Direct Activation of Human Neutrophil Procollagenase by Recombinant Stromelysin

Overview

Journal Biochem J

Specialty Biochemistry

Date 1993 Oct 15

PMID 8240261

Citations 25

Authors

V Knauper

S M Wilhelm

P K Seperack

Y A DeClerck

K E Langley

A Osthues

H Tschesche

Affiliations

Soon will be listed here.

Abstract

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 by Suzuki, Enghild, Morodomi, Salvesen and Nagase [(1990) Biochemistry 29, 10261-10270] on fibroblast collagenase.

Citing Articles

Interleukin-1β triggers matrix metalloprotease-3 expression through p65/RelA activation in melanoma cells.

Nunomura J, Nakano R, Naruke A, Suwabe Y, Nakano M, Yachiku N PLoS One. 2022; 17(11):e0278220.

PMID: 36445856 PMC: 9707762. DOI: 10.1371/journal.pone.0278220.

The Migration of Human Follicular Dendritic Cell-Like Cell Is Facilitated by Matrix Metalloproteinase 3 Expression That Is Mediated through TNF-ERK1/2-AP1 Signaling.

Pak H, Kim Y, Nam B, Lee A, Roh J, Gil M J Immunol Res. 2021; 2021:8483938.

PMID: 34222497 PMC: 8225449. DOI: 10.1155/2021/8483938.

Current Perspectives on the Role of Matrix Metalloproteinases in the Pathogenesis of Basal Cell Carcinoma.

Tampa M, Georgescu S, Mitran M, Mitran C, Matei C, Caruntu A Biomolecules. 2021; 11(6).

PMID: 34204372 PMC: 8235174. DOI: 10.3390/biom11060903.

Comparison of rapid MMP-8 and interleukin-6 point-of-care tests to identify intra-amniotic inflammation/infection and impending preterm delivery in patients with preterm labor and intact membranes.

Chaemsaithong P, Romero R, Docheva N, Chaiyasit N, Bhatti G, Pacora P J Matern Fetal Neonatal Med. 2017; 31(2):228-244.

PMID: 28081646 PMC: 5769687. DOI: 10.1080/14767058.2017.1281904.

Chitosan enriched three-dimensional matrix reduces inflammatory and catabolic mediators production by human chondrocytes.

Oprenyeszk F, Sanchez C, Dubuc J, Maquet V, Henrist C, Compere P PLoS One. 2015; 10(5):e0128362.

PMID: 26020773 PMC: 4447380. DOI: 10.1371/journal.pone.0128362.

References

He C, Wilhelm S, Pentland A, Marmer B, Grant G, Eisen A . Tissue cooperation in a proteolytic cascade activating human interstitial collagenase. Proc Natl Acad Sci U S A. 1989; 86(8):2632-6. PMC: 286971. DOI: 10.1073/pnas.86.8.2632. View

Murphy G, Cockett M, Stephens P, Smith B, Docherty A . Stromelysin is an activator of procollagenase. A study with natural and recombinant enzymes. Biochem J. 1987; 248(1):265-8. PMC: 1148528. DOI: 10.1042/bj2480265. View

Bergmann U, Michaelis J, Oberhoff R, Knauper V, Beckmann R, Tschesche H . Enzyme linked immunosorbent assays (ELISA) for the quantitative determination of human leukocyte collagenase and gelatinase. J Clin Chem Clin Biochem. 1989; 27(6):351-9. DOI: 10.1515/cclm.1989.27.6.351. View

Springman E, Angleton E, Birkedal-Hansen H, Van Wart H . Multiple modes of activation of latent human fibroblast collagenase: evidence for the role of a Cys73 active-site zinc complex in latency and a "cysteine switch" mechanism for activation. Proc Natl Acad Sci U S A. 1990; 87(1):364-8. PMC: 53264. DOI: 10.1073/pnas.87.1.364. View

Knauper V, Kramer S, Reinke H, Tschesche H . Characterization and activation of procollagenase from human polymorphonuclear leucocytes. N-terminal sequence determination of the proenzyme and various proteolytically activated forms. Eur J Biochem. 1990; 189(2):295-300. DOI: 10.1111/j.1432-1033.1990.tb15489.x. View

Hasty K, Pourmotabbed T, Goldberg G, Thompson J, Spinella D, Stevens R . Human neutrophil collagenase. A distinct gene product with homology to other matrix metalloproteinases. J Biol Chem. 1990; 265(20):11421-4. View

Van Wart H, Birkedal-Hansen H . The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family. Proc Natl Acad Sci U S A. 1990; 87(14):5578-82. PMC: 54368. DOI: 10.1073/pnas.87.14.5578. View

Knauper V, Kramer S, Reinke H, Tschesche H . Partial amino acid sequence of human PMN leukocyte procollagenase. Biol Chem Hoppe Seyler. 1990; 371 Suppl:295-304. View

Saari H, Suomalainen K, Lindy O, Konttinen Y, Sorsa T . Activation of latent human neutrophil collagenase by reactive oxygen species and serine proteases. Biochem Biophys Res Commun. 1990; 171(3):979-87. DOI: 10.1016/0006-291x(90)90780-q. View

10.

Suzuki K, Enghild J, Morodomi T, Salvesen G, Nagase H . Mechanisms of activation of tissue procollagenase by matrix metalloproteinase 3 (stromelysin). Biochemistry. 1990; 29(44):10261-70. DOI: 10.1021/bi00496a016. View

11.

Mookhtiar K, Van Wart H . Purification to homogeneity of latent and active 58-kilodalton forms of human neutrophil collagenase. Biochemistry. 1990; 29(47):10620-7. DOI: 10.1021/bi00499a007. View

12.

DeClerck Y, Yean T, Lu H, Ting J, Langley K . Inhibition of autoproteolytic activation of interstitial procollagenase by recombinant metalloproteinase inhibitor MI/TIMP-2. J Biol Chem. 1991; 266(6):3893-9. View

13.

Koklitis P, Murphy G, Sutton C, Angal S . Purification of recombinant human prostromelysin. Studies on heat activation to give high-Mr and low-Mr active forms, and a comparison of recombinant with natural stromelysin activities. Biochem J. 1991; 276 ( Pt 1):217-21. PMC: 1151167. DOI: 10.1042/bj2760217. View

14.

Netzel-Arnett S, Mallya S, Nagase H, Birkedal-Hansen H, Van Wart H . Continuously recording fluorescent assays optimized for five human matrix metalloproteinases. Anal Biochem. 1991; 195(1):86-92. DOI: 10.1016/0003-2697(91)90299-9. View

15.

Blaser J, Knauper V, Osthues A, Reinke H, Tschesche H . Mercurial activation of human polymorphonuclear leucocyte procollagenase. Eur J Biochem. 1991; 202(3):1223-30. DOI: 10.1111/j.1432-1033.1991.tb16494.x. View

16.

Osthues A, Knauper V, Oberhoff R, Reinke H, Tschesche H . Isolation and characterization of tissue inhibitors of metalloproteinases (TIMP-1 and TIMP-2) from human rheumatoid synovial fluid. FEBS Lett. 1992; 296(1):16-20. DOI: 10.1016/0014-5793(92)80393-u. View

17.

Michaelis J, Vissers M, Winterbourn C . Different effects of hypochlorous acid on human neutrophil metalloproteinases: activation of collagenase and inactivation of collagenase and gelatinase. Arch Biochem Biophys. 1992; 292(2):555-62. DOI: 10.1016/0003-9861(92)90030-z. View

18.

Allan J, Hembry R, Angal S, Reynolds J, Murphy G . Binding of latent and high Mr active forms of stromelysin to collagen is mediated by the C-terminal domain. J Cell Sci. 1991; 99 ( Pt 4):789-95. DOI: 10.1242/jcs.99.4.789. View

19.

Ogata Y, Enghild J, Nagase H . Matrix metalloproteinase 3 (stromelysin) activates the precursor for the human matrix metalloproteinase 9. J Biol Chem. 1992; 267(6):3581-4. View

20.

McDonnell J, Hoerrner L, Lark M, Harper C, Dey T, Lobner J . Recombinant human interleukin-1 beta-induced increase in levels of proteoglycans, stromelysin, and leukocytes in rabbit synovial fluid. Arthritis Rheum. 1992; 35(7):799-805. DOI: 10.1002/art.1780350714. View