Legumain and cathepsin-L expression in human unstable carotid plaque

Atherosclerosis

Volumn 208, Issue 1, 2010, Pages 83-89

  Mattock, K L ^a   Gough, P J ^b   Humphries, J ^a   Burnand, K ^a   Patel, L ^c   Suckling, K E ^c   Cuello, F ^a   Watts, C ^d   Gautel, M ^a   Avkiran, M ^a   Smith, A ^a  

^a KING'S COLLEGE LONDON   (United Kingdom)

^b GLAXOSMITHKLINE   (United States)

^c GLAXOSMITHKLINE   (United Kingdom)

^d UNIVERSITY OF DUNDEE   (United Kingdom)

Author keywords

Atherosclerosis; Carotid artery; Macrophages; Proteases; RGD

Indexed keywords

ARGINYLGLYCYLASPARTIC ACID; CATHEPSIN L; LEGUMAIN;

ADENOVIRUS; ARTICLE; ATHEROSCLEROTIC PLAQUE; CAROTID ARTERY DISEASE; CELL LINE; CELLULAR DISTRIBUTION; CONTROLLED STUDY; DENSITOMETRY; ENZYME LINKED IMMUNOSORBENT ASSAY; GENE OVEREXPRESSION; HUMAN; HUMAN CELL; IMMUNOHISTOCHEMISTRY; IMMUNOHISTOLOGY; MACROPHAGE; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN LOCALIZATION; UPREGULATION; VIRUS RECOMBINATION; WESTERN BLOTTING;

CAROTID ARTERY DISEASES; CATHEPSIN L; CYSTEINE ENDOPEPTIDASES; HUMANS;

EID: 73449137515     PISSN: 00219150     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.atherosclerosis.2009.07.022     Document Type: Article

References (34)

1. Papaspyridonos M., Smith A., Burnand K.G., et al. Novel candidate genes in unstable areas of human atherosclerotic plaques. Arterioscler Thromb Vasc Biol 26 (2006) 1837-1844
2. Clerin V., Shih H.H., Deng N., et al. Expression of the cysteine protease legumain in vascular lesions and functional implications in atherogenesis. Atherosclerosis 201 (2008) 53-66
3. Lecaille F., Muno D., Kominami E., and Ishidoh K. Proteinases participating in the processing and activation of prolegumain in primary cultured rat macrophages. Biol Chem 385 (2004) 511-516
4. Hashimoto S., Suzuki T., Dong H.Y., Yamazaki N., and Matsushima K. Serial analysis of gene expression in human monocytes and macrophages. Blood 94 (1999) 837-844
5. Watts C., Matthews S.P., Mazzeo D., Manoury B., and Moss C.X. Asparaginyl endopeptidase: case history of a class II MHC compartment protease. Immunol Rev 207 (2005) 218-228
6. Shirahama-Noda K., Yamamoto A., Sugihara K., et al. Biosynthetic processing of cathepsins and lysosomal degradation are abolished in asparaginyl endopeptidase-deficient mice. J Biol Chem 278 (2003) 33194-33199
7. Liu C., Sun C., Huang H., Janda K., and Edgington T. Overexpression of legumain in tumors is significant for invasion/metastasis and a candidate enzymatic target for prodrug therapy. Cancer Res 63 (2003) 2957-2964
8. Murthy R.V., Arbman G., Gao J., Roodman G.D., and Sun X.F. Legumain expression in relation to clinicopathologic and biological variables in colorectal cancer. Clin Cancer Res 11 (2005) 2293-2299
9. Li W., Kornmark L., Jonasson L., Forssell C., and Yuan X.M. Cathepsin L is significantly associated with apoptosis and plaque destabilization in human atherosclerosis. Atherosclerosis 202 (2009) 92-102
10. Liu J., Sukhova G.K., Yang J.T., et al. Cathepsin L expression and regulation in human abdominal aortic aneurysm, atherosclerosis, and vascular cells. Atherosclerosis 184 (2006) 302-311
11. Kitamoto S., Sukhova G.K., Sun J., et al. L deficiency reduces diet-induced atherosclerosis in low-density lipoprotein receptor-knockout mice. Circulation 115 (2007) 2065-2075
12. Li D.N., Matthews S.P., Antoniou A.N., Mazzeo D., and Watts C. Multistep autoactivation of asparaginyl endopeptidase in vitro and in vivo. J Biol Chem 278 (2003) 38980-38990
13. Johansen H.T., Knight C.G., and Barrett A.J. Colorimetric and fluorimetric microplate assays for legumain and a staining reaction for detection of the enzyme after electrophoresis. Anal Biochem 273 (1999) 278-283
14. Maehr R., Hang H.C., Mintern J.D., et al. Asparagine endopeptidase is not essential for class II MHC antigen presentation but is required for processing of cathepsin L in mice. J Immunol 174 (2005) 7066-7074
15. Morita Y., Araki H., Sugimoto T., et al. Legumain/asparaginyl endopeptidase controls extracellular matrix remodeling through the degradation of fibronectin in mouse renal proximal tubular cells. FEBS Lett 581 (2007) 1417-1424
16. Reddy V.Y., Zhang Q.Y., and Weiss S.J. Pericellular mobilization of the tissue-destructive cysteine proteinases, cathepsins B, L, and S, by human monocyte-derived macrophages. Proc Natl Acad Sci U S A 92 (1995) 3849-3853
17. Naghavi M., John R., Naguib S., et al. pH heterogeneity of human and rabbit atherosclerotic plaques; a new insight into detection of vulnerable plaque. Atherosclerosis 164 (2002) 27-35
18. Khan T., Soller B., Naghavi M., and Casscells W. Tissue pH determination for the detection of metabolically active, inflamed vulnerable plaques using near-infrared spectroscopy: an in-vitro feasibility study. Cardiology 103 (2005) 10-16
19. Lusson J., Benjannet S., Hamelin J., et al. The integrity of the RRGDL sequence of the proprotein convertase PC1 is critical for its zymogen and C-terminal processing and for its cellular trafficking. Biochem J 326 Pt 3 (1997) 737-744
20. Kubota K., Wakabayashi K., and Matsuoka T. Proteome analysis of secreted proteins during osteoclast differentiation using two different methods: two-dimensional electrophoresis and isotope-coded affinity tags analysis with two-dimensional chromatography. Proteomics 3 (2003) 616-626
21. Choi S.J., Kurihara N., Oba Y., and Roodman G.D. Osteoclast inhibitory peptide 2 inhibits osteoclast formation via its C-terminal fragment. J Bone Miner Res 16 (2001) 1804-1811
22. Chen J.M., Fortunato M., Stevens R.A., and Barrett A.J. Activation of progelatinase A by mammalian legumain, a recently discovered cysteine proteinase. Biol Chem 382 (2001) 777-783
23. Lutgens S.P., Cleutjens K.B., Daemen M.J., and Heeneman S. Cathepsin cysteine proteases in cardiovascular disease. FASEB J 21 (2007) 3029-3041
24. Newby A.C. Metalloproteinases and vulnerable atherosclerotic plaques. Trends Cardiovasc Med 17 (2007) 253-258
25. Nepal R.M., Mampe S., Shaffer B., Erickson A.H., and Bryant P. Cathepsin L maturation and activity is impaired in macrophages harboring M. avium and M. tuberculosis. Int Immunol 18 (2006) 931-939
26. Li Z., Yasuda Y., Li W., et al. Regulation of collagenase activities of human cathepsins by glycosaminoglycans. J Biol Chem 279 (2004) 5470-5479
27. Platt M.O., Ankeny R.F., and Jo H. Laminar shear stress inhibits cathepsin L activity in endothelial cells. Arterioscler Thromb Vasc Biol 26 (2006) 1784-1790
28. Chen J.M., Dando P.M., Rawlings N.D., et al. Cloning, isolation, and characterization of mammalian legumain, an asparaginyl endopeptidase. J Biol Chem 272 (1997) 8090-8098
29. Chen J.M., Dando P.M., Stevens R.A., Fortunato M., and Barrett A.J. Cloning and expression of mouse legumain, a lysosomal endopeptidase. Biochem J 335 Pt 1 (1998) 111-117
30. Ishidoh K., Saido T.C., Kawashima S., et al. Multiple processing of procathepsin L to cathepsin L in vivo. Biochem Biophys Res Commun 252 (1998) 202-207
31. Lennon-Dumenil A.M., Roberts R.A., Valentijn K., et al. The p41 isoform of invariant chain is a chaperone for cathepsin L. EMBO J 20 (2001) 4055-4064
32. Clarke M., Bennett M., and Littlewood T. Cell death in the cardiovascular system. Heart 93 (2007) 659-664
33. Urbich C., Heeschen C., Aicher A., et al. Cathepsin L is required for endothelial progenitor cell-induced neovascularization. Nat Med 11 (2005) 206-213
34. Ribatti D., Levi-Schaffer F., and Kovanen P.T. Inflammatory angiogenesis in atherogenesis-a double-edged sword. Ann Med 40 (2008) 606-621