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Genetics Home Reference: your guide to understanding genetic conditions
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LCAT

Reviewed August 2013

What is the official name of the LCAT gene?

The official name of this gene is “lecithin-cholesterol acyltransferase.”

LCAT is the gene's official symbol. The LCAT gene is also known by other names, listed below.

What is the normal function of the LCAT gene?

The LCAT gene provides instructions for making an enzyme called lecithin-cholesterol acyltransferase (LCAT). This enzyme plays a role in removing cholesterol from the blood and tissues. Cholesterol is a waxy, fat-like substance that is produced in the body and obtained from foods that come from animals (particularly egg yolks, meat, poultry, fish, and dairy products). The body needs this substance to build cell membranes, make certain hormones, and produce compounds that aid in fat digestion. Too much cholesterol, however, increases a person's risk of developing heart disease, and can also lead to buildup of cholesterol in other tissues.

The LCAT enzyme helps transport cholesterol out of the blood and tissues by a process called cholesterol esterification. This process results in a form of cholesterol that is more efficiently carried by molecules called lipoproteins, which transport the cholesterol to the liver. Once in the liver, the cholesterol is redistributed to other tissues or removed from the body. The enzyme has two major functions, called alpha- and beta-LCAT activity. Alpha-LCAT activity helps attach cholesterol to a lipoprotein called high-density lipoprotein (HDL). Beta-LCAT activity helps attach cholesterol to other lipoproteins called very low-density lipoprotein (VLDL) and low-density lipoprotein (LDL).

How are changes in the LCAT gene related to health conditions?

complete LCAT deficiency - caused by mutations in the LCAT gene

More than 70 mutations in the LCAT gene have been identified in people with complete LCAT deficiency, a disorder that primarily causes corneal clouding and kidney problems. Individuals with complete LCAT deficiency have mutations in both copies of the LCAT gene in each cell. Most of these mutations change single amino acids in the LCAT enzyme sequence. Others add or delete small amounts of genetic material in the LCAT gene. The mutations either prevent the production of LCAT or impair both alpha-LCAT and beta-LCAT activity, reducing the enzyme's ability to attach cholesterol to lipoproteins. Impairment of this mechanism for reducing cholesterol in the body leads to cholesterol deposits in the corneas, kidneys, and other tissues and organs. These deposits cause the signs and symptoms of complete LCAT deficiency.

fish-eye disease - caused by mutations in the LCAT gene

At least 18 mutations in the LCAT gene have been identified in people with fish-eye disease, also called partial LCAT deficiency. This disorder causes clouding of the clear covering of the eyes (corneas). Individuals with fish-eye disease have mutations in both copies of the LCAT gene in each cell. Most of these mutations change single protein building blocks (amino acids) in the LCAT sequence. The mutations impair alpha-LCAT activity, reducing the enzyme's ability to attach cholesterol to HDL. Impairment of this mechanism for reducing cholesterol in the body leads to cholesterol deposits in the corneas that gradually cause them to become cloudy.

other disorders - increased risk from variations of the LCAT gene

People with one LCAT gene mutation in each cell may have an increased risk of atherosclerosis, which is an accumulation of cholesterol-rich fatty deposits and scar-like tissue in the lining of the arteries that can impede blood flow and lead to heart attacks, strokes, and other health problems. A single LCAT gene mutation likely reduces alpha-LCAT activity and binding of cholesterol to HDL, leading to less efficient transport of cholesterol from the blood and resulting in the development of atherosclerosis.

Atherosclerosis also occurs in some people with fish-eye disease or complete LCAT deficiency. However, because atherosclerosis is very common in the general population and both fish-eye disease and complete LCAT deficiency are very rare, it is difficult to determine whether affected individuals are at increased risk of atherosclerosis.

Where is the LCAT gene located?

Cytogenetic Location: 16q22.1

Molecular Location on chromosome 16: base pairs 67,939,883 to 67,944,111

The LCAT gene is located on the long (q) arm of chromosome 16 at position 22.1.

The LCAT gene is located on the long (q) arm of chromosome 16 at position 22.1.

More precisely, the LCAT gene is located from base pair 67,939,883 to base pair 67,944,111 on chromosome 16.

See How do geneticists indicate the location of a gene? (http://ghr.nlm.nih.gov/handbook/howgeneswork/genelocation) in the Handbook.

Where can I find additional information about LCAT?

You and your healthcare professional may find the following resources about LCAT helpful.

You may also be interested in these resources, which are designed for genetics professionals and researchers.

What other names do people use for the LCAT gene or gene products?

  • LCAT_HUMAN
  • phosphatidylcholine-sterol acyltransferase
  • phosphatidylcholine-sterol acyltransferase precursor
  • phospholipid-cholesterol acyltransferase

See How are genetic conditions and genes named? (http://ghr.nlm.nih.gov/handbook/mutationsanddisorders/naming) in the Handbook.

What glossary definitions help with understanding LCAT?

acids ; arteries ; atherosclerosis ; cell ; cholesterol ; deficiency ; digestion ; egg ; enzyme ; gene ; HDL ; kidney ; LDL ; lipoprotein ; mutation ; phospholipid ; population ; precursor ; protein ; tissue ; VLDL

You may find definitions for these and many other terms in the Genetics Home Reference Glossary (http://ghr.nlm.nih.gov/glossary).

References

  • Calabresi L, Pisciotta L, Costantin A, Frigerio I, Eberini I, Alessandrini P, Arca M, Bon GB, Boscutti G, Busnach G, Frascà G, Gesualdo L, Gigante M, Lupattelli G, Montali A, Pizzolitto S, Rabbone I, Rolleri M, Ruotolo G, Sampietro T, Sessa A, Vaudo G, Cantafora A, Veglia F, Calandra S, Bertolini S, Franceschini G. The molecular basis of lecithin:cholesterol acyltransferase deficiency syndromes: a comprehensive study of molecular and biochemical findings in 13 unrelated Italian families. Arterioscler Thromb Vasc Biol. 2005 Sep;25(9):1972-8. Epub 2005 Jun 30. (http://www.ncbi.nlm.nih.gov/pubmed/15994445?dopt=Abstract)
  • Duivenvoorden R, Holleboom AG, van den Bogaard B, Nederveen AJ, de Groot E, Hutten BA, Schimmel AW, Hovingh GK, Kastelein JJ, Kuivenhoven JA, Stroes ES. Carriers of lecithin cholesterol acyltransferase gene mutations have accelerated atherogenesis as assessed by carotid 3.0-T magnetic resonance imaging [corrected]. J Am Coll Cardiol. 2011 Dec 6;58(24):2481-7. doi: 10.1016/j.jacc.2010.11.092. Erratum in: J Am Coll Cardiol. 2012 Jan 10;59(2):196. (http://www.ncbi.nlm.nih.gov/pubmed/22133847?dopt=Abstract)
  • OMIM: LECITHIN:CHOLESTEROL ACYLTRANSFERASE (http://omim.org/entry/606967)
  • NCBI Gene (http://www.ncbi.nlm.nih.gov/gene/3931)
  • Reshetnyak Y, Tchedre KT, Nair MP, Pritchard PH, Lacko AG. Structural differences between wild-type and fish eye disease mutant of lecithin:cholesterol acyltransferase. J Biomol Struct Dyn. 2006 Aug;24(1):75-82. (http://www.ncbi.nlm.nih.gov/pubmed/16780378?dopt=Abstract)
  • Roshan B, Ganda OP, Desilva R, Ganim RB, Ward E, Haessler SD, Polisecki EY, Asztalos BF, Schaefer EJ. Homozygous lecithin:cholesterol acyltransferase (LCAT) deficiency due to a new loss of function mutation and review of the literature. J Clin Lipidol. 2011 Nov-Dec;5(6):493-9. doi: 10.1016/j.jacl.2011.07.002. Epub 2011 Aug 23. Review. (http://www.ncbi.nlm.nih.gov/pubmed/22108153?dopt=Abstract)
  • Savel J, Lafitte M, Pucheu Y, Pradeau V, Tabarin A, Couffinhal T. Very low levels of HDL cholesterol and atherosclerosis, a variable relationship--a review of LCAT deficiency. Vasc Health Risk Manag. 2012;8:357-61. doi: 10.2147/VHRM.S29985. Epub 2012 Jun 5. Review. (http://www.ncbi.nlm.nih.gov/pubmed/22701329?dopt=Abstract)
  • van den Bogaard B, Holleboom AG, Duivenvoorden R, Hutten BA, Kastelein JJ, Hovingh GK, Kuivenhoven JA, Stroes ES, van den Born BJ. Patients with low HDL-cholesterol caused by mutations in LCAT have increased arterial stiffness. Atherosclerosis. 2012 Dec;225(2):481-5. doi: 10.1016/j.atherosclerosis.2012.09.022. Epub 2012 Sep 27. (http://www.ncbi.nlm.nih.gov/pubmed/23078883?dopt=Abstract)

 

The resources on this site should not be used as a substitute for professional medical care or advice. Users seeking information about a personal genetic disease, syndrome, or condition should consult with a qualified healthcare professional. See How can I find a genetics professional in my area? (http://ghr.nlm.nih.gov/handbook/consult/findingprofessional) in the Handbook.

 
Reviewed: August 2013
Published: January 27, 2015