View source for Biology:Lysosomal lipase

{{Short description|Mammalian protein found in Homo sapiens}}
{{infobox protein
|Name=lipase A, lysosomal acid, cholesterol esterase (Wolman disease)
|caption=
|image=
|width=
|HGNCid=6617
|Symbol=LIPA
|AltSymbols=
|EntrezGene=3988
|OMIM=278000
|RefSeq=NM_000235
|UniProt=P38571
|PDB=
|ECnumber=3.1.1.13
|Chromosome=10
|Arm=q
|Band=23.2
|LocusSupplementaryData=-23.3
}}
'''Lysosomal lipase''' is a form of [[Biology:Lipase|lipase]] which functions [[Biology:Intracellular|intracellular]]ly, in the [[Biology:Lysosome|lysosome]]s.
== Biochemical Significance ==
The primary function of lysosomal lipase is to hydrolyze lipids such as triglycerides and cholesterol.<ref>{{Cite journal|last1=Ding|first1=Hao-ran|last2=Wang|first2=Jing-lin|last3=Ren|first3=Hao-zhen|last4=Shi|first4=Xiao-lei|date=2018-12-12|title=Lipometabolism and Glycometabolism in Liver Diseases|journal=BioMed Research International|volume=2018|pages=1–7|doi=10.1155/2018/1287127|pmid=31205932|pmc=6530156|issn=2314-6133|doi-access=free}}</ref> These fats are transported and degraded into free fatty acids. Lysosomal lipases function optimally at an acidic pH which are complementary with the environment found in the lysosomal lumen.<ref name=":12">{{Cite journal|last=Cuervo|first=Ana Maria|date=June 2013|title=Preventing lysosomal fat digestion|url=https://www.nature.com/articles/ncb2778|journal=Nature Cell Biology|volume=15|issue=6|pages=565–567|doi=10.1038/ncb2778|pmid=23728462|s2cid=11119477 |via=Gale Academic OneFile}}</ref> These enzymes were believed to only hydrolyze the lipids found in organelle membranes and extracellular lipids. However, recent studies suggest that lysosomal lipases also play a significant role in the degradation of cytosolic lipids, a characteristic that was previously limited to neutral lipases.<ref name=":12" /> The ability of the lysosome to degrade a diverse set of cargo is attributed to the lysosomal lipase and other soluble hydrolases. These enzymes include sulphatases, phosphatases, peptidases, glycosidases, and nucleases.<ref name=":22">{{Cite journal|last1=Settembre|first1=Carmine|last2=Fraldi|first2=Alessandro|last3=Medina|first3=Diego L.|last4=Ballabio|first4=Andrea|date=2013-04-23|title=Signals from the lysosome: a control centre for cellular clearance and energy metabolism|url= |journal=Nature Reviews Molecular Cell Biology|volume=14|issue=5|pages=283–296|doi=10.1038/nrm3565|pmid=23609508|issn=1471-0072|pmc=4387238}}</ref>

The biochemical role of these enzymes are observed in various pathways, specifically in lipid catabolism. At the intracellular level, the byproducts released by the lysosomal lipase are recycled for membrane assembly and energy production.<ref name=":02">{{Cite journal|last=Zhang|first=Hanrui|date=June 2018|title=Lysosomal acid lipase and lipid metabolism: new mechanisms, new questions, and new therapies|journal=Current Opinion in Lipidology|volume=29|issue=3|pages=218–223|doi=10.1097/MOL.0000000000000507|issn=0957-9672|pmc=6215475|pmid=29547398}}</ref> In addition, these enzymes participate in the production of specific fatty acids necessary for the metabolic reprogramming of CD8+ memory T cells, macrophage alternative activation, and lipid mediator synthesis.<ref name=":02" /> As observed, the degradation of these lipids are essential to maintain homeostasis within the body. The absence or decreased activity of this enzyme could lead to various metabolic disorders.<ref name=":22" />

==Clinical significance==
A deficiency associated with [[Medicine:Lysosomal acid lipase deficiency|lysosomal acid lipase deficiency]], Wolman disease, and cholesteryl ester storage disease.

[[Chemistry:Chlorpromazine|Chlorpromazine]] is an inhibitor of lysosomal lipase.<ref name="pmid4004781">{{cite journal |vauthors=Sauro VS, Klamut HJ, Lin CH, Strickland KP |title=Lysosomal triacylglycerol lipase activity in L6 myoblasts and its changes on differentiation |journal=Biochem. J. |volume=227 |issue=2 |pages=583–9 |year=1985 |doi=10.1042/bj2270583 |pmid=4004781 |pmc=1144878}}</ref>

A genome wide survey suggests that lysosomal lipase A (located at chromosome 10q23.31) is associated with coronary artery disease in humans.<ref name="Wild2011">{{cite journal |vauthors=Wild PS, Zeller T, Schillert A, etal |title=A Genome-wide Association Study Identifies LIPA as a Susceptibility Gene for Coronary Artery Disease |journal=Circ Cardiovasc Genet |date=May 2011 |pmid=21606135 |doi=10.1161/CIRCGENETICS.110.958728 |url=http://circgenetics.ahajournals.org/cgi/pmidlookup?view=long&pmid=21606135 |volume=4 |issue=4 |pages=403–12 |pmc=3157552 |access-date=2011-08-09 |archive-url=https://archive.today/20130223090541/http://circgenetics.ahajournals.org/cgi/pmidlookup?view=long&pmid=21606135 |archive-date=2013-02-23 |url-status=dead }}</ref>

==References==
{{reflist}}

==External links==
* {{MeshName|lysosomal+acid+lipase,+human}}

{{Esterases}}



{{Sourceattribution|Lysosomal lipase|1}}