Catalytic- and ecto-domains of membrane type 1-matrix metalloproteinase have similar inhibition profiles but distinct endopeptidase activities

Hurst DR, Schwartz MA, Ghaffari MA, Jin YH, Tschesche H, Fields GB, Sang QXA (2004)
BIOCHEMICAL JOURNAL 377: 775-779.

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Zeitschriftenaufsatz | Veröffentlicht | Englisch
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Abstract / Bemerkung
Membrane type 1-matrix metalloproteinase (MT1-MMP/MMP-14) is a major collagenolytic enzyme that plays a vital role in development and morphogenesis. To elucidate further the structure-function relationship between the human MT1-MMP active site and the influence of the haemopexin domain on catalysis, substrate specificity and inhibition kinetics of the cdMT1-MMP (catalytic domain of MT1-MMP) and the ecto domain DeltaTM-MT1-MMP (transmembrane-domain-deleted MT1-MMP) were compared. For substrate 1 [Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2, where Mca stands for (7-methoxycoumarin-4-yl)acetyl- and Dpa for N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl], the activation energy E-a was determined to be 11.2 and 12.2 kcal/mol (1 cal = 4.184 J) for cdMT1-MMP and DeltaTM-MT1-MMP respectively, which is consistent with k(cat)/K-M values of 7.37 and 1.46 x 10(4) M-1. s(-1). The k(cat)/K-M values for a series of similar single-stranded peptide substrates were determined and found to correlate with a slope of 0.17 for the two enzyme forms. A triple-helical peptide substrate was predicted to have a k(cat)/K-M of 0.87 x 10(4) M-1 . s(-1) for DeltaTM-MT1-MMP based on the value for cdMT1-MMP of 5.12 x 10(4) M-1. s(-1); however, the actual value was determined to be 2.5-fold higher, i.e. 2.18 x 10(4) M-1. s(-1). These results suggest that cdMT1-MMP is catalytically more efficient towards small peptide substrates than ATM-MT1-MMP and the haernopexin domain of MT1-MMP facilitates the hydrolysis of triple-helical substrates. Diastereomeric inhibitor pairs were utilized to probe further binding similarities at the active site. Ratios of K-i values for the inhibitor pairs were found to correlate between the enzyme forms with a slope of 1.03, suggesting that the haernopexin domain does not significantly modify the enzyme active-site structure.
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Zeitschriftentitel
BIOCHEMICAL JOURNAL
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377
Seite
775-779
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Hurst DR, Schwartz MA, Ghaffari MA, et al. Catalytic- and ecto-domains of membrane type 1-matrix metalloproteinase have similar inhibition profiles but distinct endopeptidase activities. BIOCHEMICAL JOURNAL. 2004;377:775-779.
Hurst, D. R., Schwartz, M. A., Ghaffari, M. A., Jin, Y. H., Tschesche, H., Fields, G. B., & Sang, Q. X. A. (2004). Catalytic- and ecto-domains of membrane type 1-matrix metalloproteinase have similar inhibition profiles but distinct endopeptidase activities. BIOCHEMICAL JOURNAL, 377, 775-779.
Hurst, D. R., Schwartz, M. A., Ghaffari, M. A., Jin, Y. H., Tschesche, H., Fields, G. B., and Sang, Q. X. A. (2004). Catalytic- and ecto-domains of membrane type 1-matrix metalloproteinase have similar inhibition profiles but distinct endopeptidase activities. BIOCHEMICAL JOURNAL 377, 775-779.
Hurst, D.R., et al., 2004. Catalytic- and ecto-domains of membrane type 1-matrix metalloproteinase have similar inhibition profiles but distinct endopeptidase activities. BIOCHEMICAL JOURNAL, 377, p 775-779.
D.R. Hurst, et al., “Catalytic- and ecto-domains of membrane type 1-matrix metalloproteinase have similar inhibition profiles but distinct endopeptidase activities”, BIOCHEMICAL JOURNAL, vol. 377, 2004, pp. 775-779.
Hurst, D.R., Schwartz, M.A., Ghaffari, M.A., Jin, Y.H., Tschesche, H., Fields, G.B., Sang, Q.X.A.: Catalytic- and ecto-domains of membrane type 1-matrix metalloproteinase have similar inhibition profiles but distinct endopeptidase activities. BIOCHEMICAL JOURNAL. 377, 775-779 (2004).
Hurst, DR, Schwartz, MA, Ghaffari, MA, Jin, YH, Tschesche, Harald, Fields, GB, and Sang, QXA. “Catalytic- and ecto-domains of membrane type 1-matrix metalloproteinase have similar inhibition profiles but distinct endopeptidase activities”. BIOCHEMICAL JOURNAL 377 (2004): 775-779.

23 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

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PMID: 29643184
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PMID: 28234995
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Cerofolini L, Amar S, Lauer JL, Martelli T, Fragai M, Luchinat C, Fields GB., Sci Rep 6(), 2016
PMID: 27405411
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Gao Y, Amar S, Pahwa S, Fields G, Kodadek T., ACS Comb Sci 17(1), 2015
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PMID: 25897652
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Triple-helical transition state analogues: a new class of selective matrix metalloproteinase inhibitors.
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PMID: 15585827

25 References

Daten bereitgestellt von Europe PubMed Central.

Membrane-type matrix metalloproteinases 1 and 2 exhibit broad-spectrum proteolytic capacities comparable to many matrix metalloproteinases.
d'Ortho MP, Will H, Atkinson S, Butler G, Messent A, Gavrilovic J, Smith B, Timpl R, Zardi L, Murphy G., Eur. J. Biochem. 250(3), 1997
PMID: 9461298
Hydrolysis of triple-helical collagen peptide models by matrix metalloproteinases.
Lauer-Fields JL, Tuzinski KA, Shimokawa K, Nagase H, Fields GB., J. Biol. Chem. 275(18), 2000
PMID: 10788434
Identification and characterization of human endometase (Matrix metalloproteinase-26) from endometrial tumor.
Park HI, Ni J, Gerkema FE, Liu D, Belozerov VE, Sang QX., J. Biol. Chem. 275(27), 2000
PMID: 10801841
Expression of human membrane type 1 matrix metalloproteinase in Pichia pastoris.
Roderfeld M, Buttner FH, Bartnik E, Tschesche H., Protein Expr. Purif. 19(3), 2000
PMID: 10910727
New thiol and sulfodiimine metalloproteinase inhibitors and their effect on human microvascular endothelial cell growth.
Sang QX, Jia MC, Schwartz MA, Jaye MC, Kleinman HK, Ghaffari MA, Luo YL., Biochem. Biophys. Res. Commun. 274(3), 2000
PMID: 10924354
Kinetic analysis of matrix metalloproteinase activity using fluorogenic triple-helical substrates.
Lauer-Fields JL, Broder T, Sritharan T, Chung L, Nagase H, Fields GB., Biochemistry 40(19), 2001
PMID: 11341845
Homophilic complex formation of MT1-MMP facilitates proMMP-2 activation on the cell surface and promotes tumor cell invasion.
Itoh Y, Takamura A, Ito N, Maru Y, Sato H, Suenaga N, Aoki T, Seiki M., EMBO J. 20(17), 2001
PMID: 11532942
Matrix metalloproteinases: they're not just for matrix anymore!
McCawley LJ, Matrisian LM., Curr. Opin. Cell Biol. 13(5), 2001
PMID: 11544020
How matrix metalloproteinases regulate cell behavior.
Sternlicht MD, Werb Z., Annu. Rev. Cell Dev. Biol. 17(), 2001
PMID: 11687497
CD44 directs membrane-type 1 matrix metalloproteinase to lamellipodia by associating with its hemopexin-like domain.
Mori H, Tomari T, Koshikawa N, Kajita M, Itoh Y, Sato H, Tojo H, Yana I, Seiki M., EMBO J. 21(15), 2002
PMID: 12145196
Matrix metalloproteinases and collagen catabolism.
Lauer-Fields JL, Juska D, Fields GB., Biopolymers 66(1), 2002
PMID: 12228918
Peptide substrate specificities and protein cleavage sites of human endometase/matrilysin-2/matrix metalloproteinase-26.
Park HI, Turk BE, Gerkema FE, Cantley LC, Sang QX., J. Biol. Chem. 277(38), 2002
PMID: 12119297
Ellman's reagent: 5,5'-dithiobis(2-nitrobenzoic acid)--a reexamination.
Riddles PW, Blakeley RL, Zerner B., Anal. Biochem. 94(1), 1979
PMID: 37780
A matrix metalloproteinase expressed on the surface of invasive tumour cells.
Sato H, Takino T, Okada Y, Cao J, Shinagawa A, Yamamoto E, Seiki M., Nature 370(6484), 1994
PMID: 8015608
Biochemical characterization of human collagenase-3.
Knauper V, Lopez-Otin C, Smith B, Knight G, Murphy G., J. Biol. Chem. 271(3), 1996
PMID: 8576151
Membrane type 1 matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromolecules.
Ohuchi E, Imai K, Fujii Y, Sato H, Seiki M, Okada Y., J. Biol. Chem. 272(4), 1997
PMID: 8999957

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