Biology:Acylation stimulating protein
Complement 3 (C3) through its interaction with factors B and D (adipsin) generates C3a. In the human body, C3a is rapidly cleaved by carboxypeptidase B or carbxyopeptidase N, that remove the carboxyl-terminal arginine to generate C3adesArg.[1] Thus, most of plasmatic C3a is present in C3adesArg form. C3adesArg is more commonly named ASP or acylation-stimulating-protein due to its marked stimulating action on triacylglycerol synthesis in human adipocytes and skin fibroblasts.[2] ASP is also known for its augmentation of glucose transport and inhibiting action on hormone-sensitive lipase. Because of these actions, it is linked to the pathogenesis of obesity,[3] having been demonstrated to be present at increased levels in patients with obesity,[4] diabetes mellitus type 2[5] and coronary artery disease.[6]
ASP lis a ligand for C5L2, a G-protein-coupled receptor.[7]
The view of C3a/C3adesArg as an acylation stimulating activity is not universally accepted. The evidence is discussed in a recent review.[8]
References
- ↑ Baldo et al. 1993, pp. 1543–1547
- ↑ Cianflone et al., pp. 426–430
- ↑ (Sniderman Maslowska)
- ↑ Maslowska et al. 1999, pp. 679–686
- ↑ Koistinen et al. 2001, pp. 1034–1039
- ↑ Cianflone et al. 1997, pp. 1239–1244
- ↑ Cui et al. 2009, pp. 3207–3217
- ↑ "International Union of Pharmacology. LXXXVII. Complement peptide C5a, C4a, and C3a receptors". Pharmacol. Rev. 65 (1): 500–43. 2013. doi:10.1124/pr.111.005223. PMID 23383423.
Further reading
- Baldo, A; Sniderman, A D; St-Luce, S; Avramoglu, R K; Maslowska, M; Hoang, B; Monge, J C; Bell, A et al. (1993). "The adipsin-acylation stimulating protein system and regulation of intracellular triglyceride synthesis". Journal of Clinical Investigation 92 (3): 1543–1547. doi:10.1172/JCI116733. PMID 8376604.
- Cianflone, Katherine M.; Sniderman, Allan D.; Walsh, Mark J.; Vu, Hai T.; Gagnon, Jean; Rodriguez, Miguel A. (1989). "Purification and Characterization of Acylation Stimulating Protein". The Journal of Biological Chemistry 264 (1): 426–30. doi:10.1016/S0021-9258(17)31275-9. PMID 2909530. http://www.jbc.org/cgi/pmidlookup?view=long&pmid=2909530.
- Cianflone, K.; Zhang, XJ; Genest Jr, J; Sniderman, A (July 1997). "Plasma acylation-stimulating protein in coronary artery disease". Arterioscler Thromb Vasc Biol 17 (7): 1239–44. doi:10.1161/ATVB.17v07.1239. PMID 9261252.
- Cui, Wei; Lapointe, Marc; Gauvreau, Danny; Kalant, David; Cianflone, Katherine (October 2009). "Recombinant C3adesArg/acylation stimulating protein (ASP) is highly bioactive: a critical evaluation of C5L2 binding and 3T3-L1 adipocyte activation". Mol Immunol 46 (16): 3207–17. doi:10.1016/j.molimm.2009.08.013. PMID 19767107.
- Sniderman, Allan D.; Maslowska, Magdalena; Cianflone, Katherine (2000). "Of mice and men (and women) and the acylation-stimulating protein pathway". Current Opinion in Lipidology 11 (3): 291–6. doi:10.1097/00041433-200006000-00010. PMID 10882345.
- Maslowska, M; Vu, H; Phelis, S; Sniderman, AD; Rhode, BM; Blank, D; Cianflone, K (1999). "Plasma acylation stimulating protein, adipsin and lipids in non-obese and obese populations". European Journal of Clinical Investigation 29 (8): 679–86. doi:10.1046/j.1365-2362.1999.00514.x. PMID 10457151.
- Koistinen, Heikki A.; Vidal, Hubert; Karonen, Sirkka-Liisa; Dusserre, Eric; Vallier, Paulette; Koivisto, Veikko A.; Ebeling, Pertti (2001). "Plasma Acylation Stimulating Protein Concentration and Subcutaneous Adipose Tissue C3 mRNA Expression in Nondiabetic and Type 2 Diabetic Men". Arteriosclerosis, Thrombosis, and Vascular Biology 21 (6): 1034–9. doi:10.1161/01.atv.21.6.1034. PMID 11397716.
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