The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

Links

 

Gene Review

AGPAT2  -  1-acylglycerol-3-phosphate O...

Homo sapiens

Synonyms: 1-AGP acyltransferase 2, 1-AGPAT 2, 1-AGPAT2, 1-acyl-sn-glycerol-3-phosphate acyltransferase beta, BSCL, ...
 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

Disease relevance of AGPAT2

 

Psychiatry related information on AGPAT2

  • In our subjects, there did not appear to be any distinguishing clinical characteristics between CGL subjects with AGPAT2 or Gng3lg mutations with the exception of mental retardation in carriers of Gng3lg [6].
 

High impact information on AGPAT2

 

Chemical compound and disease context of AGPAT2

 

Biological context of AGPAT2

 

Anatomical context of AGPAT2

  • LPAAT-alpha mRNA is uniformly expressed throughout most tissues with the highest level found in skeletal muscle; whereas LPAAT-beta is differentially expressed, with the highest level found in heart and liver, and negligible level in brain and placenta [12].
  • Lysophosphatidic acid acyltransferase beta mRNA was found in all cell lines and ovarian tumours examined [3].
  • Our data therefore demonstrate for the first time that inhibiting LPAAT-beta induces cytotoxicity in MM cells in the bone marrow milieu, providing the framework for clinical trials of these novel agents in MM [4].
  • The fact that lysoPM could traverse cell membranes permitted additional characterization of LPAAT-beta activity in cells: PC-3 and DU145 cells converted exogenously added lysoPM and (14)C-labeled 18:1 into (14)C-labeled phosphatidylmethanol (PM) [15].
  • Given that PA is a cofactor in a number of signaling cascades that are constitutively active in tumors, we evaluated the role of PA produced by LPAAT-beta in Xenopus oocyte meiotic maturation assays and an isoform-specific inhibitor of LPAAT-beta in mammalian cell assays [16].
 

Associations of AGPAT2 with chemical compounds

 

Other interactions of AGPAT2

  • We conclude that CGL patients with Seipin mutations have a more severe lack of body fat, which affects both metabolically active and mechanical adipose tissue, compared with patients with mutations in the AGPAT2 gene [1].
 

Analytical, diagnostic and therapeutic context of AGPAT2

References

  1. Phenotypic heterogeneity in body fat distribution in patients with congenital generalized lipodystrophy caused by mutations in the AGPAT2 or seipin genes. Simha, V., Garg, A. J. Clin. Endocrinol. Metab. (2003) [Pubmed]
  2. Mutations in the seipin and AGPAT2 genes clustering in consanguineous families with Berardinelli-Seip congenital lipodystrophy from two separate geographical regions of Brazil. Gomes, K.B., Fernandes, A.P., Ferreira, A.C., Pardini, H., Garg, A., Magré, J., Pardini, V.C. J. Clin. Endocrinol. Metab. (2004) [Pubmed]
  3. Expression of lysophosphatidic acid acyltransferase beta (LPAAT-beta) in ovarian carcinoma: correlation with tumour grading and prognosis. Niesporek, S., Denkert, C., Weichert, W., Köbel, M., Noske, A., Sehouli, J., Singer, J.W., Dietel, M., Hauptmann, S. Br. J. Cancer (2005) [Pubmed]
  4. Antitumor activity of lysophosphatidic acid acyltransferase-beta inhibitors, a novel class of agents, in multiple myeloma. Hideshima, T., Chauhan, D., Hayashi, T., Podar, K., Akiyama, M., Mitsiades, C., MItsiades, N., Gong, B., Bonham, L., de Vries, P., Munshi, N., Richardson, P.G., Singer, J.W., Anderson, K.C. Cancer Res. (2003) [Pubmed]
  5. Antileukemic Activity of Lysophosphatidic Acid Acyltransferase-{beta} Inhibitor CT32228 in Chronic Myelogenous Leukemia Sensitive and Resistant to Imatinib. La Ros??e, P., Jia, T., Demehri, S., H??rtel, N., de Vries, P., Bonham, L., Hollenback, D., Singer, J.W., Melo, J.V., Druker, B.J., Deininger, M.W. Clin. Cancer Res. (2006) [Pubmed]
  6. Mutations in Gng3lg and AGPAT2 in Berardinelli-Seip congenital lipodystrophy and Brunzell syndrome: phenotype variability suggests important modifier effects. Fu, M., Kazlauskaite, R., Baracho, M.d.e. .F., Santos, M.G., Brandão-Neto, J., Villares, S., Celi, F.S., Wajchenberg, B.L., Shuldiner, A.R. J. Clin. Endocrinol. Metab. (2004) [Pubmed]
  7. AGPAT2 is mutated in congenital generalized lipodystrophy linked to chromosome 9q34. Agarwal, A.K., Arioglu, E., De Almeida, S., Akkoc, N., Taylor, S.I., Bowcock, A.M., Barnes, R.I., Garg, A. Nat. Genet. (2002) [Pubmed]
  8. Identification of the gene altered in Berardinelli-Seip congenital lipodystrophy on chromosome 11q13. Magré, J., Delépine, M., Khallouf, E., Gedde-Dahl, T., Van Maldergem, L., Sobel, E., Papp, J., Meier, M., Mégarbané, A., Bachy, A., Verloes, A., d'Abronzo, F.H., Seemanova, E., Assan, R., Baudic, N., Bourut, C., Czernichow, P., Huet, F., Grigorescu, F., de Kerdanet, M., Lacombe, D., Labrune, P., Lanza, M., Loret, H., Matsuda, F., Navarro, J., Nivelon-Chevalier, A., Polak, M., Robert, J.J., Tric, P., Tubiana-Rufi, N., Vigouroux, C., Weissenbach, J., Savasta, S., Maassen, J.A., Trygstad, O., Bogalho, P., Freitas, P., Medina, J.L., Bonnicci, F., Joffe, B.I., Loyson, G., Panz, V.R., Raal, F.J., O'Rahilly, S., Stephenson, T., Kahn, C.R., Lathrop, M., Capeau, J. Nat. Genet. (2001) [Pubmed]
  9. Congenital generalized lipodystrophy: significance of triglyceride biosynthetic pathways. Agarwal, A.K., Garg, A. Trends Endocrinol. Metab. (2003) [Pubmed]
  10. Diseases of adipose tissue: genetic and acquired lipodystrophies. Capeau, J., Magré, J., Lascols, O., Caron, M., Béréziat, V., Vigouroux, C., Bastard, J.P. Biochem. Soc. Trans. (2005) [Pubmed]
  11. Genetic basis of congenital generalized lipodystrophy. Agarwal, A.K., Barnes, R.I., Garg, A. Int. J. Obes. Relat. Metab. Disord. (2004) [Pubmed]
  12. The structure and functions of human lysophosphatidic acid acyltransferases. Leung, D.W. Front. Biosci. (2001) [Pubmed]
  13. Phenotypic and genetic heterogeneity in congenital generalized lipodystrophy. Agarwal, A.K., Simha, V., Oral, E.A., Moran, S.A., Gorden, P., O'Rahilly, S., Zaidi, Z., Gurakan, F., Arslanian, S.A., Klar, A., Ricker, A., White, N.H., Bindl, L., Herbst, K., Kennel, K., Patel, S.B., Al-Gazali, L., Garg, A. J. Clin. Endocrinol. Metab. (2003) [Pubmed]
  14. Cloning and characterization of murine 1-acyl-sn-glycerol 3-phosphate acyltransferases and their regulation by PPARalpha in murine heart. Lu, B., Jiang, Y.J., Zhou, Y., Xu, F.Y., Hatch, G.M., Choy, P.C. Biochem. J. (2005) [Pubmed]
  15. Substrate specificity of lysophosphatidic acid acyltransferase beta -- evidence from membrane and whole cell assays. Hollenback, D., Bonham, L., Law, L., Rossnagle, E., Romero, L., Carew, H., Tompkins, C.K., Leung, D.W., Singer, J.W., White, T. J. Lipid Res. (2006) [Pubmed]
  16. Inhibition of lysophosphatidic acid acyltransferase beta disrupts proliferative and survival signals in normal cells and induces apoptosis of tumor cells. Coon, M., Ball, A., Pound, J., Ap, S., Hollenback, D., White, T., Tulinsky, J., Bonham, L., Morrison, D.K., Finney, R., Singer, J.W. Mol. Cancer Ther. (2003) [Pubmed]
  17. A Regulatory Role for 1-Acylglycerol-3-phosphate-O-acyltransferase 2 in Adipocyte Differentiation. Gale, S.E., Frolov, A., Han, X., Bickel, P.E., Cao, L., Bowcock, A., Schaffer, J.E., Ory, D.S. J. Biol. Chem. (2006) [Pubmed]
  18. Enzymatic activity of naturally occurring 1-acylglycerol-3-phosphate-O-acyltransferase 2 mutants associated with congenital generalized lipodystrophy. Haque, W., Garg, A., Agarwal, A.K. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  19. Interaction of lipopolysaccharide with a mammalian lyso-phosphatidate acyltransferase (LPAAT) transfected into E. coli, and effect of lisofylline on LPAAT transfected into mammalian cells. Bursten, S.L. Prog. Clin. Biol. Res. (1998) [Pubmed]
 
WikiGenes - Universities