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Apln  -  apelin

Mus musculus

Synonyms: 6030430G11Rik, APJ endogenous ligand, Apel, Apelin
 
 
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Disease relevance of Apln

  • Using stably transfected cells expressing a pertussis toxin-insensitive alpha(i) subunit, we demonstrated that each apelin fragment promoted coupling of the apelin receptor to either Galpha(i1) or Galpha(i2) but not to Galpha(i3) [1].
  • Finally, we show that, similar to a number of other angiogenic factors, expression of the apelin gene is increased under conditions of hypoxia [2].
  • Taken together, these studies indicate that apelin is required for normal vascular development in the frog embryo and has properties consistent with a role during normal and pathological angiogenesis [2].
  • 5. CONCLUSIONS: Apelin reduces left ventricular preload and afterload and increases contractile reserve without evidence of hypertrophy [3].
  • In addition, we carried out histology and immunohistochemistry to assess cardiac hypertrophy and to localize apelin and APJ in the adult and embryonic mouse heart [3].
 

High impact information on Apln

  • We found that both apelin fragments inhibited adenylyl cyclase and increased the phosphorylation of ERK or Akt [1].
  • To address the physiological significance of the existence of dual ligands for a single receptor, we first compared the ability of the apelin fragments to regulate intracellular effectors, to promote G protein coupling, and to desensitize the response in Chinese hamster ovary cells expressing the murine apelin receptor [1].
  • Furthermore, studies using the mouse brain microvascular cell line bEnd.3 show that apelin acts as a mitogenic, chemotactic and anti-apoptotic agent for endothelial cells in culture [2].
  • In gain of function experiments, apelin peptide is a potent angiogenic factor when tested using two in vivo angiogenesis assays, the frog embryo and the chicken chorioallantoic membrane [2].
  • Post-mortem corrected heart weights were not different between apelin and saline groups (p=0.5) and histology revealed no evidence of cellular hypertrophy in the apelin group (nuclei per unit area, p=0.9) [3].
 

Biological context of Apln

 

Anatomical context of Apln

 

Associations of Apln with chemical compounds

  • We speculate that high glucocorticoid levels suppress apelin production and stimulate angiotensin II production in adipocyte, decreasing the counter-regulatory activity of apelin against the pressor action of angiotensin II, which might partly be involved in the mechanism underlying the development of obesity-related hypertension [4].
  • Inhibition of protein kinase C (PKC) with GF-109203X markedly attenuated the apelin-induced MLC phosphorylation [6].
  • Apelin (2 nmol/kg) also inhibited the insulin response to intravenous glucose in obese insulin resistant high-fat fed C57BL/6J mice (P=0.041) [9].
  • In rat primary aortic smooth muscle cells, apelin inhibited Ang II-mediated transcriptional regulation of multiple targets as measured by reporter assays [10].
 

Regulatory relationships of Apln

 

Analytical, diagnostic and therapeutic context of Apln

References

  1. The apelin receptor is coupled to Gi1 or Gi2 protein and is differentially desensitized by apelin fragments. Masri, B., Morin, N., Pedebernade, L., Knibiehler, B., Audigier, Y. J. Biol. Chem. (2006) [Pubmed]
  2. Apelin, the ligand for the endothelial G-protein-coupled receptor, APJ, is a potent angiogenic factor required for normal vascular development of the frog embryo. Cox, C.M., D'Agostino, S.L., Miller, M.K., Heimark, R.L., Krieg, P.A. Dev. Biol. (2006) [Pubmed]
  3. The endogenous peptide apelin potently improves cardiac contractility and reduces cardiac loading in vivo. Ashley, E.A., Powers, J., Chen, M., Kundu, R., Finsterbach, T., Caffarelli, A., Deng, A., Eichhorn, J., Mahajan, R., Agrawal, R., Greve, J., Robbins, R., Patterson, A.J., Bernstein, D., Quertermous, T. Cardiovasc. Res. (2005) [Pubmed]
  4. Regulation of apelin mRNA expression by insulin and glucocorticoids in mouse 3T3-L1 adipocytes. Wei, L., Hou, X., Tatemoto, K. Regul. Pept. (2005) [Pubmed]
  5. G protein-coupled APJ receptor signaling induces focal adhesion formation and cell motility. Hashimoto, Y., Ishida, J., Yamamoto, R., Fujiwara, K., Asada, S., Kasuya, Y., Mochizuki, N., Fukamizu, A. Int. J. Mol. Med. (2005) [Pubmed]
  6. Apelin stimulates myosin light chain phosphorylation in vascular smooth muscle cells. Hashimoto, T., Kihara, M., Ishida, J., Imai, N., Yoshida, S., Toya, Y., Fukamizu, A., Kitamura, H., Umemura, S. Arterioscler. Thromb. Vasc. Biol. (2006) [Pubmed]
  7. Expression of the murine msr/apj receptor and its ligand apelin is upregulated during formation of the retinal vessels. Saint-Geniez, M., Masri, B., Malecaze, F., Knibiehler, B., Audigier, Y. Mech. Dev. (2002) [Pubmed]
  8. Apelin is a novel angiogenic factor in retinal endothelial cells. Kasai, A., Shintani, N., Oda, M., Kakuda, M., Hashimoto, H., Matsuda, T., Hinuma, S., Baba, A. Biochem. Biophys. Res. Commun. (2004) [Pubmed]
  9. The apj receptor is expressed in pancreatic islets and its ligand, apelin, inhibits insulin secretion in mice. Sörhede Winzell, M., Magnusson, C., Ahrén, B. Regul. Pept. (2005) [Pubmed]
  10. Apelin signaling antagonizes Ang II effects in mouse models of atherosclerosis. Chun, H.J., Ali, Z.A., Kojima, Y., Kundu, R.K., Sheikh, A.Y., Agrawal, R., Zheng, L., Leeper, N.J., Pearl, N.E., Patterson, A.J., Anderson, J.P., Tsao, P.S., Lenardo, M.J., Ashley, E.A., Quertermous, T. J. Clin. Invest. (2008) [Pubmed]
  11. Apelin expression in normal human tissues. De Falco, M., De Luca, L., Onori, N., Cavallotti, I., Artigiano, F., Esposito, V., De Luca, B., Laforgia, V., Groeger, A.M., De Luca, A. In Vivo (2002) [Pubmed]
  12. Apelin (65-77) activates extracellular signal-regulated kinases via a PTX-sensitive G protein. Masri, B., Lahlou, H., Mazarguil, H., Knibiehler, B., Audigier, Y. Biochem. Biophys. Res. Commun. (2002) [Pubmed]
  13. Apelin, an APJ receptor ligand, regulates body adiposity and favors the messenger ribonucleic acid expression of uncoupling proteins in mice. Higuchi, K., Masaki, T., Gotoh, K., Chiba, S., Katsuragi, I., Tanaka, K., Kakuma, T., Yoshimatsu, H. Endocrinology (2007) [Pubmed]
 
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