A. 90 (11): 4897–901. doi:10.1073/pnas.90.11.4897. PMC 46620. PMID 8506334.
- ^ Kraemer FB, Shen WJ (October 2002). "Hormone-sensitive lipase: control of intracellular tri-(di-)acylglycerol and cholesteryl ester hydrolysis". J. Lipid Res. 43 (10): 1585–94. doi:10.1194/jlr.R200009-JLR200. PMID 12364542.
- ^ "Entrez Gene: LIPE lipase, hormone-sensitive".
- ^ Kraemer FB, Shen WJ (October 2002). "Hormone-sensitive lipase: control of intracellular tri-(di-)acylglycerol and cholesteryl ester hydrolysis". J. Lipid Res. 43 (10): 1585–94. doi:10.1194/jlr.R200009-JLR200. PMID 12364542.
- ^ Crabtree B, Newsholme EA (December 1972). "The activities of lipases and carnitine palmitoyltransferase in muscles from vertebrates and invertebrates". Biochem. J. 130 (3): 697–705. PMC 1174508. PMID 4664927.
- ^ [Meijer J] (1998-05-01). Hormone sensitive lipase: structure, function and regulation. demeijer.com. Retrieved 2009-02-04.
- ^ Kraemer FB (February 2007). "Adrenal cholesterol utilization". Mol. Cell. Endocrinol. 265-266: 42–5. doi:10.1016/j.mce.2006.12.001. PMID 17208360.
- ^ Cox, Michael; Nelson, David R.; Lehninger, Albert L (2005). Lehninger principles of biochemistry. San Francisco: W.H. Freeman. ISBN 0-7167-4339-6.
Further reading[edit]
- Kraemer FB, Shen WJ (2003). "Hormone-sensitive lipase: control of intracellular tri-(di-)acylglycerol and cholesteryl ester hydrolysis.". J. Lipid Res. 43 (10): 1585–94. doi:10.1194/jlr.R200009-JLR200. PMID 12364542.
- Langfort J, Donsmark M, Ploug T, et al. (2003). "Hormone-sensitive lipase in skeletal muscle: regulatory mechanisms.". Acta Physiol. Scand. 178 (4): 397–403. doi:10.1046/j.1365-201X.2003.01155.x. PMID 12864745.
- Holm C (2004). "Molecular mechanisms regulating hormone-sensitive lipase and lipolysis.". Biochem. Soc. Trans. 31 (Pt 6): 1120–4. doi:10.1042/BST0311120. PMID 14641008.
- Holm C, Kirchgessner TG, Svenson KL, et al. (1988). "Hormone-sensitive lipase: sequence, expression, and chromosomal localization to 19 cent-q13.3.". Science 241 (4872): 1503–6. doi:10.1126/science.3420405. PMID 3420405.
- Levitt RC, Liu Z, Nouri N, et al. (1995). "Mapping of the gene for hormone sensitive lipase (LIPE) to chromosome 19q13.1→q13.2.". Cytogenet. Cell Genet. 69 (3-4): 211–4. doi:10.1159/000133966. PMID 7698015.
- Langin D, Laurell H, Holst LS, et al. (1993). "Gene organization and primary structure of human hormone-sensitive lipase: possible significance of a sequence homology with a lipase of Moraxella TA144, an antarctic bacterium.". Proc. Natl. Acad. Sci. U.S.A. 90 (11): 4897–901. doi:10.1073/pnas.90.11.4897. PMC 46620. PMID 8506334.
- Holst LS, Langin D, Mulder H, et al. (1996). "Molecular cloning, genomic organization, and expression of a testicular isoform of hormone-sensitive lipase.". Genomics 35 (3): 441–7. doi:10.1006/geno.1996.0383. PMID 8812477.
- Anthonsen MW, Rönnstrand L, Wernstedt C, et al. (1998). "Identification of novel phosphorylation sites in hormone-sensitive lipase that are phosphorylated in response to isoproterenol and govern activation properties in vitro.". J. Biol. Chem. 273 (1): 215–21. doi:10.1074/jbc.273.1.215. PMID 9417067.
- Shen WJ, Sridhar K, Bernlohr DA, Kraemer FB (1999). "Interaction of rat hormone-sensitive lipase with adipocyte lipid-binding protein.". Proc. Natl. Acad. Sci. U.S.A. 96 (10): 5528–32. doi:10.1073/pnas.96.10.5528. PMC 21893. PMID 10318917.
- Syu LJ, Saltiel AR (1999). "Lipotransin: a novel docking protein for hormone-sensitive lipase.". Mol. Cell 4 (1): 109–15. doi:10.1016/S1097-2765(00)80192-6. PMID 10445032.
- Shen WJ, Patel S, Hong R, Kraemer FB (2000). "Hormone-sensitive lipase functions as an oligomer.". Biochemistry 39 (9): 2392–8. doi:10.1021/bi992283h. PMID 10694408.
- Johnson WJ, Jang SY, Bernard DW (2001). "Hormone sensitive lipase mRNA in both monocyte and macrophage forms of the human THP-1 cell line.". Comp. Biochem. Physiol. B, Biochem. Mol. Biol. 126 (4): 543–52. doi:10.1016/S0305-0491(00)00220-0. PMID 11026666.
- Laurin NN, Wang SP, Mitchell GA (2001). "The hormone-sensitive lipase gene is transcribed from at least five alternative first exons in mouse adipose tissue.". Mamm. Genome 11 (11): 972–8. doi:10.1007/s003350010185. PMID 11063252.
- Greenberg AS, Shen WJ, Muliro K, et al. (2002). "Stimulation of lipolysis and hormone-sensitive lipase via the extracellular signal-regulated kinase pathway.". J. Biol. Chem. 276 (48): 45456–61. doi:10.1074/jbc.M104436200. PMID 11581251.
- Talmud PJ, Palmen J, Luan J, et al. (2002). "Variation in the promoter of the human hormone sensitive lipase gene shows gender specific effects on insulin and lipid levels: results from the Ely study.". Biochim. Biophys. Acta 1537 (3): 239–44. PMID 11731226.
- Kolehmainen M, Vidal H, Ohisalo JJ, et al. (2002). "Hormone sensitive lipase expression and adipose tissue metabolism show gender difference in obese subjects after weight loss.". Int. J. Obes. Relat. Metab. Disord. 26 (1): 6–16. doi:10.1038/sj.ijo.0801858. PMID 11791141.
- Smih F, Rouet P, Lucas S, et al. (2002). "Transcriptional regulation of adipocyte hormone-sensitive lipase by glucose.". Diabetes 51 (2): 293–300. doi:10.2337/diabetes.51.2.293. PMID 11812735.
- Mairal A, Melaine N, Laurell H, et al. (2002). "Characterization of a novel testicular form of human hormone-sensitive lipase.". Biochem. Biophys. Res. Commun. 291 (2): 286–90. doi:10.1006/bbrc.2002.6427. PMID 11846402.
- Ylitalo K, Nuotio I, Viikari J, et al. (2002). "C3, hormone-sensitive lipase, and peroxisome proliferator-activated receptor gamma expression in adipose tissue of familial combined hyperlipidemia patients.". Metab. Clin. Exp. 51 (5): 664–70. PMID 11979403.
External links[edit]
- Hormone-Sensitive Lipase at the US National Library of Medicine Medical Subject Headings (MeSH)
|
Hydrolase: esterases (EC 3.1)
|
|
| 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
|
|
| 3.1.2: Thioesterase |
- Palmitoyl protein thioesterase
- Ubiquitin carboxy-terminal hydrolase L1
|
|
| 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
|
|
| 3.1.4: Phosphodiesterase |
- Autotaxin
- Phospholipase
- Sphingomyelin phosphodiesterase
- PDE1
- PDE2
- PDE3
- PDE4A/PDE4B
- PDE5
- Lecithinase (Clostridium perfringens alpha toxin)
- Cyclic nucleotide phosphodiesterase
|
|
| 3.1.6: Sulfatase |
- arylsulfatase
- Arylsulfatase A
- Arylsulfatase B
- Arylsulfatase E
- Steroid sulfatase
- Galactosamine-6 sulfatase
- Iduronate-2-sulfatase
- N-acetylglucosamine-6-sulfatase
|
|
Nuclease (includes
deoxyribonuclease and
ribonuclease) |
| 3.1.11-16: Exonuclease |
| Exodeoxyribonuclease |
|
|
| Exoribonuclease |
|
|
|
| 3.1.21-31: Endonuclease |
| Endodeoxyribonuclease |
- Deoxyribonuclease I
- Deoxyribonuclease II
- Deoxyribonuclease IV
- Restriction enzyme
- UvrABC endonuclease
|
|
| Endoribonuclease |
- RNase III
- RNase H
- RNase P
- RNase A
- RNase T1
- RNA-induced silencing complex
|
|
| either deoxy- or ribo- |
- Aspergillus nuclease S1
- Micrococcal nuclease
|
|
|
|
- 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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UpToDate Contents
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English Journal
- Effect and mechanism of waterborne prolonged Zn exposure influencing hepatic lipid metabolism in javelin goby Synechogobius hasta.
- Huang C1, Luo Z1,2, Hogstrand C3, Chen F1, Shi X1, Chen QL1, Song YF1, Pan YX1.
- Journal of applied toxicology : JAT.J Appl Toxicol.2016 Jul;36(7):886-95. doi: 10.1002/jat.3261. Epub 2015 Nov 25.
- The present study was conducted to determine the effect and mechanism of waterborne Zn exposure influencing hepatic lipid deposition and metabolism in javelin goby Synechogobius hasta. S. hasta were exposed to four waterborne Zn concentrations (Zn 0.005 [control], 0.18, 0.36 and 0.55 mg l(-1) ,
- PMID 26602879
- Diabetic and dyslipidaemic morbidly obese exhibit more liver alterations compared with healthy morbidly obese.
- Pardina E1, Ferrer R2, Rossell J1, Baena-Fustegueras JA3, Lecube A4, Fort JM5, Caubet E5, González Ó5, Vilallonga R5, Vargas V6, Balibrea JM5, Peinado-Onsurbe J1.
- BBA clinical.BBA Clin.2016 Jan 8;5:54-65. doi: 10.1016/j.bbacli.2015.12.002. eCollection 2016.
- BACKGROUND & AIMS: To study the origin of fat excess in the livers of morbidly obese (MO) individuals, we analysed lipids and lipases in both plasma and liver and genes involved in lipid transport, or related with, in that organ.METHODS: Thirty-two MO patients were grouped according to the absen
- PMID 27051590
- Data on hepatic lipolysis, adipose triglyceride lipase, and hormone-sensitive lipase in fasted and non-fasted C57BL/6J female mice.
- Marvyn PM1, Mardian EB1, Bradley RM1, A Marks K1, Duncan RE1.
- Data in brief.Data Brief.2016 Mar 11;7:721-5. doi: 10.1016/j.dib.2016.03.033. eCollection 2016.
- Liver homogenates produced from fasted and non-fasted C57BL/6J female mice were assayed for total lipolytic activity measured as hydrolysis of [9,10-(3)H(N)]-triolein into [(3)H] free fatty acids (FFA). Liver homogenates were also used for immunoblotting to determine levels of the lipolytic enzymes
- PMID 27054184
Japanese Journal
- Increased Norepinephrine by Medium-Chain Triglyceride Attributable to Lipolysis in White and Brown Adipose Tissue of C57BL/6J Mice
- LIU Ying-hua,ZHANG Yong,XU Qing [他]
- Bioscience, Biotechnology, and Biochemistry 76(6), 1213-1218, 2012-06
- NAID 40019320159
★リンクテーブル★
[★]
- 英
- hormone-sensitive lipase, HSL
- 関
- ホルモン感受性トリアシルグリセロールリパーゼ
[★]
- 関
- acutely、alive、sensibility、sensitively、sensitivity、susceptibility、susceptible、tender