Ceramide synthase 2: Difference between revisions
new page |
(No difference)
|
Revision as of 02:10, 17 February 2014
Ceramide synthase 2 | |||||||
---|---|---|---|---|---|---|---|
Identifiers | |||||||
Symbol | CERS2 | ||||||
Alt. symbols | LASS2, TMSG1, TRH3, LAGIHs-2 | ||||||
NCBI gene | 29956 | ||||||
HGNC | 14076 | ||||||
OMIM | 606920 | ||||||
Orthologs | 29956 | ||||||
RefSeq | NP_071358.1 | ||||||
UniProt | Q96G23 | ||||||
Other data | |||||||
Locus | Chr. 1 q21.3 | ||||||
|
Ceramide synthase 2, also known as LAG1 longevity assurance homolog 2 or Tumor metastasis-suppressor gene 1 protein, is a ceramide synthase that catalyses the synthesis of very long acyl chain ceramides, including C20 and C26 ceramides. It is the most ubiquitously expressed of all CerS and has the broadest distribution in the human body.[1]
CerS2 was first identified in 2001.[2] It contains the conserved TLC domain and Hox-like domain common to almost all CerS.[3]
Distribution
CerS2 is much more widely distributed than Ceramide synthase 1 (CerS1) and is found in at least 12 tissues in the human body, with high expression in the kidney and liver, and moderate expression in the brain and other organs. In the mouse brain, CerS2 is mainly expressed white matter tracts, specifically in oligodendrocytes and Schwann cells. [3][4]
Function
Expression of CerS2 is also transiently increased during periods of active myelination, suggesting that it is important for the synthesis of myelin sphingolipids.[4]
The CerS2 gene is compact in size and is located in a chromosomal region that are replicated early in the cell cycle.[3] CerS2 activity is regulated by sphingosine-1-phosphate (S1P) via two sphingosine-1-phosphate receptor-like residues on CerS2 that operate independently.[3]
Knockdown of CerS2 induces the autophagy and activation of the unfolded protein response (UPR).[3]
CerS2 knockout mice showed no decreased in overall ceramide level, but elevated levels of sphinganine. These mice developed severe liver disease, but there was no change in the kidneys.[5]
Pathological Significance
CerS2 levels are significantly elevated in breast cancer tissue compared to normal tissue, along with increased levels of ceramide synthase 6 (CerS6).[3]
CerS2 was also implicated in the control of body weight. The administration of leptin to rats induced a decrease in CerS2 was observed in white adipose tissue.[3]
References
- ^ Stiban J, Tidhar R, Futerman AH (2010). "Ceramide synthases: roles in cell physiology and signaling". Advances in Experimental Medicine and Biology. 688: 60–71. PMID 20919646.
{{cite journal}}
:|access-date=
requires|url=
(help)CS1 maint: multiple names: authors list (link) - ^ Pan H, Qin WX, Huo KK; et al. (2001). "Cloning, mapping, and characterization of a human homologue of the yeast longevity assurance gene LAG1". Genomics. 77 (1–2): 58–64. doi:10.1006/geno.2001.6614. PMID 11543633.
{{cite journal}}
:|access-date=
requires|url=
(help); Explicit use of et al. in:|author=
(help); Unknown parameter|month=
ignored (help)CS1 maint: multiple names: authors list (link) - ^ a b c d e f g Levy, Michal; Futerman, Anthony H. (2010). "Mammalian ceramide synthases". IUBMB Life: NA–NA. doi:10.1002/iub.319. ISSN 1521-6543.
- ^ a b Becker I, Wang-Eckhardt L, Yaghootfam A, Gieselmann V, Eckhardt M (2008). "Differential expression of (dihydro)ceramide synthases in mouse brain: oligodendrocyte-specific expression of CerS2/Lass2". Histochemistry and Cell Biology. 129 (2): 233–41. doi:10.1007/s00418-007-0344-0. PMID 17901973.
{{cite journal}}
:|access-date=
requires|url=
(help); Unknown parameter|month=
ignored (help)CS1 maint: multiple names: authors list (link) - ^ Pewzner-Jung, Y.; Brenner, O.; Braun, S.; Laviad, E. L.; Ben-Dor, S.; Feldmesser, E.; Horn-Saban, S.; Amann-Zalcenstein, D.; Raanan, C.; Berkutzki, T.; Erez-Roman, R.; Ben-David, O.; Levy, M.; Holzman, D.; Park, H.; Nyska, A.; Merrill, A. H.; Futerman, A. H. (2010). "A Critical Role for Ceramide Synthase 2 in Liver Homeostasis: II. INSIGHTS INTO MOLECULAR CHANGES LEADING TO HEPATOPATHY". Journal of Biological Chemistry. 285 (14): 10911–10923. doi:10.1074/jbc.M109.077610. ISSN 0021-9258.
{{cite journal}}
: CS1 maint: unflagged free DOI (link)