Adenylyl cyclase-associated protein-1/CAP1 as a biological target substrate of gelatinase B/MMP-9

Experimental Cell Research

Volumn 314, Issue 15, 2008, Pages 2739-2749

  Cauwe, Bénédicte ^a   Martens, Erik ^a   Van den Steen, Philippe E ^a   Proost, Paul ^a   Van Aelst, Ilse ^a   Blockmans, Daniel ^b   Opdenakker, Ghislain ^a  

^a REGA INSTITUTE FOR MEDICAL RESEARCH   (Belgium)

^b UNIVERSITY HOSPITALS LEUVEN   (Belgium)

Author keywords

Actin; Apoptosis; Autoimmunity; Cytolysis; Inflammation; Intracellular; Necrosis; Proteolysis; Substrate; Urine

Indexed keywords

CYTOSKELETON PROTEIN; GELATINASE B; PROTEIN CAP1; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

ADOLESCENT; ADULT; AGED; APOPTOSIS; ARTICLE; AUTOIMMUNE DISEASE; CLINICAL ARTICLE; CONTROLLED STUDY; FEMALE; FLOW CYTOMETRY; GENE DELETION; HUMAN; HUMAN CELL; IN VITRO STUDY; INCUBATION TIME; KIDNEY FAILURE; MALE; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN METABOLISM; PROTEIN PROCESSING; PROTEIN PURIFICATION; PROTEIN STRUCTURE; SJOEGREN SYNDROME; SYSTEMIC LUPUS ERYTHEMATOSUS; TEMPORAL ARTERITIS; URINALYSIS;

EID: 50049122649     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yexcr.2008.07.008     Document Type: Article

References (35)

1. Sternlicht M.D., and Werb Z. How matrix metalloproteinases regulate cell behavior. Annu. Rev. Cell Dev. Biol. 17 (2001) 463-516
2. Lopez-Otin C., and Overall C.M. Protease degradomics: a new challenge for proteomics. Nat. Rev., Mol. Cell Biol. 3 (2002) 509-519
3. Cauwe B., Van den Steen P.E., and Opdenakker G. The biochemical, biological, and pathological kaleidoscope of cell surface substrates processed by matrix metalloproteinases. Crit. Rev. Biochem. Mol. Biol. 42 (2007) 113-185
4. Szklarczyk A., Oyler G., McKay R., Gerfen C., and Conant K. Cleavage of neuronal synaptosomal-associated protein of 25 kDa by exogenous matrix metalloproteinase-7. J. Neurochem. 102 (2007) 1256-1263
5. Kwan J.A., Schulze C.J., Wang W., Leon H., Sariahmetoglu M., Sung M., Sawicka J., Sims D.E., Sawicki G., and Schulz R. Matrix metalloproteinase-2 (MMP-2) is present in the nucleus of cardiac myocytes and is capable of cleaving poly (ADP-ribose) polymerase (PARP) in vitro. FASEB J. 18 (2004) 690-692
6. Starckx S., Van den Steen P.E., Verbeek R., van Noort J.M., and Opdenakker G. A novel rationale for inhibition of gelatinase B in multiple sclerosis: MMP-9 destroys alpha B-crystallin and generates a promiscuous T cell epitope. J. Neuroimmunol. 141 (2003) 47-57
7. Descamps F.J., Martens E., Proost P., Starckx S., Van den Steen P.E., Van Damme J., and Opdenakker G. Gelatinase B/matrix metalloproteinase-9 provokes cataract by cleaving lens betaB1 crystallin. FASEB J. 19 (2005) 29-35
8. Ousman S.S., Tomooka B.H., van Noort J.M., Wawrousek E.F., O'Connor K.C., Hafler D.A., Sobel R.A., Robinson W.H., and Steinman L. Protective and therapeutic role for alphaB-crystallin in autoimmune demyelination. Nature 448 (2007) 474-479
9. Masure S., Proost P., Van Damme J., and Opdenakker G. Purification and identification of 91-kDa neutrophil gelatinase. Release by the activating peptide interleukin-8. Eur. J. Biochem. 198 (1991) 391-398
10. Van den Steen P.E., Van Aelst I., Hvidberg V., Piccard H., Fiten P., Jacobsen C., Moestrup S.K., Fry S., Royle L., Wormald M.R., Wallis R., Rudd P.M., Dwek R.A., and Opdenakker G. The hemopexin and O-glycosylated domains tune gelatinase B/MMP-9 bioavailability via inhibition and binding to cargo receptors. J. Biol. Chem. 281 (2006) 18626-18637
11. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
12. Descamps F.J., Martens E., and Opdenakker G. Analysis of gelatinases in complex biological fluids and tissue extracts. Lab. Invest. 82 (2002) 1607-1608
13. Hubberstey A.V., and Mottillo E.P. Cyclase-associated proteins: CAPacity for linking signal transduction and actin polymerization. FASEB J. 16 (2002) 487-499
14. Overall C.M., McQuibban G.A., and Clark-Lewis I. Discovery of chemokine substrates for matrix metalloproteinases by exosite scanning: a new tool for degradomics. Biol. Chem. 383 (2002) 1059-1066
15. Piccard H., Van den Steen P.E., and Opdenakker G. Hemopexin domains as multifunctional liganding modules in matrix metalloproteinases and other proteins. J. Leukoc. Biol. 81 (2007) 870-892
16. Frampton G., Moriya S., Pearson J.D., Isenberg D.A., Ward F.J., Smith T.A., Panayiotou A., Staines N.A., and Murphy J.J. Identification of candidate endothelial cell autoantigens in systemic lupus erythematosus using a molecular cloning strategy: a role for ribosomal P protein P0 as an endothelial cell autoantigen. Rheumatology 39 (2000) 1114-1120
17. Kinloch A., Tatzer V., Wait R., Peston D., Lundberg K., Donatien P., Moyes D., Taylor P.C., and Venables P.J. Identification of citrullinated alpha-enolase as a candidate autoantigen in rheumatoid arthritis. Arthritis Res. Ther. 7 (2005) R1421-R1429
18. Van den Steen P.E., Dubois B., Nelissen I., Rudd P.M., Dwek R.A., and Opdenakker G. Biochemistry and molecular biology of gelatinase B or matrix metalloproteinase-9 (MMP-9). Crit. Rev. Biochem. Mol. Biol. 37 (2002) 375-536
19. Opdenakker G., Van den Steen P.E., and Van Damme J. Gelatinase B: a tuner and amplifier of immune functions. Trends Immunol. 22 (2001) 571-579
20. Allan J.A., Docherty A.J., Barker P.J., Huskisson N.S., Reynolds J.J., and Murphy G. Binding of gelatinases A and B to type-I collagen and other matrix components. Biochem. J. 309 (1995) 299-306
21. Freeman N.L., Lila T., Mintzer K.A., Chen Z., Pahk A.J., Ren R., Drubin D.G., and Field J. A conserved proline-rich region of the Saccharomyces cerevisiae cyclase-associated protein binds SH3 domains and modulates cytoskeletal localization. Mol. Cell. Biol. 16 (1996) 548-556
22. Yu G., Swiston J., and Young D. Comparison of human CAP and CAP2, homologs of the yeast adenylyl cyclase-associated proteins. J. Cell. Sci. 107 (1994) 1671-1678
23. Peche V., Shekar S., Leichter M., Korte H., Schroder R., Schleicher M., Holak T.A., Clemen C.S., Ramanath Y., Pfitzer G., Karakesisoglou I., and Noegel A.A. CAP2, cyclase-associated protein 2, is a dual compartment protein. Cell. Mol. Life Sci. 64 (2007) 2702-2715
24. Bertling E., Hotulainen P., Mattila P.K., Matilainen T., Salminen M., and Lappalainen P. Cyclase-associated protein 1 (CAP1) promotes cofilin-induced actin dynamics in mammalian nonmuscle cells. Mol. Biol. Cell 15 (2004) 2324-2334
25. Moriyama K., and Yahara I. Human CAP1 is a key factor in the recycling of cofilin and actin for rapid actin turnover. J. Cell Sci. 115 (2002) 1591-1601
26. Tiu R.V., Mountantonakis S.E., Dunbar A.J., and Schreiber Jr. M.J. Tumor lysis syndrome. Semin. Thromb. Hemost. 33 (2007) 397-407
27. Haddad J.G., Harper K.D., Guoth M., Pietra G.G., and Sanger J.W. Angiopathic consequences of saturating the plasma scavenger system for actin. Proc. Natl. Acad. Sci. U. S. A 87 (1990) 1381-1385
28. Dahl B. The extracellular actin scavenger system in trauma and major surgery. Clinical and experimental studies. Acta Orthop. Suppl 76 (2005) 2-24
29. Lee W.M., and Galbraith R.M. The extracellular actin-scavenger system and actin toxicity. N. Engl. J. Med. 326 (1992) 1335-1341
30. Meier U., Gressner O., Lammert F., and Gressner A.M. Gc-globulin: roles in response to injury. Clin. Chem. 52 (2006) 1247-1253
31. Sung M.M., Schulz C.G., Wang W., Sawicki G., Bautista-Lopez N.L., and Schulz R. Matrix metalloproteinase-2 degrades the cytoskeletal protein alpha-actinin in peroxynitrite mediated myocardial injury. J. Mol. Cell. Cardiol. 43 (2007) 429-436
32. Hwang I.K., Park S.M., Kim S.Y., and Lee S.T. A proteomic approach to identify substrates of matrix metalloproteinase-14 in human plasma. Biochim. Biophys. Acta 1702 (2004) 79-87
33. Park S.M., Hwang I.K., Kim S.Y., Lee S.J., Park K.S., and Lee S.T. Characterization of plasma gelsolin as a substrate for matrix metalloproteinases. Proteomics 6 (2006) 1192-1199
34. Rosen A., and Casciola-Rosen L. Autoantigens as substrates for apoptotic proteases: implications for the pathogenesis of systemic autoimmune disease. Cell Death Differ. 6 (1999) 6-12
35. Eggleton P., Haigh R., and Winyard P.G. Consequence of neo-antigenicity of the 'altered self'. Rheumatology (Oxford) 47 (2008) 567-571