Acylation stimulating protein

Complement 3 (C3) through its interaction with factors B and D (adipsin) generates C3a. In the human body, C3a is rapidily 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 ligates a specific receptor named C5L2 which is coupled with a G-protein.[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

  1. ↑ (Baldo et al. 1993, pp. 1543–1547)
  2. ↑ (Cianflone et al., pp. 426–430)
  3. ↑ (Sniderman, Maslowska & Cianflone 2000, pp. 291–296)
  4. ↑ (Maslowska et al. 1999, pp. 679–686)
  5. ↑ (Koistinen et al. 2001, pp. 1034–1039)
  6. ↑ (Cianflone et al. 1997, pp. 1239–1244)
  7. ↑ (Cui et al. 2009, pp. 3207–3217)
  8. ↑ Klos A, Wende E, Wareham KJ, Monk PN (2013). "International Union of Pharmacology. LXXXVII. Complement peptide C5a, C4a, and C3a receptors". Pharmacol. Rev. 65 (1): 500–43. 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; Mulay, S; Cianflone, K (1993). "The adipsin-acylation stimulating protein system and regulation of intracellular triglyceride synthesis". Journal of Clinical Investigation. 92 (3). doi:10.1172/JCI116733. PMC 288301. 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. PMID 2909530.
  • 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.
This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.