Clinical relevance of matrix metalloproteinase-13 determined with a new highly specific and sensitive ELISA in ascitic fluid of advanced ovarian carcinoma patients

Hantke B, Harbeck N, Schmalfeldt B, Claes I, Hiller O, Luther MO, Welk A, Kuhn W, Schmitt M, Tschesche H, Muehlenweg B (2003)
BIOLOGICAL CHEMISTRY 384(8): 1247-1251.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
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Autor*in
Hantke, B; Harbeck, N; Schmalfeldt, B; Claes, I; Hiller, O; Luther, MO; Welk, A; Kuhn, W; Schmitt, M; Tschesche, HaraldUniBi; Muehlenweg, B
Abstract / Bemerkung
Matrix metalloproteinases (MMPs) are involved in many physiological and pathophysiological processes, including tumor cell invasion and metastasis. For one member of this family, MMP-13 (collagenase-3), a new, highly specific ELISA with a sensitivity of 0.5 ng MMP-13/ml was established. The protein levels of MMP-13 in ascitic fluids of 30 patients with advanced ovarian cancer FIGO stage III (n=19) and IV (n=11) were measured with this ELISA. Using a cutoff value of 0.5 ng MMP-13/mg total protein, two patient subpopulations with short (median 16 months) and long (median 36 months) overall survival were identified. Together with other prognostic markers, determination of MMP-13 in ascitic fluid may help to identify patients at risk for early death and help to individualize adjuvant therapy.
Stichworte
collagenase-3; cancer; prognosis
Erscheinungsjahr
2003
Zeitschriftentitel
BIOLOGICAL CHEMISTRY
Band
384
Ausgabe
8
Seite(n)
1247-1251
ISSN
1431-6730
Page URI
https://pub.uni-bielefeld.de/record/1610443

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Hantke B, Harbeck N, Schmalfeldt B, et al. Clinical relevance of matrix metalloproteinase-13 determined with a new highly specific and sensitive ELISA in ascitic fluid of advanced ovarian carcinoma patients. BIOLOGICAL CHEMISTRY. 2003;384(8):1247-1251.
Hantke, B., Harbeck, N., Schmalfeldt, B., Claes, I., Hiller, O., Luther, M. O., Welk, A., et al. (2003). Clinical relevance of matrix metalloproteinase-13 determined with a new highly specific and sensitive ELISA in ascitic fluid of advanced ovarian carcinoma patients. BIOLOGICAL CHEMISTRY, 384(8), 1247-1251. https://doi.org/10.1515/BC.2003.137
Hantke, B, Harbeck, N, Schmalfeldt, B, Claes, I, Hiller, O, Luther, MO, Welk, A, et al. 2003. “Clinical relevance of matrix metalloproteinase-13 determined with a new highly specific and sensitive ELISA in ascitic fluid of advanced ovarian carcinoma patients”. BIOLOGICAL CHEMISTRY 384 (8): 1247-1251.
Hantke, B., Harbeck, N., Schmalfeldt, B., Claes, I., Hiller, O., Luther, M. O., Welk, A., Kuhn, W., Schmitt, M., Tschesche, H., et al. (2003). Clinical relevance of matrix metalloproteinase-13 determined with a new highly specific and sensitive ELISA in ascitic fluid of advanced ovarian carcinoma patients. BIOLOGICAL CHEMISTRY 384, 1247-1251.
Hantke, B., et al., 2003. Clinical relevance of matrix metalloproteinase-13 determined with a new highly specific and sensitive ELISA in ascitic fluid of advanced ovarian carcinoma patients. BIOLOGICAL CHEMISTRY, 384(8), p 1247-1251.
B. Hantke, et al., “Clinical relevance of matrix metalloproteinase-13 determined with a new highly specific and sensitive ELISA in ascitic fluid of advanced ovarian carcinoma patients”, BIOLOGICAL CHEMISTRY, vol. 384, 2003, pp. 1247-1251.
Hantke, B., Harbeck, N., Schmalfeldt, B., Claes, I., Hiller, O., Luther, M.O., Welk, A., Kuhn, W., Schmitt, M., Tschesche, H., Muehlenweg, B.: Clinical relevance of matrix metalloproteinase-13 determined with a new highly specific and sensitive ELISA in ascitic fluid of advanced ovarian carcinoma patients. BIOLOGICAL CHEMISTRY. 384, 1247-1251 (2003).
Hantke, B, Harbeck, N, Schmalfeldt, B, Claes, I, Hiller, O, Luther, MO, Welk, A, Kuhn, W, Schmitt, M, Tschesche, Harald, and Muehlenweg, B. “Clinical relevance of matrix metalloproteinase-13 determined with a new highly specific and sensitive ELISA in ascitic fluid of advanced ovarian carcinoma patients”. BIOLOGICAL CHEMISTRY 384.8 (2003): 1247-1251.

5 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

The Long Noncoding RNA MALAT-1 Is Highly Expressed in Ovarian Cancer and Induces Cell Growth and Migration.
Zhou Y, Xu X, Lv H, Wen Q, Li J, Tan L, Li J, Sheng X., PLoS One 11(5), 2016
PMID: 27227769
Ovarian cancer: involvement of the matrix metalloproteinases.
Al-Alem L, Curry TE., Reproduction 150(2), 2015
PMID: 25918438
Inhibition of RUNX2 transcriptional activity blocks the proliferation, migration and invasion of epithelial ovarian carcinoma cells.
Wang ZQ, Keita M, Bachvarova M, Gobeil S, Morin C, Plante M, Gregoire J, Renaud MC, Sebastianelli A, Trinh XB, Bachvarov D., PLoS One 8(10), 2013
PMID: 24124450
CCL25-CCR9 interaction modulates ovarian cancer cell migration, metalloproteinase expression, and invasion.
Johnson EL, Singh R, Singh S, Johnson-Holiday CM, Grizzle WE, Partridge EE, Lillard JW., World J Surg Oncol 8(), 2010
PMID: 20649989

28 References

Daten bereitgestellt von Europe PubMed Central.

Human keratinocyte cell lines differ in the expression of the collagenolytic matrix metalloproteinases-1,-8, and -13 and of TIMP-1.
Bachmeier BE, Nerlich AG, Boukamp P, Lichtinghagen R, Tschesche H, Fritz H, Fink E., Biol. Chem. 381(5-6), 2000
PMID: 10937883
Matrix metalloproteinases: a review.
Birkedal-Hansen H, Moore WG, Bodden MK, Windsor LJ, Birkedal-Hansen B, DeCarlo A, Engler JA., Crit. Rev. Oral Biol. Med. 4(2), 1993
PMID: 8435466
Increased expression of collagenase-3 (MMP-13) and MT1-MMP in oesophageal cancer is related to cancer aggressiveness.
Etoh T, Inoue H, Yoshikawa Y, Barnard GF, Kitano S, Mori M., Gut 47(1), 2000
PMID: 10861264
Matrix metalloproteinases in cancer invasion, metastasis and angiogenesis.
Foda HD, Zucker S., Drug Discov. Today 6(9), 2001
PMID: 11344033
Molecular cloning and expression of collagenase-3, a novel human matrix metalloproteinase produced by breast carcinomas.
Freije JM, Diez-Itza I, Balbin M, Sanchez LM, Blasco R, Tolivia J, Lopez-Otin C., J. Biol. Chem. 269(24), 1994
PMID: 8207000
Influence of flavonoids and vitamins on the MMP- and TIMP-expression of human dermal fibroblasts after UVA irradiation.
Hantke B, Lahmann C, Venzke K, Fischer T, Kocourek A, Windsor LJ, Bergemann J, Stab F, Tschesche H., Photochem. Photobiol. Sci. 1(10), 2002
PMID: 12656486
The collagen substrate specificity of human neutrophil collagenase.
Hasty KA, Jeffrey JJ, Hibbs MS, Welgus HG., J. Biol. Chem. 262(21), 1987
PMID: 3038863
High levels of expression of collagenase-3 (MMP-13) in pathological conditions associated with a foreign-body reaction.
Imai S, Konttinen YT, Jumppanen M, Lindy O, Ceponis A, Kemppinen P, Sorsa T, Santavirta S, Xu JW, Lopez-Otin C., J Bone Joint Surg Br 80(4), 1998
PMID: 9699841
Collagenase-3 (MMP-13) is expressed by hypertrophic chondrocytes, periosteal cells, and osteoblasts during human fetal bone development.
Johansson N, Saarialho-Kere U, Airola K, Herva R, Nissinen L, Westermarck J, Vuorio E, Heino J, Kahari VM., Dev. Dyn. 208(3), 1997
PMID: 9056642
Expression of collagenase-3 (MMP-13) by tumor cells in squamous cell carcinomas of the head and neck.
Kahari VM, Johansson N, Grenman R, Airola K, Saarialho-Kere U., Adv. Exp. Med. Biol. 451(), 1998
PMID: 10026851
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
Protein measurement with the Folin phenol reagent.
LOWRY OH, ROSEBROUGH NJ, FARR AL, RANDALL RJ., J. Biol. Chem. 193(1), 1951
PMID: 14907713
Cloning, expression, and type II collagenolytic activity of matrix metalloproteinase-13 from human osteoarthritic cartilage.
Mitchell PG, Magna HA, Reeves LM, Lopresti-Morrow LL, Yocum SA, Rosner PJ, Geoghegan KF, Hambor JE., J. Clin. Invest. 97(3), 1996
PMID: 8609233
Collagenase-3 expression in breast myofibroblasts as a molecular marker of transition of ductal carcinoma in situ lesions to invasive ductal carcinomas.
Nielsen BS, Rank F, Lopez JM, Balbin M, Vizoso F, Lund LR, Dano K, Lopez-Otin C., Cancer Res. 61(19), 2001
PMID: 11585740
CD87-positive tumor cells in bone marrow aspirates identified by confocal laser scanning fluorescence microscopy.
Noack F, Helmecke D, Rosenberg R, Thorban S, Nekarda H, Fink U, Lewald J, Stich M, Schutze K, Harbeck N, Magdolen V, Graeff H, Schmitt M., Int. J. Oncol. 15(4), 1999
PMID: 10493940
Molecular cloning of a novel membrane-type matrix metalloproteinase from a human breast carcinoma.
Puente XS, Pendas AM, Llano E, Velasco G, Lopez-Otin C., Cancer Res. 56(5), 1996
PMID: 8640782
Patterns of matrix metalloproteinase and TIMP expression in chronic ulcers.
Saarialho-Kere UK., Arch. Dermatol. Res. 290 Suppl(), 1998
PMID: 9710383
Primary tumor and metastasis in ovarian cancer differ in their content of urokinase-type plasminogen activator, its receptor, and inhibitors types 1 and 2.
Schmalfeldt B, Kuhn W, Reuning U, Pache L, Dettmar P, Schmitt M, Janicke F, Hofler H, Graeff H., Cancer Res. 55(18), 1995
PMID: 7664262
Increased expression of matrix metalloproteinases (MMP)-2, MMP-9, and the urokinase-type plasminogen activator is associated with progression from benign to advanced ovarian cancer.
Schmalfeldt B, Prechtel D, Harting K, Spathe K, Rutke S, Konik E, Fridman R, Berger U, Schmitt M, Kuhn W, Lengyel E., Clin. Cancer Res. 7(8), 2001
PMID: 11489818

AUTHOR UNKNOWN, 0
Matrix metalloproteinases in tumor invasion and metastasis.
Stamenkovic I., Semin. Cancer Biol. 10(6), 2000
PMID: 11170864
How matrix metalloproteinases regulate cell behavior.
Sternlicht MD, Werb Z., Annu. Rev. Cell Dev. Biol. 17(), 2001
PMID: 11687497

Tamei, Connective Tissue 30(), 1998

Tschesche, J. Prot. Chem. 17(), 1998
Cloning of collagenase 3 from the synovial membrane and its expression in rheumatoid arthritis and osteoarthritis.
Wernicke D, Seyfert C, Hinzmann B, Gromnica-Ihle E., J. Rheumatol. 23(4), 1996
PMID: 8730110
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