Immunological characterization of cell-surface and soluble forms of membrane type 1 matrix metalloproteinase in human breast cancer cells and in fibroblasts
Li H, Bauzon DE, Xu XY, Tschesche H, Cao J, Sang QXA (1998)
MOLECULAR CARCINOGENESIS 22(2): 84-94.
Zeitschriftenaufsatz
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Autor*in
Li, H;
Bauzon, DE;
Xu, XY;
Tschesche, HaraldUniBi;
Cao, J;
Sang, QXA
Einrichtung
Abstract / Bemerkung
Membrane type (MT) 1 matrix metalloproteinase (MMP) activates progelatinase A (pro-MMP-2), a type IV collagenase, on the cell surface of tumors; however, its function in breast cancer progression and metastasis is not fully understood. To examine the expression of MT1-MMP in breast cancer cells and fibroblasts, a specific rabbit antibody (Ab) directed against a unique synthetic peptide derived from the human MT1-MMP catalytic domain was produced, purified, and characterized. This Ab is not likely to cross-react with MT2-, MT3-, or MT4-MMP or any other MMPs. MT1-MMP expression and pro-M M P-2 activation were stimulated by concanavalin A in two human breast carcinoma cell lines (BT549 and MDA-MB-231) and in normal human fetal-lung fibroblasts (HFL-1) and were slightly upregulated by breast cancer cell-fibroblast interactions. Both pro-MT1-MMP in plasma membrane (63.4 kDa) and the soluble forms of the enzyme in culture medium (57.6 and 25-30 kDa) were detected by immunoblot analysis, suggesting that cell-surface MT1-MMP exhibits an active conformation without the removal of its propeptide domain and that the mature enzyme is shed into the medium. In breast cancer cells, MT1-MMP and a recombinant catalytic domain of MT1-MMP were unable to activate pro-matrilysin, indicating that MT1-MMP is not a universal activator of all MMPs. MT1-MMP may play an important role in the invasive growth and spread of breast cancer cells by specifically activating pro-MMP-2 to cleave the connective-tissue barrier. Furthermore, use of the specific Ab may aid in the investigation of the role of MT1-MMP in human tumors. Mel. Carcinog. 22:84-94, 1998. (C) 1998 Wiley-Liss, Inc.
Stichworte
antibody production;
matrilysin;
proteinase processing;
invasion and metastasis;
gelatinase A
Erscheinungsjahr
1998
Zeitschriftentitel
MOLECULAR CARCINOGENESIS
Band
22
Ausgabe
2
Seite(n)
84-94
ISSN
0899-1987
eISSN
1098-2744
Page URI
https://pub.uni-bielefeld.de/record/1625271
Zitieren
Li H, Bauzon DE, Xu XY, Tschesche H, Cao J, Sang QXA. Immunological characterization of cell-surface and soluble forms of membrane type 1 matrix metalloproteinase in human breast cancer cells and in fibroblasts. MOLECULAR CARCINOGENESIS. 1998;22(2):84-94.
Li, H., Bauzon, D. E., Xu, X. Y., Tschesche, H., Cao, J., & Sang, Q. X. A. (1998). Immunological characterization of cell-surface and soluble forms of membrane type 1 matrix metalloproteinase in human breast cancer cells and in fibroblasts. MOLECULAR CARCINOGENESIS, 22(2), 84-94. https://doi.org/10.1002/(SICI)1098-2744(199806)22:2<84::AID-MC3>3.0.CO;2-K
Li, H, Bauzon, DE, Xu, XY, Tschesche, Harald, Cao, J, and Sang, QXA. 1998. “Immunological characterization of cell-surface and soluble forms of membrane type 1 matrix metalloproteinase in human breast cancer cells and in fibroblasts”. MOLECULAR CARCINOGENESIS 22 (2): 84-94.
Li, H., Bauzon, D. E., Xu, X. Y., Tschesche, H., Cao, J., and Sang, Q. X. A. (1998). Immunological characterization of cell-surface and soluble forms of membrane type 1 matrix metalloproteinase in human breast cancer cells and in fibroblasts. MOLECULAR CARCINOGENESIS 22, 84-94.
Li, H., et al., 1998. Immunological characterization of cell-surface and soluble forms of membrane type 1 matrix metalloproteinase in human breast cancer cells and in fibroblasts. MOLECULAR CARCINOGENESIS, 22(2), p 84-94.
H. Li, et al., “Immunological characterization of cell-surface and soluble forms of membrane type 1 matrix metalloproteinase in human breast cancer cells and in fibroblasts”, MOLECULAR CARCINOGENESIS, vol. 22, 1998, pp. 84-94.
Li, H., Bauzon, D.E., Xu, X.Y., Tschesche, H., Cao, J., Sang, Q.X.A.: Immunological characterization of cell-surface and soluble forms of membrane type 1 matrix metalloproteinase in human breast cancer cells and in fibroblasts. MOLECULAR CARCINOGENESIS. 22, 84-94 (1998).
Li, H, Bauzon, DE, Xu, XY, Tschesche, Harald, Cao, J, and Sang, QXA. “Immunological characterization of cell-surface and soluble forms of membrane type 1 matrix metalloproteinase in human breast cancer cells and in fibroblasts”. MOLECULAR CARCINOGENESIS 22.2 (1998): 84-94.
24 Zitationen in Europe PMC
Daten bereitgestellt von Europe PubMed Central.
Reversal of established liver fibrosis by IC-2-engineered mesenchymal stem cell sheets.
Itaba N, Kono Y, Watanabe K, Yokobata T, Oka H, Osaki M, Kakuta H, Morimoto M, Shiota G., Sci Rep 9(1), 2019
PMID: 31048740
Itaba N, Kono Y, Watanabe K, Yokobata T, Oka H, Osaki M, Kakuta H, Morimoto M, Shiota G., Sci Rep 9(1), 2019
PMID: 31048740
Detection of a latent soluble form of membrane type 1 matrix metalloprotease bound with tissue inhibitor of matrix metalloproteinases-2 in periprosthetic tissues and fluids from loose arthroplasty endoprostheses.
Niarakis A, Giannopoulou E, Ravazoula P, Panagiotopoulos E, Zarkadis IK, Aletras AJ., FEBS J 280(24), 2013
PMID: 24112707
Niarakis A, Giannopoulou E, Ravazoula P, Panagiotopoulos E, Zarkadis IK, Aletras AJ., FEBS J 280(24), 2013
PMID: 24112707
The role of matrix metalloproteinases 2 and 9 during rat tongue carcinogenesis induced by 4-nitroquinoline 1-oxide.
Fracalossi AC, Miranda SR, Oshima CT, Franco M, Ribeiro DA., J Mol Histol 41(1), 2010
PMID: 20213142
Fracalossi AC, Miranda SR, Oshima CT, Franco M, Ribeiro DA., J Mol Histol 41(1), 2010
PMID: 20213142
Expression and prognostic role of MMP2, MMP9, MMP13, and MMP14 matrix metalloproteinases in sinonasal and oral malignant melanomas.
Kondratiev S, Gnepp DR, Yakirevich E, Sabo E, Annino DJ, Rebeiz E, Laver NV., Hum Pathol 39(3), 2008
PMID: 18045645
Kondratiev S, Gnepp DR, Yakirevich E, Sabo E, Annino DJ, Rebeiz E, Laver NV., Hum Pathol 39(3), 2008
PMID: 18045645
Association between serum soluble membrane type matrix metalloproteinase-1 (MT1-MMP) levels and bone mineral density, and biochemical markers in postmenopausal women.
Ren XH, Peng XD, Wu XP, Liao EY, Sun ZQ., Clin Chim Acta 390(1-2), 2008
PMID: 18230350
Ren XH, Peng XD, Wu XP, Liao EY, Sun ZQ., Clin Chim Acta 390(1-2), 2008
PMID: 18230350
The inactive 44-kDa processed form of membrane type 1 matrix metalloproteinase (MT1-MMP) enhances proteolytic activity via regulation of endocytosis of active MT1-MMP.
Cho JA, Osenkowski P, Zhao H, Kim S, Toth M, Cole K, Aboukameel A, Saliganan A, Schuger L, Bonfil RD, Fridman R., J Biol Chem 283(25), 2008
PMID: 18413312
Cho JA, Osenkowski P, Zhao H, Kim S, Toth M, Cole K, Aboukameel A, Saliganan A, Schuger L, Bonfil RD, Fridman R., J Biol Chem 283(25), 2008
PMID: 18413312
Matrix metalloproteinases: contribution to pathogenesis, diagnosis and treatment of periodontal inflammation.
Sorsa T, Tjäderhane L, Konttinen YT, Lauhio A, Salo T, Lee HM, Golub LM, Brown DL, Mäntylä P., Ann Med 38(5), 2006
PMID: 16938801
Sorsa T, Tjäderhane L, Konttinen YT, Lauhio A, Salo T, Lee HM, Golub LM, Brown DL, Mäntylä P., Ann Med 38(5), 2006
PMID: 16938801
ERK1/2 and p38 MAP kinase control MMP-2, MT1-MMP, and TIMP action and affect cell migration: a comparison between mesothelioma and mesothelial cells.
Zhong J, Gencay MM, Bubendorf L, Burgess JK, Parson H, Robinson BW, Tamm M, Black JL, Roth M., J Cell Physiol 207(2), 2006
PMID: 16447244
Zhong J, Gencay MM, Bubendorf L, Burgess JK, Parson H, Robinson BW, Tamm M, Black JL, Roth M., J Cell Physiol 207(2), 2006
PMID: 16447244
MT1-MMP shedding involves an ADAM and is independent of its localization in lipid rafts.
Toth M, Sohail A, Mobashery S, Fridman R., Biochem Biophys Res Commun 350(2), 2006
PMID: 17007816
Toth M, Sohail A, Mobashery S, Fridman R., Biochem Biophys Res Commun 350(2), 2006
PMID: 17007816
Spatio-temporal expression of matrix metalloproteinase-26 in human placental trophoblasts and fetal red cells during normal placentation.
Qiu W, Bai SX, Zhao MR, Wu XQ, Zhao YG, Sang QX, Wang YL., Biol Reprod 72(4), 2005
PMID: 15601912
Qiu W, Bai SX, Zhao MR, Wu XQ, Zhao YG, Sang QX, Wang YL., Biol Reprod 72(4), 2005
PMID: 15601912
Matrix metalloproteinases and their tissue inhibitors in aqueous humor of patients with primary open-angle glaucoma, exfoliation syndrome, and exfoliation glaucoma.
Määttä M, Tervahartiala T, Harju M, Airaksinen J, Autio-Harmainen H, Sorsa T., J Glaucoma 14(1), 2005
PMID: 15650607
Määttä M, Tervahartiala T, Harju M, Airaksinen J, Autio-Harmainen H, Sorsa T., J Glaucoma 14(1), 2005
PMID: 15650607
Cleavage at the stem region releases an active ectodomain of the membrane type 1 matrix metalloproteinase.
Toth M, Osenkowski P, Hesek D, Brown S, Meroueh S, Sakr W, Mobashery S, Fridman R., Biochem J 387(pt 2), 2005
PMID: 15560752
Toth M, Osenkowski P, Hesek D, Brown S, Meroueh S, Sakr W, Mobashery S, Fridman R., Biochem J 387(pt 2), 2005
PMID: 15560752
Inhibition of enzyme activity of and cell-mediated substrate cleavage by membrane type 1 matrix metalloproteinase by newly developed mercaptosulphide inhibitors.
Hurst DR, Schwartz MA, Jin Y, Ghaffari MA, Kozarekar P, Cao J, Sang QX., Biochem J 392(pt 3), 2005
PMID: 16026329
Hurst DR, Schwartz MA, Jin Y, Ghaffari MA, Kozarekar P, Cao J, Sang QX., Biochem J 392(pt 3), 2005
PMID: 16026329
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 Y, Tschesche H, Fields GB, Sang QX., Biochem J 377(pt 3), 2004
PMID: 14533979
Hurst DR, Schwartz MA, Ghaffari MA, Jin Y, Tschesche H, Fields GB, Sang QX., Biochem J 377(pt 3), 2004
PMID: 14533979
Processing, shedding, and endocytosis of membrane type 1-matrix metalloproteinase (MT1-MMP).
Osenkowski P, Toth M, Fridman R., J Cell Physiol 200(1), 2004
PMID: 15137052
Osenkowski P, Toth M, Fridman R., J Cell Physiol 200(1), 2004
PMID: 15137052
Vascular cell adhesion molecule 1 (VCAM-1) activation of endothelial cell matrix metalloproteinases: role of reactive oxygen species.
Deem TL, Cook-Mills JM., Blood 104(8), 2004
PMID: 15265790
Deem TL, Cook-Mills JM., Blood 104(8), 2004
PMID: 15265790
Matrix metalloproteinase-26 is expressed in human endometrium but not in endometrial carcinoma.
Isaka K, Nishi H, Nakai H, Nakada T, Feng Li Y, Ebihara Y, Takayama M., Cancer 97(1), 2003
PMID: 12491508
Isaka K, Nishi H, Nakai H, Nakada T, Feng Li Y, Ebihara Y, Takayama M., Cancer 97(1), 2003
PMID: 12491508
TIMP-2 (tissue inhibitor of metalloproteinase-2) regulates MMP-2 (matrix metalloproteinase-2) activity in the extracellular environment after pro-MMP-2 activation by MT1 (membrane type 1)-MMP.
Bernardo MM, Fridman R., Biochem J 374(pt 3), 2003
PMID: 12755684
Bernardo MM, Fridman R., Biochem J 374(pt 3), 2003
PMID: 12755684
Protein engineering and properties of human metalloproteinase and thrombospondin 1.
Wei P, Zhao YG, Zhuang L, Hurst DR, Ruben S, Sang QX., Biochem Biophys Res Commun 293(1), 2002
PMID: 12054626
Wei P, Zhao YG, Zhuang L, Hurst DR, Ruben S, Sang QX., Biochem Biophys Res Commun 293(1), 2002
PMID: 12054626
Soluble membrane-type 1 matrix metalloproteinase (MT1-MMP) and gelatinase A (MMP-2) in induced sputum and bronchoalveolar lavage fluid of human bronchial asthma and bronchiectasis.
Maisi P, Prikk K, Sepper R, Pirilä E, Salo T, Hietanen J, Sorsa T., APMIS 110(11), 2002
PMID: 12588417
Maisi P, Prikk K, Sepper R, Pirilä E, Salo T, Hietanen J, Sorsa T., APMIS 110(11), 2002
PMID: 12588417
Differential roles of TIMP-4 and TIMP-2 in pro-MMP-2 activation by MT1-MMP.
Hernandez-Barrantes S, Shimura Y, Soloway PD, Sang QA, Fridman R., Biochem Biophys Res Commun 281(1), 2001
PMID: 11178970
Hernandez-Barrantes S, Shimura Y, Soloway PD, Sang QA, Fridman R., Biochem Biophys Res Commun 281(1), 2001
PMID: 11178970
Collaborative interactions between neutrophil elastase and metalloproteinases in extracellular matrix degradation in three-dimensional collagen gels.
Zhu Y, Liu X, Sköld CM, Wang H, Kohyama T, Wen FQ, Ertl RF, Rennard SI., Respir Res 2(5), 2001
PMID: 11686900
Zhu Y, Liu X, Sköld CM, Wang H, Kohyama T, Wen FQ, Ertl RF, Rennard SI., Respir Res 2(5), 2001
PMID: 11686900
Calmodulin inhibitors trigger the proteolytic processing of membrane type-1 matrix metalloproteinase, but not its shedding in glioblastoma cells.
Annabi B, Pilorget A, Bousquet-Gagnon N, Gingras D, Béliveau R., Biochem J 359(pt 2), 2001
PMID: 11583578
Annabi B, Pilorget A, Bousquet-Gagnon N, Gingras D, Béliveau R., Biochem J 359(pt 2), 2001
PMID: 11583578
The in vivo expression of the collagenolytic matrix metalloproteinases (MMP-2, -8, -13, and -14) and matrilysin (MMP-7) in adult and localized juvenile periodontitis.
Tervahartiala T, Pirilä E, Ceponis A, Maisi P, Salo T, Tuter G, Kallio P, Törnwall J, Srinivas R, Konttinen YT, Sorsa T., J Dent Res 79(12), 2000
PMID: 11201047
Tervahartiala T, Pirilä E, Ceponis A, Maisi P, Salo T, Tuter G, Kallio P, Törnwall J, Srinivas R, Konttinen YT, Sorsa T., J Dent Res 79(12), 2000
PMID: 11201047
48 References
Daten bereitgestellt von Europe PubMed Central.
Matrisian, Bio Essays 14(), 1992
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
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
Computational sequence analysis of matrix metalloproteinases.
Sang QA, Douglas DA., J. Protein Chem. 15(2), 1996
PMID: 8924199
Sang QA, Douglas DA., J. Protein Chem. 15(2), 1996
PMID: 8924199
Computational sequence analysis of the tissue inhibitor of metalloproteinase family.
Douglas DA, Shi YE, Sang QA., J. Protein Chem. 16(4), 1997
PMID: 9188064
Douglas DA, Shi YE, Sang QA., J. Protein Chem. 16(4), 1997
PMID: 9188064
Tumor cell interactions with the extracellular matrix during invasion and metastasis.
Stetler-Stevenson WG, Aznavoorian S, Liotta LA., Annu. Rev. Cell Biol. 9(), 1993
PMID: 8280471
Stetler-Stevenson WG, Aznavoorian S, Liotta LA., Annu. Rev. Cell Biol. 9(), 1993
PMID: 8280471
Immunohistochemical distribution of type IV collagenase in normal, benign, and malignant breast tissue.
Monteagudo C, Merino MJ, San-Juan J, Liotta LA, Stetler-Stevenson WG., Am. J. Pathol. 136(3), 1990
PMID: 2156430
Monteagudo C, Merino MJ, San-Juan J, Liotta LA, Stetler-Stevenson WG., Am. J. Pathol. 136(3), 1990
PMID: 2156430
Stetler-Stevenson, Invasion Metastasis 14(), 0
Activity of type IV collagenases in benign and malignant breast disease.
Davies B, Miles DW, Happerfield LC, Naylor MS, Bobrow LG, Rubens RD, Balkwill FR., Br. J. Cancer 67(5), 1993
PMID: 8494711
Davies B, Miles DW, Happerfield LC, Naylor MS, Bobrow LG, Rubens RD, Balkwill FR., Br. J. Cancer 67(5), 1993
PMID: 8494711
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
Sato H, Takino T, Okada Y, Cao J, Shinagawa A, Yamamoto E, Seiki M., Nature 370(6484), 1994
PMID: 8015608
Processing of a precursor of 72-kilodalton type IV collagenase/gelatinase A by a recombinant membrane-type 1 matrix metalloproteinase.
Kinoshita T, Sato H, Takino T, Itoh M, Akizawa T, Seiki M., Cancer Res. 56(11), 1996
PMID: 8653693
Kinoshita T, Sato H, Takino T, Itoh M, Akizawa T, Seiki M., Cancer Res. 56(11), 1996
PMID: 8653693
Membrane-type matrix metalloproteinase (MT-MMP) gene is expressed in stromal cells of human colon, breast, and head and neck carcinomas.
Okada A, Bellocq JP, Rouyer N, Chenard MP, Rio MC, Chambon P, Basset P., Proc. Natl. Acad. Sci. U.S.A. 92(7), 1995
PMID: 7708715
Okada A, Bellocq JP, Rouyer N, Chenard MP, Rio MC, Chambon P, Basset P., Proc. Natl. Acad. Sci. U.S.A. 92(7), 1995
PMID: 7708715
Expression of most matrix metalloproteinase family members in breast cancer represents a tumor-induced host response.
Heppner KJ, Matrisian LM, Jensen RA, Rodgers WH., Am. J. Pathol. 149(1), 1996
PMID: 8686751
Heppner KJ, Matrisian LM, Jensen RA, Rodgers WH., Am. J. Pathol. 149(1), 1996
PMID: 8686751
Complex regulation of membrane-type matrix metalloproteinase expression and matrix metalloproteinase-2 activation by concanavalin A in MDA-MB-231 human breast cancer cells.
Yu M, Sato H, Seiki M, Thompson EW., Cancer Res. 55(15), 1995
PMID: 7614461
Yu M, Sato H, Seiki M, Thompson EW., Cancer Res. 55(15), 1995
PMID: 7614461
Transmembrane-deletion mutants of the membrane-type matrix metalloproteinase-1 process progelatinase A and express intrinsic matrix-degrading activity.
Pei D, Weiss SJ., J. Biol. Chem. 271(15), 1996
PMID: 8621565
Pei D, Weiss SJ., J. Biol. Chem. 271(15), 1996
PMID: 8621565
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
Ohuchi E, Imai K, Fujii Y, Sato H, Seiki M, Okada Y., J. Biol. Chem. 272(4), 1997
PMID: 8999957
Cellular mechanisms for human procollagenase-3 (MMP-13) activation. Evidence that MT1-MMP (MMP-14) and gelatinase a (MMP-2) are able to generate active enzyme.
Knauper V, Will H, Lopez-Otin C, Smith B, Atkinson SJ, Stanton H, Hembry RM, Murphy G., J. Biol. Chem. 271(29), 1996
PMID: 8663255
Knauper V, Will H, Lopez-Otin C, Smith B, Atkinson SJ, Stanton H, Hembry RM, Murphy G., J. Biol. Chem. 271(29), 1996
PMID: 8663255
Membrane-type matrix metalloproteinases (MT-MMPs) in tumor metastasis.
Sato H, Seiki M., J. Biochem. 119(2), 1996
PMID: 8882706
Sato H, Seiki M., J. Biochem. 119(2), 1996
PMID: 8882706
Proteolytic and non-proteolytic activation of human neutrophil progelatinase B.
Sang QX, Birkedal-Hansen H, Van Wart HE., Biochim. Biophys. Acta 1251(2), 1995
PMID: 7669817
Sang QX, Birkedal-Hansen H, Van Wart HE., Biochim. Biophys. Acta 1251(2), 1995
PMID: 7669817
Activation of human progelatinase A by collagenase and matrilysin: activation of procollagenase by matrilysin.
Sang QA, Bodden MK, Windsor LJ., J. Protein Chem. 15(3), 1996
PMID: 8804571
Sang QA, Bodden MK, Windsor LJ., J. Protein Chem. 15(3), 1996
PMID: 8804571
Tumor and stromal expression of matrix metalloproteinases and their role in tumor progression.
Crawford HC, Matrisian LM., Invasion Metastasis 14(1-6), 1994
PMID: 7657516
Crawford HC, Matrisian LM., Invasion Metastasis 14(1-6), 1994
PMID: 7657516
Cancer progression and growth: relationship of paracrine and autocrine growth mechanisms to organ preference of metastasis.
Nicolson GL., Exp. Cell Res. 204(2), 1993
PMID: 8382620
Nicolson GL., Exp. Cell Res. 204(2), 1993
PMID: 8382620
Association of MMP-2 activation potential with metastatic progression in human breast cancer cell lines independent of MMP-2 production.
Azzam HS, Arand G, Lippman ME, Thompson EW., J. Natl. Cancer Inst. 85(21), 1993
PMID: 8411260
Azzam HS, Arand G, Lippman ME, Thompson EW., J. Natl. Cancer Inst. 85(21), 1993
PMID: 8411260
Phase separation of integral membrane proteins in Triton X-114 solution.
Bordier C., J. Biol. Chem. 256(4), 1981
PMID: 6257680
Bordier C., J. Biol. Chem. 256(4), 1981
PMID: 6257680
A potential marker protease of invasiveness, seprase, is localized on invadopodia of human malignant melanoma cells.
Monsky WL, Lin CY, Aoyama A, Kelly T, Akiyama SK, Mueller SC, Chen WT., Cancer Res. 54(21), 1994
PMID: 7923219
Monsky WL, Lin CY, Aoyama A, Kelly T, Akiyama SK, Mueller SC, Chen WT., Cancer Res. 54(21), 1994
PMID: 7923219
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
Puente XS, Pendas AM, Llano E, Velasco G, Lopez-Otin C., Cancer Res. 56(5), 1996
PMID: 8640782
Harlow, 1988
Identification, developmental regulation, and response to heat shock of two antigenically related forms of a major nuclear envelope protein in Drosophila embryos: application of an improved method for affinity purification of antibodies using polypeptides immobilized on nitrocellulose blots.
Smith DE, Fisher PA., J. Cell Biol. 99(1 Pt 1), 1984
PMID: 6203917
Smith DE, Fisher PA., J. Cell Biol. 99(1 Pt 1), 1984
PMID: 6203917
The activation of human type IV collagenase proenzyme. Sequence identification of the major conversion product following organomercurial activation.
Stetler-Stevenson WG, Krutzsch HC, Wacher MP, Margulies IM, Liotta LA., J. Biol. Chem. 264(3), 1989
PMID: 2536363
Stetler-Stevenson WG, Krutzsch HC, Wacher MP, Margulies IM, Liotta LA., J. Biol. Chem. 264(3), 1989
PMID: 2536363
The recombinant catalytic domain of membrane-type matrix metalloproteinase-1 (MT1-MMP) induces activation of progelatinase A and progelatinase A complexed with TIMP-2.
Lichte A, Kolkenbrock H, Tschesche H., FEBS Lett. 397(2-3), 1996
PMID: 8955363
Lichte A, Kolkenbrock H, Tschesche H., FEBS Lett. 397(2-3), 1996
PMID: 8955363
Thrombin induces the activation of progelatinase A in vascular endothelial cells. Physiologic regulation of angiogenesis.
Zucker S, Conner C, DiMassmo BI, Ende H, Drews M, Seiki M, Bahou WF., J. Biol. Chem. 270(40), 1995
PMID: 7559545
Zucker S, Conner C, DiMassmo BI, Ende H, Drews M, Seiki M, Bahou WF., J. Biol. Chem. 270(40), 1995
PMID: 7559545
Membrane type matrix metalloproteinase 1 activates pro-gelatinase A without furin cleavage of the N-terminal domain.
Cao J, Rehemtulla A, Bahou W, Zucker S., J. Biol. Chem. 271(47), 1996
PMID: 8939968
Cao J, Rehemtulla A, Bahou W, Zucker S., J. Biol. Chem. 271(47), 1996
PMID: 8939968
The C-terminal region of membrane type matrix metalloproteinase is a functional transmembrane domain required for pro-gelatinase A activation.
Cao J, Sato H, Takino T, Seiki M., J. Biol. Chem. 270(2), 1995
PMID: 7822314
Cao J, Sato H, Takino T, Seiki M., J. Biol. Chem. 270(2), 1995
PMID: 7822314
Enrichment of collagen and gelatin degrading activities in the plasma membranes of human cancer cells.
Zucker S, Wieman JM, Lysik RM, Wilkie D, Ramamurthy NS, Golub LM, Lane B., Cancer Res. 47(6), 1987
PMID: 3545450
Zucker S, Wieman JM, Lysik RM, Wilkie D, Ramamurthy NS, Golub LM, Lane B., Cancer Res. 47(6), 1987
PMID: 3545450
Identification of type IV collagenase in rat testicular cell culture: influence of peritubular-Sertoli cell interactions.
Sang QX, Stetler-Stevenson WG, Liotta LA, Byers SW., Biol. Reprod. 43(6), 1990
PMID: 1963327
Sang QX, Stetler-Stevenson WG, Liotta LA, Byers SW., Biol. Reprod. 43(6), 1990
PMID: 1963327
Soluble laminin and arginine-glycine-aspartic acid containing peptides differentially regulate type IV collagenase messenger RNA, activation, and localization in testicular cell culture.
Sang QX, Thompson EW, Grant D, Stetler-Stevenson WG, Byers SW., Biol. Reprod. 45(3), 1991
PMID: 1664247
Sang QX, Thompson EW, Grant D, Stetler-Stevenson WG, Byers SW., Biol. Reprod. 45(3), 1991
PMID: 1664247
Secreted metalloproteinases in testicular cell culture.
Sang QX, Dym M, Byers SW., Biol. Reprod. 43(6), 1990
PMID: 2127232
Sang QX, Dym M, Byers SW., Biol. Reprod. 43(6), 1990
PMID: 2127232
Basic local alignment search tool.
Altschul SF, Gish W, Miller W, Myers EW, Lipman DJ., J. Mol. Biol. 215(3), 1990
PMID: 2231712
Altschul SF, Gish W, Miller W, Myers EW, Lipman DJ., J. Mol. Biol. 215(3), 1990
PMID: 2231712
Gapped BLAST and PSI-BLAST: a new generation of protein database search programs.
Altschul SF, Madden TL, Schaffer AA, Zhang J, Zhang Z, Miller W, Lipman DJ., Nucleic Acids Res. 25(17), 1997
PMID: 9254694
Altschul SF, Madden TL, Schaffer AA, Zhang J, Zhang Z, Miller W, Lipman DJ., Nucleic Acids Res. 25(17), 1997
PMID: 9254694
A novel coumarin-labelled peptide for sensitive continuous assays of the matrix metalloproteinases.
Knight CG, Willenbrock F, Murphy G., FEBS Lett. 296(3), 1992
PMID: 1537400
Knight CG, Willenbrock F, Murphy G., FEBS Lett. 296(3), 1992
PMID: 1537400
Membrane-type matrix metalloproteinase 1 is a gelatinolytic enzyme and is secreted in a complex with tissue inhibitor of metalloproteinases 2.
Imai K, Ohuchi E, Aoki T, Nomura H, Fujii Y, Sato H, Seiki M, Okada Y., Cancer Res. 56(12), 1996
PMID: 8665498
Imai K, Ohuchi E, Aoki T, Nomura H, Fujii Y, Sato H, Seiki M, Okada Y., Cancer Res. 56(12), 1996
PMID: 8665498
Regulation of membrane-type matrix metalloproteinase-1 expression by growth factors and phorbol 12-myristate 13-acetate.
Lohi J, Lehti K, Westermarck J, Kahari VM, Keski-Oja J., Eur. J. Biochem. 239(2), 1996
PMID: 8706726
Lohi J, Lehti K, Westermarck J, Kahari VM, Keski-Oja J., Eur. J. Biochem. 239(2), 1996
PMID: 8706726
The soluble catalytic domain of membrane type 1 matrix metalloproteinase cleaves the propeptide of progelatinase A and initiates autoproteolytic activation. Regulation by TIMP-2 and TIMP-3.
Will H, Atkinson SJ, Butler GS, Smith B, Murphy G., J. Biol. Chem. 271(29), 1996
PMID: 8663332
Will H, Atkinson SJ, Butler GS, Smith B, Murphy G., J. Biol. Chem. 271(29), 1996
PMID: 8663332
Plasma membrane-dependent activation of the 72-kDa type IV collagenase is prevented by complex formation with TIMP-2.
Strongin AY, Marmer BL, Grant GA, Goldberg GI., J. Biol. Chem. 268(19), 1993
PMID: 8314771
Strongin AY, Marmer BL, Grant GA, Goldberg GI., J. Biol. Chem. 268(19), 1993
PMID: 8314771
Cell surface binding and activation of gelatinase A induced by expression of membrane-type-1-matrix metalloproteinase (MT1-MMP).
Sato H, Takino T, Kinoshita T, Imai K, Okada Y, Stetler Stevenson WG, Seiki M., FEBS Lett. 385(3), 1996
PMID: 8647259
Sato H, Takino T, Kinoshita T, Imai K, Okada Y, Stetler Stevenson WG, Seiki M., FEBS Lett. 385(3), 1996
PMID: 8647259
Activation of progelatinase B (MMP-9) by gelatinase A (MMP-2).
Fridman R, Toth M, Pena D, Mobashery S., Cancer Res. 55(12), 1995
PMID: 7780967
Fridman R, Toth M, Pena D, Mobashery S., Cancer Res. 55(12), 1995
PMID: 7780967
Induction of membrane-type matrix metalloproteinase 1 (MT1-MMP) expression in human fibroblasts by breast adenocarcinoma cells.
Polette M, Gilles C, Marchand V, Seiki M, Tournier JM, Birembaut P., Clin. Exp. Metastasis 15(2), 1997
PMID: 9062392
Polette M, Gilles C, Marchand V, Seiki M, Tournier JM, Birembaut P., Clin. Exp. Metastasis 15(2), 1997
PMID: 9062392
Activation of a recombinant membrane type 1-matrix metalloproteinase (MT1-MMP) by furin and its interaction with tissue inhibitor of metalloproteinases (TIMP)-2.
Sato H, Kinoshita T, Takino T, Nakayama K, Seiki M., FEBS Lett. 393(1), 1996
PMID: 8804434
Sato H, Kinoshita T, Takino T, Nakayama K, Seiki M., FEBS Lett. 393(1), 1996
PMID: 8804434
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
Strongin AY, Collier I, Bannikov G, Marmer BL, Grant GA, Goldberg GI., J. Biol. Chem. 270(10), 1995
PMID: 7890645
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