Activation of type IV procollagenases by human tumor-associated trypsin-2

Sorsa T, Salo T, Koivunen E, Tyynela J, Konttinen YT, Bergmann U, Tuuttila A, Niemi E, Teronen O, Heikkila P, Tschesche H, et al. (1997)
JOURNAL OF BIOLOGICAL CHEMISTRY 272(34): 21067-21074.

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

No fulltext has been uploaded

Author
; ; ; ; ; ; ; ; ; ; ;
All
Abstract
Increased production of proteinases, such as matrix metalloproteinases (MMPs), is a characteristic feature of malignant tumors. Some human cancers :Ind cell lines derived from them also express trypsinogen, but the function of the extrapancreatic trypsin has remained unclear, In this study we cloned and sequenced trypsinogen-a cDNA from human COLO 205 colon carcinoma cells and characterized the ability of the enzyme to activate latent human type TV procollagenases (proMMP-2 and proMMP-9). As shown by cloning and N-terminal amino acid sequencing, the amino acid sequence of tumor associated trypsin-a is identical to that of pancreatic trypsin-a. We found that both pancreatic trypsin-a and tumor cell-derived trypsin-a are efficient activators of proMMP-9 and are capable of activating proMMP-9 at a molar ratio of 1:1000, the lowest reported so far. Human trypsin-a was a more efficient activator than widely used bovine trypsin and converted the 92-kDa proMMP-9 to a single 77-kDa product that was not fragmented further. The single peptide bond cleaved by trypsin-a in proMMP-9 was Arg(87)-Phe(88), The generation of the 77-kDa species coincided with the increase in specific activity of MMP-9. In contrast, trypsin-2 only partially activated proMMP-2. Trypsin-a cleaved the Arg(99)-Lys(100) peptide bond of proMMP-2 generating 62-65-kDa MMP-2 species. Trypsin-a-induced proMMP-2 and -9 conversions were inhibited by tumor-associated trypsin inhibitor added either prior to or during activation indicating that proMMPs were not activated autocatalytically. Trypsin-2 also activated proMMPs associated with tissue inhibitor of matrix metalloproteinases, the complexes of which are thought to be the major MMP forms in vivo. The ability of human tumor cell-derived trypsin-a to activate latent MMPs suggests a role fbr trypsin-a in initiating the proteinase cascade that mediates tumor invasion and metastasis formation.
Publishing Year
ISSN
PUB-ID

Cite this

Sorsa T, Salo T, Koivunen E, et al. Activation of type IV procollagenases by human tumor-associated trypsin-2. JOURNAL OF BIOLOGICAL CHEMISTRY. 1997;272(34):21067-21074.
Sorsa, T., Salo, T., Koivunen, E., Tyynela, J., Konttinen, Y. T., Bergmann, U., Tuuttila, A., et al. (1997). Activation of type IV procollagenases by human tumor-associated trypsin-2. JOURNAL OF BIOLOGICAL CHEMISTRY, 272(34), 21067-21074. doi:10.1074/jbc.272.34.21067
Sorsa, T., Salo, T., Koivunen, E., Tyynela, J., Konttinen, Y. T., Bergmann, U., Tuuttila, A., Niemi, E., Teronen, O., Heikkila, P., et al. (1997). Activation of type IV procollagenases by human tumor-associated trypsin-2. JOURNAL OF BIOLOGICAL CHEMISTRY 272, 21067-21074.
Sorsa, T., et al., 1997. Activation of type IV procollagenases by human tumor-associated trypsin-2. JOURNAL OF BIOLOGICAL CHEMISTRY, 272(34), p 21067-21074.
T. Sorsa, et al., “Activation of type IV procollagenases by human tumor-associated trypsin-2”, JOURNAL OF BIOLOGICAL CHEMISTRY, vol. 272, 1997, pp. 21067-21074.
Sorsa, T., Salo, T., Koivunen, E., Tyynela, J., Konttinen, Y.T., Bergmann, U., Tuuttila, A., Niemi, E., Teronen, O., Heikkila, P., Tschesche, H., Leinonen, J., Osman, S., Stenman, U.H.: Activation of type IV procollagenases by human tumor-associated trypsin-2. JOURNAL OF BIOLOGICAL CHEMISTRY. 272, 21067-21074 (1997).
Sorsa, T, Salo, T, Koivunen, E, Tyynela, J, Konttinen, YT, Bergmann, U, Tuuttila, A, Niemi, E, Teronen, O, Heikkila, P, Tschesche, Harald, Leinonen, J, Osman, S, and Stenman, UH. “Activation of type IV procollagenases by human tumor-associated trypsin-2”. JOURNAL OF BIOLOGICAL CHEMISTRY 272.34 (1997): 21067-21074.
This data publication is cited in the following publications:
This publication cites the following data publications:

106 Citations in Europe PMC

Data provided by Europe PubMed Central.

Treponema denticola chymotrypsin-like proteinase may contribute to orodigestive carcinogenesis through immunomodulation.
Nieminen MT, Listyarifah D, Hagstrom J, Haglund C, Grenier D, Nordstrom D, Uitto VJ, Hernandez M, Yucel-Lindberg T, Tervahartiala T, Ainola M, Sorsa T., Br. J. Cancer 118(3), 2018
PMID: 29149107
Differential gene expression profiling of endometrium during the mid-luteal phase of the estrous cycle between a repeat breeder (RB) and non-RB cows.
Hayashi KG, Hosoe M, Kizaki K, Fujii S, Kanahara H, Takahashi T, Sakumoto R., Reprod. Biol. Endocrinol. 15(1), 2017
PMID: 28335821
Common Matrix Metalloproteinases (MMP-8, -9, -25, and -26) Cannot Explain Dentigerous Cyst Expansion.
Suojanen J, Lehtonen N, Farkkila E, Hietanen J, Teronen O, Sorsa T, Hagstrom J., J Clin Diagn Res 8(9), 2014
PMID: 25386530
Matrix metalloproteinase-8/collagenase-2 in childhood otitis media with effusion.
Lauhio A, Rezes S, Tervahartiala T, Sziklai I, Pitkaranta A, Sorsa T., Ann. Med. 44(1), 2012
PMID: 21047154
Specific monoclonal antibody against human trypsin.
Acosta Bas C, Baluja Conde IB, Brito Moreno AI, Rodriguez Lopez MR, Melchor A, Hernandez L, Frometa A., Hybrid. Hybridomics 21(4), 2002
PMID: 12193285

Export

0 Marked Publications

Open Data PUB

Web of Science

View record in Web of Science®

Sources

PMID: 9261109
PubMed | Europe PMC

Search this title in

Google Scholar