ABHD6: Difference between revisions

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'''alpha/beta-Hydrolase domain containing 6''' ('''ABHD6'''), also known as '''monoacylglycerol lipase ABHD6''' or '''2-arachidonoylglycerol hydrolase''' is an enzyme that in humans is encoded by the ABHD6 [[gene]].
'''alpha/beta-Hydrolase domain containing 6''' ('''ABHD6'''), also known as '''monoacylglycerol lipase ABHD6''' or '''2-arachidonoylglycerol hydrolase''' is an enzyme that in humans is encoded by the ABHD6 [[gene]].


==Function==  
== Function ==  
ABHD6 is a serine hydrolyzing enzyme that possesses typical [[Alpha/beta hydrolase fold|α/β-hydrolase]] family domains. ABHD6 was first studied because of its over-expression in certain forms of tumours.<ref name="pmid18360779">{{cite journal | vauthors = Li F, Fei X, Xu J, Ji C | title = An unannotated alpha/beta hydrolase superfamily member, ABHD6 differentially expressed among cancer cell lines | journal = Mol. Biol. Rep. | volume = 36 | issue = 4 | pages = 691–6 |date=April 2009 | pmid = 18360779 | doi = 10.1007/s11033-008-9230-7 }}</ref>
ABHD6 is a serine hydrolyzing enzyme that possesses typical [[Alpha/beta hydrolase fold|α/β-hydrolase]] family domains. ABHD6 was first studied because of its over-expression in certain forms of [[Neoplasm|tumours]].<ref name="pmid18360779">{{cite journal | vauthors = Li F, Fei X, Xu J, Ji C | title = An unannotated alpha/beta hydrolase superfamily member, ABHD6 differentially expressed among cancer cell lines | journal = Molecular Biology Reports | volume = 36 | issue = 4 | pages = 691–6 | date = April 2009 | pmid = 18360779 | doi = 10.1007/s11033-008-9230-7 }}</ref>


ABHD6 has been linked to regulation of the [[endocannabinoid system]] as it controls the accumulation of [[2-arachidonoylglycerol]] (2-AG) at the [[cannabinoid receptor]]s.<ref name="pmid20657592">{{cite journal | vauthors = Marrs WR, Blankman JL, Horne EA, Thomazeau A, Lin YH, Coy J, Bodor AL, Muccioli GG, Hu SS, Woodruff G, Fung S, Lafourcade M, Alexander JP, Long JZ, Li W, Xu C, Möller T, Mackie K, Manzoni OJ, Cravatt BF, Stella N | title = The serine hydrolase ABHD6 controls the accumulation and efficacy of 2-AG at cannabinoid receptors | journal = Nat. Neurosci. | volume = 13 | issue = 8 | pages = 951–7 |date=August 2010 | pmid = 20657592 | pmc = 2970523 | doi = 10.1038/nn.2601 }}</ref>
ABHD6 has been linked to regulation of the [[endocannabinoid system]] as it controls the accumulation of [[2-arachidonoylglycerol]] (2-AG) at the [[cannabinoid receptor]]s.<ref name="pmid20657592">{{cite journal | vauthors = Marrs WR, Blankman JL, Horne EA, Thomazeau A, Lin YH, Coy J, Bodor AL, Muccioli GG, Hu SS, Woodruff G, Fung S, Lafourcade M, Alexander JP, Long JZ, Li W, Xu C, Möller T, Mackie K, Manzoni OJ, Cravatt BF, Stella N | title = The serine hydrolase ABHD6 controls the accumulation and efficacy of 2-AG at cannabinoid receptors | journal = Nature Neuroscience | volume = 13 | issue = 8 | pages = 951–7 | date = August 2010 | pmid = 20657592 | pmc = 2970523 | doi = 10.1038/nn.2601 }}</ref>


ABHD6 accounts for about 4% of 2-AG brain [[hydrolysis]].<ref name="ScholarlyEditions2012">{{cite book|title=Cannabinoid Receptors—Advances in Research and Application: 2012 Edition: ScholarlyBrief|url=https://books.google.com/books?id=QZqtIuUdJnQC&pg=PA68|date=26 December 2012|publisher=ScholarlyEditions|isbn=978-1-4816-0672-1|pages=68–}}</ref> Together, [[monoacylglycerol lipase]] (MAGL), [[ABHD12]], and ABHD6 control 99% of 2-AG signalling in the brain.<ref name="ScholarlyEditions2012" /><ref name="pmid21418147">{{cite journal | vauthors = Savinainen JR, Saario SM, Laitinen JT | title = The serine hydrolases MAGL, ABHD6 and ABHD12 as guardians of 2-arachidonoylglycerol signalling through cannabinoid receptors | journal = Acta Physiol (Oxf) | volume = 204 | issue = 2 | pages = 267–76 |date=February 2012 | pmid = 21418147 | pmc = 3320662 | doi = 10.1111/j.1748-1716.2011.02280.x }}</ref>
ABHD6 accounts for about 4% of 2-AG brain [[hydrolysis]].<ref name="ScholarlyEditions2012">{{cite book|title=Cannabinoid Receptors—Advances in Research and Application: 2012 Edition: ScholarlyBrief|url=https://books.google.com/books?id=QZqtIuUdJnQC&pg=PA68|date=26 December 2012|publisher=ScholarlyEditions|isbn=978-1-4816-0672-1|pages=68–}}</ref> Together, [[monoacylglycerol lipase]] (MAGL), [[ABHD12]], and ABHD6 control about 99% of 2-AG signalling in the brain,<ref name="ScholarlyEditions2012" /><ref name="pmid21418147">{{cite journal | vauthors = Savinainen JR, Saario SM, Laitinen JT | title = The serine hydrolases MAGL, ABHD6 and ABHD12 as guardians of 2-arachidonoylglycerol signalling through cannabinoid receptors | journal = Acta Physiologica | volume = 204 | issue = 2 | pages = 267–76 | date = February 2012 | pmid = 21418147 | pmc = 3320662 | doi = 10.1111/j.1748-1716.2011.02280.x }}</ref> and each enzyme exhibits a distinct [[Subcellular localization|subcellular]] distribution, suggesting that they regulate distinct pools of 2-AG in the [[nervous system]].<ref>{{cite journal | vauthors = Blankman JL, Simon GM, Cravatt BF | title = A comprehensive profile of brain enzymes that hydrolyze the endocannabinoid 2-arachidonoylglycerol | journal = Chemistry & Biology | volume = 14 | issue = 12 | pages = 1347–56 | date = December 2007 | pmid = 18096503 | pmc = 2692834 | doi = 10.1016/j.chembiol.2007.11.006 }}</ref>


==See also==
== See also ==
* [[Fatty acid amide hydrolase]]
* [[Fatty acid amide hydrolase]]


==References==
== References ==
{{Reflist|2}}
{{Reflist|2}}


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{{Cannabinoidergics}}
{{Cannabinoidergics}}


==External links==
== External links ==
* {{UCSC gene info|ABHD6}}
* {{UCSC gene info|ABHD6}}


{{gene-3-stub}}
{{gene-3-stub}}

Latest revision as of 05:06, 1 July 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

alpha/beta-Hydrolase domain containing 6 (ABHD6), also known as monoacylglycerol lipase ABHD6 or 2-arachidonoylglycerol hydrolase is an enzyme that in humans is encoded by the ABHD6 gene.

Function

ABHD6 is a serine hydrolyzing enzyme that possesses typical α/β-hydrolase family domains. ABHD6 was first studied because of its over-expression in certain forms of tumours.[1]

ABHD6 has been linked to regulation of the endocannabinoid system as it controls the accumulation of 2-arachidonoylglycerol (2-AG) at the cannabinoid receptors.[2]

ABHD6 accounts for about 4% of 2-AG brain hydrolysis.[3] Together, monoacylglycerol lipase (MAGL), ABHD12, and ABHD6 control about 99% of 2-AG signalling in the brain,[3][4] and each enzyme exhibits a distinct subcellular distribution, suggesting that they regulate distinct pools of 2-AG in the nervous system.[5]

See also

References

  1. Li F, Fei X, Xu J, Ji C (April 2009). "An unannotated alpha/beta hydrolase superfamily member, ABHD6 differentially expressed among cancer cell lines". Molecular Biology Reports. 36 (4): 691–6. doi:10.1007/s11033-008-9230-7. PMID 18360779.
  2. Marrs WR, Blankman JL, Horne EA, Thomazeau A, Lin YH, Coy J, Bodor AL, Muccioli GG, Hu SS, Woodruff G, Fung S, Lafourcade M, Alexander JP, Long JZ, Li W, Xu C, Möller T, Mackie K, Manzoni OJ, Cravatt BF, Stella N (August 2010). "The serine hydrolase ABHD6 controls the accumulation and efficacy of 2-AG at cannabinoid receptors". Nature Neuroscience. 13 (8): 951–7. doi:10.1038/nn.2601. PMC 2970523. PMID 20657592.
  3. 3.0 3.1 Cannabinoid Receptors—Advances in Research and Application: 2012 Edition: ScholarlyBrief. ScholarlyEditions. 26 December 2012. pp. 68–. ISBN 978-1-4816-0672-1.
  4. Savinainen JR, Saario SM, Laitinen JT (February 2012). "The serine hydrolases MAGL, ABHD6 and ABHD12 as guardians of 2-arachidonoylglycerol signalling through cannabinoid receptors". Acta Physiologica. 204 (2): 267–76. doi:10.1111/j.1748-1716.2011.02280.x. PMC 3320662. PMID 21418147.
  5. Blankman JL, Simon GM, Cravatt BF (December 2007). "A comprehensive profile of brain enzymes that hydrolyze the endocannabinoid 2-arachidonoylglycerol". Chemistry & Biology. 14 (12): 1347–56. doi:10.1016/j.chembiol.2007.11.006. PMC 2692834. PMID 18096503.

External links