DIRECT ACTIVATION OF HUMAN NEUTROPHIL PROCOLLAGENASE BY RECOMBINANT STROMELYSIN

KNAUPER V, WILHELM SM, SEPERACK PK, DECLERCK YA, LANGLEY KE, OSTHUES A, Tschesche H (1993)
BIOCHEMICAL JOURNAL 295: 581-586.

Download
No fulltext has been uploaded. References only!
Journal Article | Original Article | Published | English

No fulltext has been uploaded

Author
; ; ; ; ; ;
Abstract / Notes
Human neutrophil procollagenase was activated by incubation with recombinant active stromelysin. Activation was achieved by cleavage of the Gly78-Phe79 peptide bond at the end of the propeptide domain in a single-step activation mechanism. In addition, accelerated activation was achieved when N-terminally truncated, latent collagenase (with Phe49 as its N-terminal residue) was incubated with recombinant active stromelysin. Determination of the specific activity of recombinant-stromelysin-activated neutrophil collagenase with dinitrophenyl-octapeptide or type I collagen demonstrated the generation of high specific activity. The specific activity of stromelysin-activated enzyme was considerably higher than that of trypsin- or HgCl2-activated collagenase. Thus human neutrophil collagenase is superactivated, like the homologous fibroblast collagenase [Murphy, Cockett, Stephens, Smith and Docherty (1987) Biochem. J. 248, 265-268]. The occurrence of Phe79 at the N-terminus of the neutrophil collagenase seemed to be critical for superactivation, which is in agreement with data published Suzuki. Enghild, Morodomi, Salvesen and Nagase [(1990) Biochemistry 29. 10261-10270] on fibroblast collagenase.
Publishing Year
ISSN
PUB-ID

Cite this

KNAUPER V, WILHELM SM, SEPERACK PK, et al. DIRECT ACTIVATION OF HUMAN NEUTROPHIL PROCOLLAGENASE BY RECOMBINANT STROMELYSIN. BIOCHEMICAL JOURNAL. 1993;295:581-586.
KNAUPER, V., WILHELM, S. M., SEPERACK, P. K., DECLERCK, Y. A., LANGLEY, K. E., OSTHUES, A., & Tschesche, H. (1993). DIRECT ACTIVATION OF HUMAN NEUTROPHIL PROCOLLAGENASE BY RECOMBINANT STROMELYSIN. BIOCHEMICAL JOURNAL, 295, 581-586.
KNAUPER, V., WILHELM, S. M., SEPERACK, P. K., DECLERCK, Y. A., LANGLEY, K. E., OSTHUES, A., and Tschesche, H. (1993). DIRECT ACTIVATION OF HUMAN NEUTROPHIL PROCOLLAGENASE BY RECOMBINANT STROMELYSIN. BIOCHEMICAL JOURNAL 295, 581-586.
KNAUPER, V., et al., 1993. DIRECT ACTIVATION OF HUMAN NEUTROPHIL PROCOLLAGENASE BY RECOMBINANT STROMELYSIN. BIOCHEMICAL JOURNAL, 295, p 581-586.
V. KNAUPER, et al., “DIRECT ACTIVATION OF HUMAN NEUTROPHIL PROCOLLAGENASE BY RECOMBINANT STROMELYSIN”, BIOCHEMICAL JOURNAL, vol. 295, 1993, pp. 581-586.
KNAUPER, V., WILHELM, S.M., SEPERACK, P.K., DECLERCK, Y.A., LANGLEY, K.E., OSTHUES, A., Tschesche, H.: DIRECT ACTIVATION OF HUMAN NEUTROPHIL PROCOLLAGENASE BY RECOMBINANT STROMELYSIN. BIOCHEMICAL JOURNAL. 295, 581-586 (1993).
KNAUPER, V, WILHELM, SM, SEPERACK, PK, DECLERCK, YA, LANGLEY, KE, OSTHUES, A, and Tschesche, Harald. “DIRECT ACTIVATION OF HUMAN NEUTROPHIL PROCOLLAGENASE BY RECOMBINANT STROMELYSIN”. BIOCHEMICAL JOURNAL 295 (1993): 581-586.
This data publication is cited in the following publications:
This publication cites the following data publications:

71 Citations in Europe PMC

Data provided by Europe PubMed Central.

A matrix metalloproteinase proenzyme activator produced by articular cartilage.
Towle CA, Wright M, Hecht AC, Kuong SJ, Papanicolas LE, Totkovic R, Mankin HJ, Treadwell BV., Biochem Biophys Res Commun 247(2), 1998
PMID: 9642125
Mast cells in bronchiectasis.
Sepper R, Konttinen YT, Kemppinen P, Sorsa T, Eklund KK., Ann Med 30(3), 1998
PMID: 9677018
Matrix metalloproteinases: the clue to intervertebral disc degeneration?
Goupille P, Jayson MI, Valat JP, Freemont AJ., Spine (Phila Pa 1976) 23(14), 1998
PMID: 9682320
Matrix metalloproteinases, tumor necrosis factor and multiple sclerosis: an overview.
Chandler S, Miller KM, Clements JM, Lury J, Corkill D, Anthony DC, Adams SE, Gearing AJ., J Neuroimmunol 72(2), 1997
PMID: 9042108
The proteasome: a macromolecular assembly designed to confine proteolysis to a nanocompartment.
Baumeister W, Cejka Z, Kania M, Seemüller E., Biol Chem 378(3-4), 1997
PMID: 9165062
Highly increased levels of active stromelysin in rheumatoid synovial fluid determined by a selective fluorogenic assay.
Beekman B, van El B, Drijfhout JW, Ronday HK, TeKoppele JM., FEBS Lett 418(3), 1997
PMID: 9428733
Activation of human neutrophil procollagenase by stromelysin 2.
Knäuper V, Murphy G, Tschesche H., Eur J Biochem 235(1-2), 1996
PMID: 8631328
Computational sequence analysis of matrix metalloproteinases.
Sang QA, Douglas DA., J Protein Chem 15(2), 1996
PMID: 8924199
Increased matrix metalloproteinases in the aqueous humor of patients and experimental animals with uveitis.
Di Girolamo N, Verma MJ, McCluskey PJ, Lloyd A, Wakefield D., Curr Eye Res 15(10), 1996
PMID: 8921246
Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease.
Strongin AY, Collier I, Bannikov G, Marmer BL, Grant GA, Goldberg GI., J Biol Chem 270(10), 1995
PMID: 7890645
Rat hepatic lipocytes synthesize and secrete transin (stromelysin) in early primary culture.
Vyas SK, Leyland H, Gentry J, Arthur MJ., Gastroenterology 109(3), 1995
PMID: 7657119
Cellular source, activation and inhibition of dental plaque collagenase.
Sorsa T, Ding YL, Ingman T, Salo T, Westerlund U, Haapasalo M, Tschesche H, Konttinen YT., J Clin Periodontol 22(9), 1995
PMID: 7593702
Stromelysin-1: three-dimensional structure of the inhibited catalytic domain and of the C-truncated proenzyme.
Becker JW, Marcy AI, Rokosz LL, Axel MG, Burbaum JJ, Fitzgerald PM, Cameron PM, Esser CK, Hagmann WK, Hermes JD., Protein Sci 4(10), 1995
PMID: 8535233
Structural implications for the role of the N terminus in the 'superactivation' of collagenases. A crystallographic study.
Reinemer P, Grams F, Huber R, Kleine T, Schnierer S, Piper M, Tschesche H, Bode W., FEBS Lett 338(2), 1994
PMID: 8307185
Neutrophil procollagenase can be activated by stromelysin-2.
Knäuper V, Murphy G, Tschesche H., Ann N Y Acad Sci 732(), 1994
PMID: 7978810

Export

0 Marked Publications

Open Data PUB

Web of Science

View record in Web of Science®

Sources

PMID: 8240261
PubMed | Europe PMC

Search this title in

Google Scholar