Leukolysin/MMP25/MT6-MMP: A novel matrix metalloproteinase specifically expressed in the leukocyte lineage

Cell Research

Volumn 9, Issue 4, 1999, Pages 291-303

  Pei, Duanqing ^a  

^a UNIVERSITY OF MINNESOTA   (United States)

Author keywords

Leukocytes; Leukolysin; Matrix Remodeling; MMP; MMP25; MT6 MMP

Indexed keywords

COMPLEMENTARY DNA; ENZYME PRECURSOR; MATRIX METALLOPROTEINASE; MATRIX METALLOPROTEINASE 25;

AMINO ACID SEQUENCE; ANIMAL; ARTICLE; CELL GRANULE; CELL LINE; CELL LINEAGE; CELL STRAIN COS1; CLASSIFICATION; DOG; ENZYMOLOGY; GENETICS; HUMAN; LEUKOCYTE; METABOLISM; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; SEQUENCE HOMOLOGY; SOLUBILITY; TISSUE DISTRIBUTION;

AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; CELL LINE; CELL LINEAGE; COS CELLS; CYTOPLASMIC GRANULES; DNA, COMPLEMENTARY; DOGS; ENZYME PRECURSORS; HUMANS; LEUKOCYTES; MATRIX METALLOPROTEINASES; MATRIX METALLOPROTEINASES, MEMBRANE-ASSOCIATED; MOLECULAR SEQUENCE DATA; SEQUENCE HOMOLOGY, AMINO ACID; SOLUBILITY; TISSUE DISTRIBUTION;

EID: 0033256294     PISSN: 10010602     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.cr.7290028     Document Type: Article

References (27)

1. Woessner JF Jr. Matrix metalloproteinases and their inhibitors in connective tissue remodeling. Faseb J 1991; 5:2145-54.
2. Hahn-Dantona E, N Ramos-DeSimone, J Sipley, H Nagase, DL French, JP Quigley. Activation of proMMP-9 by a plasmin/MMP-3 cascade in a tumor cell model. Regulation by tissue inhibitors of metalloproteinases. Ann N Y Acad Sci 1999; 878:372-87.
3. Woolley DE, ED Harris, Jr CL Mainardi, CE Brinckerhoff. Collagenase immunolocalization in cultures of rheumatoid synovial cells. Science 1978; 200:773-5.
4. Weiss SJ. Tissue destruction by neutrophils [see comments]. N Engl J Med 1989; 320:365-76.
5. Massova I, LP Kotra, R Fridman, S Mobashery. Matrix metalloproteinases: structures, evolution, and diversification. Faseb J 1998; 12:1075-95.
6. Stocker W, F Grams, U Baumann, P Reinemer, FX Gomis-Ruth, DB McKay, W Bode. The metzincins-topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases. Protein Sci 1995; 4:823-40.
7. Nagase H, JF Woessner, Jr. Matrix metalloproteinases. J Biol Chem 1999; 274:21491-4.
8. Van Wart HE, H Birkedal-Hansen. The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family. Proc Natl Acad Sci USA 1999; 87:5578-82.
9. Pei D. CA-MMP: a matrix metalloproteinase with a novel cysteine array, but without the classic cysteine switch(1). FEBS Lett1999; 457:262-70.
10. Muller D, B Quantin, MC Gesnel, R Millon-Collard, J Abecassis, R Breathnach. The collagenase gene family in humans consists of at least four members. Biochem J 1988; 253:187-92.
11. Velasco G, AM Pendas, A Fueyo, V Knauper, G Murphy, C Lopez-Otin. Cloning and characterization of human MMP-23, a new matrix metalloproteinase predominantly expressed in reproductive tissues and lacking conserved domains in other family members. J Biol Chem 1999; 274:4570-6.
12. Pei D, SJ Weiss. Furin-dependent intracellular activation of the human stromelysin-3 zymogen. Nature 1995; 375:244-7.
13. Santavicca M, A Noel, H Angliker, I Stoll, JP Segain, P Anglard, M Chretien, N Seidah, P Basset. Characterization of structural determinants and molecular mechanisms involved in prostromelysin-3 activation by 4-aminophenylmercuric acetate and furin-type convertases. Biochem J 1996; 315:953-8.
14. Steiner DF. The proprotein convertases. Curr Opin Chem Biol 1998; 2:31-9.
15. Sato H, T Takino, Y Okada, J Cao, A Shinagawa, E Yamamoto, M Seiki. A matrix metalloproteinase expressed on the surface of invasive tumour cells [see comments]. Nature 1994; 370:61-5.
16. Takino T, H Sato, A Shinagawa, M Seiki. Identification of the second membrane-type matrix metalloproteinase (MT-MMP-2) gene from a human placenta cDNA library. MT-MMPs form a unique membrane-type subclass in the MMP family. J Biol Chem 1995; 270:23013-20.
17. Will H, B Hinzmann. cDNA sequence and mRNA tissue distribution of a novel human matrix metalloproteinase with a potential transmembrane segment. Eur J Biochem 1995; 231:602-8.
18. Puente XS, AM Pendas, E Llano, G Velasco, C Lopez-Otin. Molecular cloning of a novel membrane-type matrix metalloproteinase from a human breast carcinoma. Cancer Res 1996; 56:944-9.
19. Pei D, J Yi. A high-level mammalian expression system based on the Madin-Darby canine kidney cell line. Protein Expr Purif 1998; 13:277-81.
20. Pei D. Identification and characterization of the fifth membrane-type matrix metalloproteinase MT5-MMP [In Process Citation]. J Biol Chem 1999; 274:8925-32.
21. Lennon G, C Auffray, M Polymeropoulos, MB Soares. The I.M.A.G.E. Consortium: an integrated molecular analysis of genomes and their expression. Genomics 1996; 33:151-2.
22. Kajita M, H Kinoh, N Ito, A Takamura, Y Itoh, A Okada, H Sato, M Seiki. Human membrane type-4 matrix metalloproteinase (MT4-MMP) is encoded by a novel major transcript: isolation of complementary DNA clones for human and mouse mt4-mmp transcripts. FEBS Lett 1999; 457:353-6.
23. Llano E, AM Pendas, JP Freije, A Nakano, V Knauper, G Murphy, C Lopez-Otin. Identification and characterization of human MT5-MMP, a new membrane-bound activator of progelatinase a overexpressed in brain tumors. Cancer Res 1999; 59:2570-6.
24. Nagase H. Activation mechanisms of matrix metalloproteinases. Biol Chem 1997; 378:151-60.
25. Pei D, SJ Weiss. Transmembrane-deletion mutants of the membrane-type matrix metalloproteinase-1 process progelatinase A and express intrinsic matrix-degrading activity. J Biol Chem 1996; 271:9135-40.
26. Hasty KA, TF Pourmotabbed, GI Goldberg, JP Thompson, DG Spinella, RM Stevens, CL Mainardi. Human neutrophil collagenase. A distinct gene product with homology to other matrix metalloproteinases. J Biol Chem 1990; 265:11421-4.
27. Hibbs MS, KA Hasty, JM Seyer, AH Kang, CL Mainardi. Biochemical and immunological characterization of the secreted forms of human neutrophil gelatinase. J Biol Chem 1985; 260:2493-500.