Biology:AGPAT2
From HandWiki
Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
1-acyl-sn-glycerol-3-phosphate acyltransferase beta is an enzyme that in humans is encoded by the AGPAT2 gene.[1][2][3]
Function
This gene encodes a member of the 1-acylglycerol-3-phosphate O-acyltransferase family. The protein is located within the endoplasmic reticulum membrane and converts lysophosphatidic acid to phosphatidic acid, the second step in de novo phospholipid biosynthesis. Mutations in this gene have been associated with congenital generalized lipodystrophy, a disease characterized by a near absence of adipose tissue and severe insulin resistance. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.[3]
References
- ↑ "Human lysophosphatidic acid acyltransferase. cDNA cloning, expression, and localization to chromosome 9q34.3". The Journal of Biological Chemistry 272 (32): 20299–305. Aug 1997. doi:10.1074/jbc.272.32.20299. PMID 9242711.
- ↑ "Cloning and expression of two human lysophosphatidic acid acyltransferase cDNAs that enhance cytokine-induced signaling responses in cells". DNA and Cell Biology 16 (6): 691–701. Jun 1997. doi:10.1089/dna.1997.16.691. PMID 9212163.
- ↑ 3.0 3.1 "Entrez Gene: AGPAT2 1-acylglycerol-3-phosphate O-acyltransferase 2 (lysophosphatidic acid acyltransferase, beta)". https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=10555.
External links
- Human AGPAT2 genome location and AGPAT2 gene details page in the UCSC Genome Browser.
Further reading
- "Acquired and inherited lipodystrophies". The New England Journal of Medicine 350 (12): 1220–34. Mar 2004. doi:10.1056/NEJMra025261. PMID 15028826.
- "A human cDNA sequence with homology to non-mammalian lysophosphatidic acid acyltransferases". The Biochemical Journal 326 (2): 455–61. Sep 1997. doi:10.1042/bj3260455. PMID 9291118.
- "Characterization of a human lysophosphatidic acid acyltransferase that is encoded by a gene located in the class III region of the human major histocompatibility complex". The Journal of Biological Chemistry 273 (7): 4096–105. Feb 1998. doi:10.1074/jbc.273.7.4096. PMID 9461603.
- "A gene for congenital generalized lipodystrophy maps to human chromosome 9q34". The Journal of Clinical Endocrinology and Metabolism 84 (9): 3390–4. Sep 1999. doi:10.1210/jcem.84.9.6103. PMID 10487716.
- "AGPAT2 is mutated in congenital generalized lipodystrophy linked to chromosome 9q34". Nature Genetics 31 (1): 21–3. May 2002. doi:10.1038/ng880. PMID 11967537.
- "Phenotypic heterogeneity in body fat distribution in patients with congenital generalized lipodystrophy caused by mutations in the AGPAT2 or seipin genes". The Journal of Clinical Endocrinology and Metabolism 88 (11): 5433–7. Nov 2003. doi:10.1210/jc.2003-030835. PMID 14602785.
- "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation". Nature Biotechnology 22 (6): 707–16. Jun 2004. doi:10.1038/nbt971. PMID 15146197.
- "Mutations in Gng3lg and AGPAT2 in Berardinelli-Seip congenital lipodystrophy and Brunzell syndrome: phenotype variability suggests important modifier effects". The Journal of Clinical Endocrinology and Metabolism 89 (6): 2916–22. Jun 2004. doi:10.1210/jc.2003-030485. PMID 15181077.
- "Enzymatic activity of naturally occurring 1-acylglycerol-3-phosphate-O-acyltransferase 2 mutants associated with congenital generalized lipodystrophy". Biochemical and Biophysical Research Communications 327 (2): 446–53. Feb 2005. doi:10.1016/j.bbrc.2004.12.024. PMID 15629135.
- "Expression of lysophosphatidic acid acyltransferase beta (LPAAT-beta) in ovarian carcinoma: correlation with tumour grading and prognosis". British Journal of Cancer 92 (9): 1729–36. May 2005. doi:10.1038/sj.bjc.6602528. PMID 15841084.
- "Phenotypic heterogeneity in biochemical parameters correlates with mutations in AGPAT2 or Seipin genes among Berardinelli-Seip congenital lipodystrophy patients". Journal of Inherited Metabolic Disease 28 (6): 1123–31. 2006. doi:10.1007/s10545-005-0038-5. PMID 16435205.
- "Sustained elevations in NEFA induce cyclooxygenase-2 activity and potentiate THP-1 macrophage foam cell formation". Atherosclerosis 192 (1): 49–55. May 2007. doi:10.1016/j.atherosclerosis.2006.06.014. PMID 16870193.
 |  |
