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0  structures 300  species 0  interactions 528  sequences 18  architectures

Family: HSL_N (PF06350)

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

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This is the Wikipedia entry entitled "Hormone-sensitive lipase". More...

Hormone-sensitive lipase Edit Wikipedia article

AliasesLIPE, AOMS4, FPLD6, HSL, LHS, lipase E, hormone sensitive type
External IDsOMIM: 151750 MGI: 96790 HomoloGene: 3912 GeneCards: LIPE
Gene location (Human)
Chromosome 19 (human)
Chr.Chromosome 19 (human)[1]
Chromosome 19 (human)
Genomic location for LIPE
Genomic location for LIPE
Band19q13.2Start42,401,514 bp[1]
End42,427,388 bp[1]
RNA expression pattern
PBB GE LIPE 208186 s at fs.png

PBB GE LIPE 213855 s at fs.png
More reference expression data
RefSeq (mRNA)



RefSeq (protein)



Location (UCSC)Chr 19: 42.4 – 42.43 MbChr 7: 25.38 – 25.4 Mb
PubMed search[3][4]
View/Edit HumanView/Edit Mouse
Hormone-sensitive lipase (HSL) N-terminus

Hormone-sensitive lipase (EC, HSL), also previously known as cholesteryl ester hydrolase (CEH),[5] sometimes referred to as triacylglycerol lipase, is an enzyme that, in humans, is encoded by the LIPE gene.[6]

HSL is an intracellular neutral lipase that is capable of hydrolyzing a variety of esters.[7] 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.[8]


During fasting-state the increased free fatty acid secretion by adipocyte cells was attributed to the hormone epinephrine, hence the name "hormone-sensitive lipase".[9] Other catecholamines and adrenocorticotropic hormone (ACTH) can also stimulate such responses. Such enzymatic action plays a key role in providing major source of energy for most cells.


The main function of hormone-sensitive lipase is to mobilize the stored fats. Mobilization and Cellular Uptake of Stored Fats (with Animation) HSL functions to hydrolyze either a fatty acid from a triacylglycerol molecule, freeing a fatty acid and diglyceride, or a fatty acid from a diacylglycerol molecule, freeing a fatty acid and monoglyceride. Another enzyme found in adipose tissue, Adipose Triglyceride Lipase (ATGL), has a higher affinity for triglycerides than HSL, and ATGL predominantly acts as the enzyme for triglyceride hydrolysis in the adipocyte. HSL 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.[10][11]

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 cholesteryl esters for use in the production of steroids[12] and cholesterol efflux.[13] Activity of HSL is important in preventing or ameliorating the generation of foam cells in atherosclerosis.[13]


It may be activated by two mechanisms.[14]


  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000079435 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000003123 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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.
  6. ^ 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.
  7. ^ 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.
  8. ^ "Entrez Gene: LIPE lipase, hormone-sensitive".
  9. ^ 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.
  10. ^ 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.
  11. ^ de Meijer J (1998-05-01). "Hormone sensitive lipase: structure, function and regulation" (PDF). Retrieved 2009-02-04. Cite journal requires |journal= (help)
  12. ^ Kraemer FB (February 2007). "Adrenal cholesterol utilization". Mol. Cell. Endocrinol. 265-266: 42–5. doi:10.1016/j.mce.2006.12.001. PMID 17208360.
  13. ^ a b Ouimet M, Marcel YL (February 2012). "Regulation of Lipid Droplet Cholesterol Efflux From Macrophage Foam Cells". Arterioscler. Thromb. Vasc. Biol. 32: 575–581. doi:10.1161/ATVBAHA.111.240705. PMID 22207731.
  14. ^ Cox, Michael; Nelson, David R.; Lehninger, Albert L (2005). Lehninger principles of biochemistry. San Francisco: W.H. Freeman. ISBN 0-7167-4339-6.

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This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

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

  1. 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

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].

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Seed source: Pfam-B_13329 (release 9.0)
Previous IDs: HSL;
Type: Family
Sequence Ontology: SO:0100021
Author: Moxon SJ
Number in seed: 27
Number in full: 528
Average length of the domain: 270.10 aa
Average identity of full alignment: 36 %
Average coverage of the sequence by the domain: 36.56 %

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build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 47079205 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 25.0 25.0
Trusted cut-off 26.3 27.0
Noise cut-off 24.9 24.6
Model length: 306
Family (HMM) version: 13
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