Summary: Hormone-sensitive lipase (HSL) N-terminus

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Hormone-sensitive lipase Edit Wikipedia article

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	â¢ triglyceride lipase activity â¢ protein binding â¢ protein kinase binding â¢ hormone-sensitive lipase activity â¢ acylglycerol lipase activity
Cellular component	â¢ extracellular space â¢ lipid particle â¢ cytosol â¢ caveola
Biological process	â¢ protein phosphorylation â¢ lipid metabolic process â¢ female pregnancy â¢ cholesterol metabolic process â¢ lipid catabolic process â¢ triglyceride catabolic process â¢ response to drug â¢ small molecule metabolic process â¢ diacylglycerol catabolic process
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 19:
42.91 â 42.93 Mb

Chr 7:
25.38 â 25.4 Mb

PubMed search

[1]

[2]

Hormone-sensitive lipase (HSL) N-terminus

Identifiers

Symbol

HSL_N

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]

[edit] Nomenclature

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.

[edit] Function

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]

[edit] Activation

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 G_s 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.

[edit] References

^ 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): 1110â7. 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): 4897â901. 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): 1585â94. 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): 1585â94. 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): 697â705. 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: 42â5. 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.

[edit] Further reading

Kraemer FB, Shen WJ (2003). "Hormone-sensitive lipase: control of intracellular tri-(di-)acylglycerol and cholesteryl ester hydrolysis.". J. Lipid Res. 43 (10): 1585â94. 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): 397â403. 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): 1120â4. 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): 1503â6. 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 19q13.1âq13.2.". Cytogenet. Cell Genet. 69 (3-4): 211â4. 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): 4897â901. 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): 441â7. doi:10.1006/geno.1996.0383. PMID 8812477.
Anthonsen MW, RÃ¶nnstrand 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): 215â21. 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): 5528â32. 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): 109â15. 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): 2392â8. 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): 543â52. 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): 972â8. 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): 45456â61. 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): 239â44. 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): 6â16. 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): 293â300. 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): 286â90. 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): 664â70. PMID 11979403.

[edit] External links

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

Lipase
- Bile salt-dependent
- Gastric/Lingual
- Pancreatic
- Lysosomal
- Hormone-sensitive
- Endothelial
- Hepatic
- Lipoprotein
- Monoacylglycerol
- Diacylglycerol

Phospholipase
- A1
- A2
- B

3.1.2: Thioesterase

3.1.3: Phosphatase

3.1.4: Phosphodiesterase

3.1.6: Sulfatase

Nuclease (includes
deoxyribonuclease and
ribonuclease)

3.1.11-16: Exonuclease

Exodeoxyribonuclease	RecBCD

Exoribonuclease	Oligonucleotidase

3.1.21-31: Endonuclease

Endodeoxyribonuclease	Deoxyribonuclease I Deoxyribonuclease II Deoxyribonuclease IV Restriction enzyme UvrABC endonuclease

Endoribonuclease	RNase III RNase H 1 2A 2B 2C RNase P RNase A 1 2 3 4/5 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
- 3
- 4
- 5
- 6
- 7
- 8
2.7.10
2.7.11-12
3.1
- - 3.1.3.48
- 2
- 3
- 4
  - 3.4.21
- 5
- 6
- 7
- 22
- 23
- 24
4.1
- 2
- 3
- 4
- 5
- 6
5.1
- 2
- 3
- 4
- 99
6.1-3
- 4
- 5-6

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Hormone-sensitive lipase (HSL) N-terminus Provide feedback

This family consists of several mammalian hormone-sensitive lipase (HSL) proteins ( EC:3.1.1.-). Hormone-sensitive lipase, a key enzyme in fatty acid mobilisation, overall energy homeostasis, and possibly steroidogenesis, is acutely controlled through reversible phosphorylation by catecholamines and insulin [1].

Literature references

Holm C, Kirchgessner TG, Svenson KL, Fredrikson G, Nilsson S, Miller CG, Shively JE, Heinzmann C, Sparkes RS, Mohandas T, et al.; , Science 1988;241:1503-1506.: Hormone-sensitive lipase: sequence, expression, and chromosomal localization to 19 cent-q13.3. PUBMED:3420405 EPMC:3420405

External database links

PANDIT:	PF06350
Pseudofam:	PF06350
SYSTERS:	HSL_N

This tab holds annotation information from the InterPro database.

InterPro entry IPR010468

This domain is found in several mammalian hormone-sensitive lipase (HSL) proteins. Hormone-sensitive lipase, a key enzyme in fatty acid mobilisation, overall energy homeostasis, and possibly steroidogenesis, is acutely controlled via reversible phosphorylation by catecholamines and insulin [PUBMED:3420405].

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Molecular function	lipase activity (GO:0016298)
Biological process	lipid catabolic process (GO:0016042)
Biological process	cholesterol metabolic process (GO:0008203)

Domain organisation

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Alignments

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RP15/RP35/RP55/RP75: Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
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meta: alignment generated by searching the metagenomics sequence database using the family HMM

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	Seed (6)	Full (166)	Representative proteomes				NCBI (151)	Meta (0)
	Seed (6)	Full (166)	RP15 (32)	RP35 (39)	RP55 (65)	RP75 (86)	NCBI (151)	Meta (0)
Jalview	View	View	View	View	View	View	View
HTML	View	View	View	View	View	View
PP/heatmap	₁	View	View	View	View	View
Pfam viewer	View	View

¹Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: available, not generated, — not available.

Format an alignment

	Seed (6)	Full (166)	Representative proteomes				NCBI (151)	Meta (0)
	Seed (6)	Full (166)	RP15 (32)	RP35 (39)	RP55 (65)	RP75 (86)	NCBI (151)	Meta (0)
Alignment:
Format:
Order:	Tree Alphabetical
Sequence:	Inserts lower case All upper case
Gaps:
Download/view:	Download View

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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

	Seed (6)	Full (166)	Representative proteomes				NCBI (151)	Meta (0)
	Seed (6)	Full (166)	RP15 (32)	RP35 (39)	RP55 (65)	RP75 (86)	NCBI (151)	Meta (0)
Raw Stockholm	Download	Download	Download	Download	Download	Download	Download
Gzipped	Download	Download	Download	Download	Download	Download	Download

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.

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Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

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Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation

Seed source:

Pfam-B_13329 (release 9.0)

Previous IDs:

HSL;

Type:

Family

Author:

Moxon SJ

Number in seed:

6

Number in full:

166

Average length of the domain:

251.30 aa

Average identity of full alignment:

43 %

Average coverage of the sequence by the domain:

37.71 %

HMM information

HMM build commands:

build method: hmmbuild -o /dev/null HMM SEED

search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq

Model details:

Parameter	Sequence	Domain
Gathering cut-off	25.0	25.0
Trusted cut-off	25.1	29.8
Noise cut-off	17.7	24.4

Model length:

313

Family (HMM) version:

7

Download:

download the raw HMM for this family

Species distribution

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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

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order
family
genus
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Unmapped species names

The tree is built by looking at each sequence in the full alignment for the family. We take the name of the species given by UniProt and try to map that to the full taxonomic tree from NCBI. In some cases, the name chosen by UniProt does not map to any node in the NCBI tree, perhaps because the chosen name is listed as a synonym or a misspelling in the NCBI taxonomy.

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Interactive tree

For all of the domain matches in a full alignment, we count the number that are found on all sequences in the alignment. This total is shown in the purple box.

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We use the NCBI species tree to group organisms according to their taxonomy and this forms the structure of the displayed tree. Note that in some cases the trees are too large (have too many nodes) to allow us to build an interactive tree, but in most cases you can still view the tree in a plain text, non-interactive representation. Those species which are represented in the seed alignment for this domain are highlighted.

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Archea	Eukaryota
Bacteria	Other sequences
Viruses	Unclassified
Viroids	Unclassified sequence

Family: HSL_N (PF06350)

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