Apolipoprotein C-II is a novel substrate for matrix metalloproteinases

Biochemical and Biophysical Research Communications

Volumn 339, Issue 1, 2006, Pages 47-54

  Kim, Se Yeon ^a   Park, Sung Min ^a   Lee, Seung Taek ^a  

^a Yonsei University   (South Korea)

Author keywords

Apolipoprotein C II; Atherosclerosis; Cleavage site; Lipoprotein lipase; Matrix metalloproteinase; Proteomics

Indexed keywords

APOLIPOPROTEIN C2; CHYLOMICRON; LIPOPROTEIN; MATRIX METALLOPROTEINASE;

AMINO ACID ANALYSIS; ARTICLE; CONTROLLED STUDY; DNA CLEAVAGE; ENZYME ACTIVITY; HYDROLYSIS; NONHUMAN; PATHOPHYSIOLOGY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEOMICS;

AMINO ACID SEQUENCE; APOLIPOPROTEIN C-II; APOLIPOPROTEINS C; CLONING, MOLECULAR; ELECTROPHORESIS, GEL, TWO-DIMENSIONAL; HUMANS; MATRIX METALLOPROTEINASE 7; MATRIX METALLOPROTEINASES; MATRIX METALLOPROTEINASES, MEMBRANE-ASSOCIATED; MOLECULAR SEQUENCE DATA; PROTEOMICS; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; SUBSTRATE SPECIFICITY;

EID: 28144440373     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.10.182     Document Type: Article

References (28)

1. J.C. Osborne Jr., and H.B. Brewer Jr. The plasma lipoproteins Adv. Protein Chem. 31 1977 253 337
2. M.C. Jong, M.H. Hofker, and L.M. Havekes Role of ApoCs in lipoprotein metabolism: functional differences between ApoC1, ApoC2, and ApoC3 Arterioscler. Thromb. Vasc. Biol. 19 1999 472 484
3. J.C. LaRosa, R.I. Levy, P. Herbert, S.E. Lux, and D.S. Fredrickson A specific apoprotein activator for lipoprotein lipase Biochem. Biophys. Res. Commun. 41 1970 57 62
4. I.J. Goldberg Lipoprotein lipase and lipolysis: central roles in lipoprotein metabolism and atherogenesis J. Lipid Res. 37 1996 693 707
5. J.R. Mead, S.A. Irvine, and D.P. Ramji Lipoprotein lipase: structure, function, regulation, and role in disease J. Mol. Med. 80 2002 753 769
6. P.K. Kinnunen, R.L. Jackson, L.C. Smith, A.M. Gotto Jr., and J.T. Sparrow Activation of lipoprotein lipase by native and synthetic fragments of human plasma apolipoprotein C-II Proc. Natl. Acad. Sci. USA 74 1977 4848 4851
7. J.T. Sparrow, and A.M. Gotto Jr. Phospholipid binding studies with synthetic apolipoprotein fragments Ann. N.Y. Acad. Sci. 348 1980 187 211
8. W.C. Breckenridge, J.A. Little, G. Steiner, A. Chow, and M. Poapst Hypertriglyceridemia associated with deficiency of apolipoprotein C-II N. Engl. J. Med. 298 1978 1265 1273
9. A.R. Nelson, B. Fingleton, M.L. Rothenberg, and L.M. Matrisian Matrix metalloproteinases: biologic activity and clinical implications J. Clin. Oncol. 18 2000 1135 1149
10. W.C. Parks, and R.P. Mecham Matrix Metalloproteinases 1998 Academic Press San Diego
11. D.E. Kleiner, and W.G. Stetler-Stevenson Matrix metalloproteinases and metastasis Cancer Chemother. Pharmacol. 43 1999 S42 S51
12. S. Zucker, J. Cao, and W.T. Chen Critical appraisal of the use of matrix metalloproteinase inhibitors in cancer treatment Oncogene 19 2000 6642 6650
13. I.K. Hwang, S.M. Park, S.Y. Kim, and S.-T. Lee A proteomic approach to identify substrates of matrix metalloproteinase-14 in human plasma Biochim. Biophys. Acta 1702 2004 79 87
14. H.M. Koo, J.-H. Kim, I.K. Hwang, S.-J. Lee, T.-H. Kim, K.-H. Rhee, and S.-T. Lee Refolding of the catalytic and hinge domains of human MT1-MMP expressed in Escherichia coli and its characterization Mol. Cells 13 2002 114 120
15. M. Itoh, K. Masuda, Y. Ito, T. Akizawa, M. Yoshioka, K. Imai, Y. Okada, H. Sato, and M. Seiki Purification and refolding of recombinant human proMMP-7 (pro-matrilysin) expressed in Escherichia coli and its characterization J. Biochem. 119 1996 667 673
16. Y. Jo, D.-W. Yoon, M.-Y. Kim, Y.-J. Lee, H.-J. Kim, and S.-T. Lee Tissue inhibitor of metalloproteinases-2 inhibits the 4-aminophenylmercuric acetate-induced activation and autodegradation of the free promatrix metalloproteinase-2 J. Biochem. Mol. Biol. 32 1999 60 66
17. S.M. Wilhelm, I.E. Collier, B.L. Marmer, A.Z. Eisen, G.A. Grant, and G.I. Goldberg SV40-transformed human lung fibroblasts secrete a 92-kDa type IV collagenase which is identical to that secreted by normal human macrophages J. Biol. Chem. 264 1989 17213 17221
18. O. Myklebost, B. Williamson, A.F. Markham, S.R. Myklebost, J. Rogers, D.E. Woods, and S.E. Humphries The isolation and characterization of cDNA clones for human apolipoprotein CII J. Biol. Chem. 259 1984 4401 4404
19. C.S. Wang, D. Downs, A. Dashti, and K.W. Jackson Isolation and characterization of recombinant human apolipoprotein C-II expressed in Escherichia coli Biochim. Biophys. Acta 16 1996 224 230
20. L. Lindstedt, J. Saarinen, N. Kalkkinen, H. Welgus, and P.T. Kovanen Matrix metalloproteinases-3, -7, and -12, but not -9, reduce high density lipoprotein-induced cholesterol efflux from human macrophage foam cells by truncation of the carboxyl terminus of apolipoprotein A-I. Parallel losses of pre-beta particles and the high affinity component of efflux J. Biol. Chem. 274 1999 22627 22634
21. B.E. Turk, L.L. Huang, E.T. Piro, and L.C. Cantley Determination of protease cleavage site motifs using mixture-based oriented peptide libraries Nat. Biotechnol. 19 2001 661 667
22. C.A. MacRaild, D.M. Hatters, G.J. Howlett, and P.R. Gooley NMR structure of human apolipoprotein C-II in the presence of sodium dodecyl sulfate Biochemistry 40 2001 5414 5421
23. P. Vainio, J.A. Virtanen, P.K. Kinnunen, A.M. Gotto Jr., J.T. Sparrow, F. Pattus, P. Bougis, and R. Verger Action of lipoprotein lipase on mixed triacylglycerol/phosphatidylcholine monolayers. Activation by apolipoprotein C-II J. Biol. Chem. 258 1983 5477 5482
24. C.E. MacPhee, G.J. Howlett, and W.H. Sawyer Mass spectrometry to characterize the binding of a peptide to a lipid surface Anal. Biochem. 275 1999 22 29
25. G. Olivecrona, and U. Beisiegel Lipid binding of apolipoprotein CII is required for stimulation of lipoprotein lipase activity against apolipoprotein CII-deficient chylomicrons Arterioscler. Thromb. Vasc. Biol. 17 1997 1545 1549
26. T.B. Rajavashisth, X.P. Xu, S. Jovinge, S. Meisel, X.O. Xu, N.N. Chai, M.C. Fishbein, S. Kaul, B. Cercek, B. Sharifi, and P.K. Shah Membrane type 1 matrix metalloproteinase expression in human atherosclerotic plaques: evidence for activation by proinflammatory mediators Circulation 99 1999 3103 3109
27. I. Halpert, U.I. Sires, J.D. Roby, S. Potter-Perigo, T.N. Wight, S.D. Shapiro, H.G. Welgus, S.A. Wickline, and W.C. Parks Matrilysin is expressed by lipid-laden macrophages at sites of potential rupture in atherosclerotic lesions and localizes to areas of versican deposition, a proteoglycan substrate for the enzyme Proc. Natl. Acad. Sci. USA 93 1996 9748 9753
28. A.R. Folgueras, A.M. Pendas, L.M. Sanchez, and C. Lopez-Otin Matrix metalloproteinases in cancer: from new functions to improved inhibition strategies Int. J. Dev. Biol. 48 2004 411 424