Preferential apelin-13 production by the proprotein convertase PCSK3 is implicated in obesity

FEBS Open Bio

Volumn 3, Issue , 2013, Pages 328-333

  Shin, Kyungsoo ^a   Pandey, Aditya ^a   Liu, Xiang Qin ^a   Anini, Younes ^b   Rainey, Jan K ^a,b  

^a DALHOUSIE UNIVERSITY   (Canada)

^b DALHOUSIE UNIVERSITY   (Canada)

Author keywords

Adipocyte differentiation; Furin; Proapelin; Prohormone processing; Proprotein convertase subtisilin kexin 3

Indexed keywords

APELIN; APELIN 13; FURIN; PROPROTEIN CONVERTASE 1; PROPROTEIN CONVERTASE SUBTILISIN KEXIN 3; SERINE PROTEINASE; UNCLASSIFIED DRUG;

ADIPOGENESIS; ADIPOSE TISSUE; ARTICLE; CONTROLLED STUDY; HUMAN; HUMAN CELL; IN VITRO STUDY; OBESITY; PRIORITY JOURNAL; PROCESSING; PROTEIN CLEAVAGE; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN SYNTHESIS; TRANSCRIPTION REGULATION;

EID: 84883039536     PISSN: 22115463     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.fob.2013.08.001     Document Type: Article

References (31)

1. Tatemoto K., Hosoya M., Habata Y., Fujii R., Kakegawa T., Zou M.X., Kawamata Y., Fukusumi S., Hinuma S., Kitada C., Kurokawa T., Onda H., Fujino M. Isolation and characterization of a novel endogenous peptide ligand for the human APJ receptor. Biochem. Biophys. Res. Commun. 1998, 251:471-476.
2. Japp A.G., Newby D.E. The apelin-APJ system in heart failure: pathophysiologic relevance and therapeutic potential. Biochem. Pharmacol. 2008, 75:1882-1892.
3. Kleinz M.J., Davenport A.P. Emerging roles of apelin in biology and medicine. Pharmacol. Ther. 2005, 107:198-211.
4. O'Dowd B.F., Heiber M., Chan A., Heng H.H., Tsui L.C., Kennedy J.L., Shi X., Petronis A., George S.R., Nguyen T. A human gene that shows identity with the gene encoding the angiotensin receptor is located on chromosome 11. Gene 1993, 136:355-360.
5. Soriguer F., Garrido-Sanchez L., Garcia-Serrano S., Garcia-Almeida J.M., Garcia-Arnes J., Tinahones F.J., Garcia-Fuentes E. Apelin levels are increased in morbidly obese subjects with type 2 diabetes mellitus. Obes. Surg. 2009, 19:1574-1580.
6. Than A., Cheng Y., Foh L.C., Leow M.K., Lim S.C., Chuah Y.J., Kang Y., Chen P. Apelin inhibits adipogenesis and lipolysis through distinct molecular pathways. Mol. Cell. Endocrinol. 2012, 362:227-241.
7. Castan-Laurell I., Dray C., Knauf C., Kunduzova O., Valet P. Apelin, a promising target for type 2 diabetes treatment?. Trends Endocrinol. Metab. 2012, 23:234-241.
8. Masri B., Knibiehler B., Audigier Y. Apelin signalling: a promising pathway from cloning to pharmacology. Cell. Signal. 2005, 17:415-426.
9. Tatemoto K., Takayama K., Zou M.X., Kumaki I., Zhang W., Kumano K., Fujimiya M. The novel peptide apelin lowers blood pressure via a nitric oxide-dependent mechanism. Regul. Pept. 2001, 99:87-92.
10. Pitkin S.L., Maguire J.J., Bonner T.I., Davenport A.P. International Union of Basic and Clinical Pharmacology. LXXIV. Apelin receptor nomenclature, distribution, pharmacology, and function. Pharmacol. Rev. 2010, 62:331-342.
11. Lee D.K., Ferguson S.S., George S.R., O'Dowd B.F. The fate of the internalized apelin receptor is determined by different isoforms of apelin mediating differential interaction with beta-arrestin. Biochem. Biophys. Res. Commun. 2010, 395:185-189.
12. Kawamata Y., Habata Y., Fukusumi S., Hosoya M., Fujii R., Hinuma S., Nishizawa N., Kitada C., Onda H., Nishimura O., Fujino M. Molecular properties of apelin: tissue distribution and receptor binding. Biochim. Biophys. Acta 2001, 1538:162-171.
13. De Mota N., Lenkei Z., Llorens-Cortes C. Cloning, pharmacological characterization and brain distribution of the rat apelin receptor. Neuroendocrinology 2000, 72:400-407.
14. Maguire J.J., Kleinz M.J., Pitkin S.L., Davenport A.P. [Pyr1]apelin-13 identified as the predominant apelin isoform in the human heart: vasoactive mechanisms and inotropic action in disease. Hypertension 2009, 54:598-604.
15. Seidah N.G. The proprotein convertases, 20years later. Methods Mol. Biol. 2011, 768:23-57.
16. Brakch N., Rholam M., Boussetta H., Cohen P. Role of beta-turn in proteolytic processing of peptide hormone precursors at dibasic sites. Biochemistry 1993, 32:4925-4930.
17. Langelaan D.N., Bebbington E.M., Reddy T., Rainey J.K. Structural insight into G-protein coupled receptor binding by apelin. Biochemistry 2009, 48:537-548.
18. Green H., Kehinde O. An established preadipose cell line and its differentiation in culture. II. Factors affecting the adipose conversion. Cell 1975, 5:19-27.
19. Morash M.G., Gagnon J., Nelson S., Anini Y. Tissue distribution and effects of fasting and obesity on the ghrelin axis in mice. Regul. Pept. 2010, 163:62-73.
20. Beaubien G., Schafer M.K., Weihe E., Dong W., Chretien M., Seidah N.G., Day R. The distinct gene expression of the pro-hormone convertases in the rat heart suggests potential substrates. Cell Tissue Res. 1995, 279:539-549.
21. Enomoto T., Shibata R., Ohashi K., Kambara T., Kataoka Y., Uemura Y., Yuasa D., Murohara T., Ouchi N. Regulation of adipolin/CTRP12 cleavage by obesity. Biochem. Biophys. Res. Commun. 2012, 428:155-159.
22. Paroutis P., Touret N., Grinstein S. The pH of the secretory pathway: measurement, determinants, and regulation. Physiology 2004, 19:207-215.
23. Molloy S.S., Bresnahan P.A., Leppla S.H., Klimpel K.R., Thomas G. Human furin is a calcium-dependent serine endoprotease that recognizes the sequence Arg-X-X-Arg and efficiently cleaves anthrax toxin protective antigen. J. Biol. Chem. 1992, 267:16396-16402.
24. Rholam M., Fahy C. Processing of peptide and hormone precursors at the dibasic cleavage sites. Cell. Mol. Life. Sci. 2009, 66:2075-2091.
25. Fan X., Zhou N., Zhang X., Mukhtar M., Lu Z., Fang J., DuBois G.C., Pomerantz R.J. Structural and functional study of the apelin-13 peptide, an endogenous ligand of the HIV-1 coreceptor, APJ. Biochemistry 2003, 42:10163-10168.
26. Scamuffa N., Basak A., Lalou C., Wargnier A., Marcinkiewicz J., Siegfried G., Chretien M., Calvo F., Seidah N.G., Khatib A.M. Regulation of prohepcidin processing and activity by the subtilisin-like proprotein convertases Furin, PC5, PACE4 and PC7. Gut 2008, 57:1573-1582.
27. Jean F., Basak A., Rondeau N., Benjannet S., Hendy G.N., Seidah N.G., Chretien M., Lazure C. Enzymic characterization of murine and human prohormone convertase-1 (mPC1 and hPC1) expressed in mammalian GH4C1 cells. Biochem. J. 1993, 292(Pt. 3):891-900.
28. Remacle A.G., Shiryaev S.A., Oh E.S., Cieplak P., Srinivasan A., Wei G., Liddington R.C., Ratnikov B.I., Parent A., Desjardins R., Day R., Smith J.W., Lebl M., Strongin A.Y. Substrate cleavage analysis of furin and related proprotein convertases. A comparative study. J. Biol. Chem. 2008, 283:20897-20906.
29. Siegfried G., Basak A., Cromlish J.A., Benjannet S., Marcinkiewicz J., Chretien M., Seidah N.G., Khatib A.M. The secretory proprotein convertases furin, PC5, and PC7 activate VEGF-C to induce tumorigenesis. J. Clin. Invest. 2003, 111:1723-1732.
30. Boucher J., Masri B., Daviaud D., Gesta S., Guigne C., Mazzucotelli A., Castan-Laurell I., Tack I., Knibiehler B., Carpene C., Audigier Y., Saulnier-Blache J.S., Valet P. Apelin, a newly identified adipokine up-regulated by insulin and obesity. Endocrinology 2005, 146:1764-1771.
31. Castan-Laurell I., Vitkova M., Daviaud D., Dray C., Kovacikova M., Kovacova Z., Hejnova J., Stich V., Valet P. Effect of hypocaloric diet-induced weight loss in obese women on plasma apelin and adipose tissue expression of apelin and APJ. Eur. J. Endocrinol. 2008, 158:905-910.