Identification of a functional proprotein convertase cleavage site in microfibril-associated glycoprotein 2

Matrix Biology

Volumn 32, Issue 2, 2013, Pages 117-122

  Donovan, Lauren J ^a   Cha, Seung E ^a   Yale, Andrew R ^a   Dreikorn, Stephanie ^a   Miyamoto, Alison ^a  

^a CALIFORNIA STATE UNIVERSITY   (United States)

Author keywords

Glycoprotein; Microfibril; Proprotein convertase; Secretion

Indexed keywords

AMINO ACID; GLYCOPROTEIN; INTEGRIN; MICROFIBRIL ASSOCIATED GLYCOPROTEIN 2; NOTCH RECEPTOR; PROPROTEIN CONVERTASE 1; UNCLASSIFIED DRUG;

ANGIOGENESIS; ARTICLE; CELL SURFACE; CONSENSUS; FIBER; HUMAN; MUTAGENESIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN FUNCTION; PROTEIN SECRETION;

AMINO ACID SEQUENCE; CELL LINE; CONTRACTILE PROTEINS; EXTRACELLULAR MATRIX; GLYCOPROTEINS; HUMANS; INTEGRINS; MICROFIBRILS; PROPROTEIN CONVERTASES; PROTEIN ISOFORMS; PROTEOLYSIS;

EID: 84875813134     PISSN: 0945053X     EISSN: 15691802     Source Type: Journal    
DOI: 10.1016/j.matbio.2012.11.009     Document Type: Article

References (26)

1. Albig A.R., Roy T.G., Becenti D.J., Schiemann W.P. Transcriptome analysis of endothelial cell gene expression induced by growth on Matrigel matrices: identification and characterization of MAGP-2 and lumican as novel regulators of angiogenesis. Angiogenesis 2007, 10:197-216.
2. Albig A.R., Becenti D.J., Roy T.G., Schiemann W.P. Microfibril-associate glycoprotein-2 (MAGP-2) promotes angiogenic cell sprouting by blocking notch signaling in endothelial cells. Microvasc. Res. 2008, 76:7-14.
3. Bush G., diSibio G., Miyamoto A., Denault J.B., Leduc R., Weinmaster G. Ligand-induced signaling in the absence of furin processing of Notch1. Dev. Biol. 2001, 229:494-502.
4. Duckert P., Brunak S., Blom N. Prediction of proprotein convertase cleavage sites. Protein Eng. Des. Sel. 2004, 17:107-112.
5. Dufour E.K., Denault J.B., Bissonnette L., Hopkins P.C., Lavigne P., Leduc R. The contribution of arginine residues within the P6-P1 region of alpha 1-antitrypsin to its reaction with furin. J. Biol. Chem. 2001, 276:38971-38979.
6. Endres K., Anders A., Kojro E., Gilbert S., Fahrenholz F., Postina R. Tumor necrosis factor-alpha converting enzyme is processed by proprotein-convertases to its mature form which is degraded upon phorbol ester stimulation. Eur. J. Biochem. 2003, 270:2386-2393.
7. Gibson M.A., Hatzinikolas G., Kumaratilake J.S., Sandberg L.B., Nicholl J.K., Sutherland G.R., Cleary E.G. Further characterization of proteins associated with elastic fiber microfibrils including the molecular cloning of MAGP-2 (MP25). J. Biol. Chem. 1996, 271:1096-1103.
8. Lemaire R., Bayle J., Mecham R.P., Lafyatis R. Microfibril-associated MAGP-2 stimulates elastic fiber assembly. J. Biol. Chem. 2007, 282:800-808.
9. Li Q., Rajanahally S., Edson M.A., Matzuk M.M. Stable expression and characterization of N-terminal tagged recombinant human bone morphogenetic protein 15. Mol. Hum. Reprod. 2009, 15:779-788.
10. Logeat F., Bessia C., Brou C., LeBail O., Jarriault S., Seidah N.G., Israel A. The Notch1 receptor is cleaved constitutively by a furin-like convertase. Proc. Natl. Acad. Sci. U. S. A. 1998, 95:8108-8112.
11. Lonnqvist L., Reinhardt D., Sakai L., Peltonen L. Evidence for furin-type activity-mediated C-terminal processing of profibrillin-1 and interference in the processing by certain mutations. Hum. Mol. Genet. 1998, 7:2039-2044.
12. McColl B.K., Paavonen K., Karnezis T., Harris N.C., Davydova N., Rothacker J., Nice E.C., Harder K.W., Roufail S., Hibbs M.L., Rogers P.A., Alitalo K., Stacker S.A., Achen M.G. Proprotein convertases promote processing of VEGF-D, a critical step for binding the angiogenic receptor VEGFR-2. FASEB J. 2007, 21:1088-1098.
13. Mesnard D., Donnison M., Fuerer C., Pfeffer P.L., Constam D.B. The microenvironment patterns the pluripotent mouse epiblast through paracrine Furin and Pace4 proteolytic activities. Genes Dev. 2011, 25:1871-1880.
14. Miyamoto A., Lau R., Hein P.W., Shipley J.M., Weinmaster G. Microfibrillar proteins MAGP-1 and MAGP-2 induce Notch1 extracellular domain dissociation and receptor activation. J. Biol. Chem. 2006, 281:10089-10097.
15. Mok S.C., Bonome T., Vathipadiekal V., Bell A., Johnson M.E., Wong K.K., Park D.C., Hao K., Yip D.K., Donninger H., Ozbun L., Samimi G., Brady J., Randonovich M., Pise-Masison C.A., Barrett J.C., Wong W.H., Welch W.R., Berkowitz R.S., Birrer M.J. A gene signature predictive for outcome in advanced ovarian cancer identifies a survival factor: microfibril-associated glycoprotein 2. Cancer Cell 2009, 16:521-532.
16. Noel D., Nikaido K., Ames G.F. A single amino acid substitution in a histidine-transport protein drastically alters its mobility in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Biochemistry 1979, 18:4159-4165.
17. Phillips C.L., Shrago-Howe A.W., Pinnell S.R., Wenstrup R.J. A substitution at a non-glycine position in the triple-helical domain of pro alpha 2(I) collagen chains present in an individual with a variant of the Marfan syndrome. J. Clin. Invest. 1990, 86:1723-1728.
18. Raghunath M., Putnam E.A., Ritty T., Hamstra D., Park E.S., Tschodrich-Rotter M., Peters R., Rehemtulla A., Milewicz D.M. Carboxy-terminal conversion of profibrillin to fibrillin at a basic site by PACE/furin-like activity required for incorporation in the matrix. J. Cell Sci. 1999, 112(Pt. 7):1093-1100.
19. Rodriguez-Manzaneque J.C., Milchanowski A.B., Dufour E.K., Leduc R., Iruela-Arispe M.L. Characterization of METH-1/ADAMTS1 processing reveals two distinct active forms. J. Biol. Chem. 2000, 275:33471-33479.
20. Sasanami T., Toriyama M., Mori M. Carboxy-terminal proteolytic processing at a consensus furin cleavage site is a prerequisite event for quail ZPC secretion. Biol. Reprod. 2003, 68:1613-1619.
21. Schagger H. Tricine-SDS-PAGE. Nat. Protoc. 2006, 1:16-22.
22. Segade F. Functional evolution of the microfibril-associated glycoproteins. Gene 2009, 439:43-54.
23. Seidah N.G. What lies ahead for the proprotein convertases?. Ann. N. Y. Acad. Sci. 2011, 1220:149-161.
24. Takahashi N., Takahashi Y., Blumberg B.S., Putnam F.W. Amino acid substitutions in genetic variants of human serum albumin and in sequences inferred from molecular cloning. Proc. Natl. Acad. Sci. U. S. A. 1987, 84:4413-4417.
25. UniProt Consortium Reorganizing the protein space at the Universal Protein Resource (UniProt). Nucleic Acids Res. 2012, 40:D71-D75.
26. Wallis D.D., Putnam E.A., Cretoiu J.S., Carmical S.G., Cao S.N., Thomas G., Milewicz D.M. Profibrillin-1 maturation by human dermal fibroblasts: proteolytic processing and molecular chaperones. J. Cell. Biochem. 2003, 90:641-652.