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Volumn 116, Issue 3, 2007, Pages 391-400

Regulation of extracellular matrix remodeling and cell fate determination by matrix metalloproteinase stromelysin-3 during thyroid hormone-dependent post-embryonic development

Author keywords

Apoptosis; Extracellular matrix; Matrix metalloproteinase; Metamorphosis; Thyroid hormone receptor; Xenopus laevis

Indexed keywords

LAMININ RECEPTOR; MATRIX METALLOPROTEINASE; STROMELYSIN 3; THYROID HORMONE; THYROID HORMONE RECEPTOR;

EID: 36148995458     PISSN: 01637258     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pharmthera.2007.07.005     Document Type: Review
Times cited : (31)

References (104)
  • 1
    • 0031935209 scopus 로고    scopus 로고
    • Stromelysin 3: an independent prognostic factor for relapse-free survival in node-positive breast cancer and demonstration of novel breast carcinoma cell expression
    • Ahmad A., Hanby A., Dublin E., Poulsom R., Smith P., Barnes D., et al. Stromelysin 3: an independent prognostic factor for relapse-free survival in node-positive breast cancer and demonstration of novel breast carcinoma cell expression. Am J Pathol 152 (1998) 721-728
    • (1998) Am J Pathol , vol.152 , pp. 721-728
    • Ahmad, A.1    Hanby, A.2    Dublin, E.3    Poulsom, R.4    Smith, P.5    Barnes, D.6
  • 2
    • 0000999998 scopus 로고
    • Extracellular matrix degradation
    • Hay E.D. (Ed), Plenum Press, New York
    • Alexander C.M., and Werb Z. Extracellular matrix degradation. In: Hay E.D. (Ed). Cell Biology of Extracellular Matrix (1991), Plenum Press, New York 255-302
    • (1991) Cell Biology of Extracellular Matrix , pp. 255-302
    • Alexander, C.M.1    Werb, Z.2
  • 3
    • 0029896682 scopus 로고    scopus 로고
    • Expression and function of matrix metalloproteinases and their inhibitors at the maternal-embryonic boundary during mouse embryo implantation
    • Alexander C.M., Hansell E.J., Behrendtsen O., Flannery M.L., Kishnani N.S., Hawkes S.P., et al. Expression and function of matrix metalloproteinases and their inhibitors at the maternal-embryonic boundary during mouse embryo implantation. Development 122 (1996) 1723-1736
    • (1996) Development , vol.122 , pp. 1723-1736
    • Alexander, C.M.1    Hansell, E.J.2    Behrendtsen, O.3    Flannery, M.L.4    Kishnani, N.S.5    Hawkes, S.P.6
  • 4
    • 0031893395 scopus 로고    scopus 로고
    • Metamorphosis-associated and region-specific expression of calbindin gene in the posterior intestinal epithelium of Xenopus laevis larva
    • Amano T., Noro N., Kawabata H., Kobayashi Y., and Yoshizato K. Metamorphosis-associated and region-specific expression of calbindin gene in the posterior intestinal epithelium of Xenopus laevis larva. Dev Growth Differ 40 (1998) 177-188
    • (1998) Dev Growth Differ , vol.40 , pp. 177-188
    • Amano, T.1    Noro, N.2    Kawabata, H.3    Kobayashi, Y.4    Yoshizato, K.5
  • 5
    • 15244347280 scopus 로고    scopus 로고
    • Substrate specificity of Xenopus matrix metalloproteinase stromelysin-3
    • Amano T., Fu L., Sahu S., Markey M., and Shi Y.-B. Substrate specificity of Xenopus matrix metalloproteinase stromelysin-3. Int J Mol Med 14 (2004) 233-239
    • (2004) Int J Mol Med , vol.14 , pp. 233-239
    • Amano, T.1    Fu, L.2    Sahu, S.3    Markey, M.4    Shi, Y.-B.5
  • 6
    • 23944518358 scopus 로고    scopus 로고
    • Spatio-temporal regulation and cleavage by matrix metalloproteinase stromelysin-3 implicate a role for laminin receptor in intestinal remodeling during Xenopus laevis metamorphosis
    • Amano T., Fu L., Marshak A., Kwak O., and Shi Y.B. Spatio-temporal regulation and cleavage by matrix metalloproteinase stromelysin-3 implicate a role for laminin receptor in intestinal remodeling during Xenopus laevis metamorphosis. Dev Dyn 234 (2005) 190-200
    • (2005) Dev Dyn , vol.234 , pp. 190-200
    • Amano, T.1    Fu, L.2    Marshak, A.3    Kwak, O.4    Shi, Y.B.5
  • 7
    • 23044468956 scopus 로고    scopus 로고
    • The matrix metalloproteinase stromelysin-3 cleaves laminin receptor at two distinct sites between the transmembrane domain and laminin binding sequence within the extracellular domain
    • Amano T., Kwak O., Fu L., Marshak A., and Shi Y.-B. The matrix metalloproteinase stromelysin-3 cleaves laminin receptor at two distinct sites between the transmembrane domain and laminin binding sequence within the extracellular domain. Cell Res 15 (2005) 150-159
    • (2005) Cell Res , vol.15 , pp. 150-159
    • Amano, T.1    Kwak, O.2    Fu, L.3    Marshak, A.4    Shi, Y.-B.5
  • 8
    • 0029090448 scopus 로고
    • Stromelysin-3 is overexpressed by stromal elements in primary non-small-cell lung cancers and regulated by retinoic acid in pulmonary fibroblasts
    • Anderson I.C., Sugarbaker D.J., Ganju R.K., Tsarwhas D.G., Richards W.G., Sunday M., et al. Stromelysin-3 is overexpressed by stromal elements in primary non-small-cell lung cancers and regulated by retinoic acid in pulmonary fibroblasts. Cancer Res 55 (1995) 4120-4126
    • (1995) Cancer Res , vol.55 , pp. 4120-4126
    • Anderson, I.C.1    Sugarbaker, D.J.2    Ganju, R.K.3    Tsarwhas, D.G.4    Richards, W.G.5    Sunday, M.6
  • 9
    • 0029022983 scopus 로고
    • Structure and promoter characterization of the human stromelysin-3 gene
    • Anglard P., Melot T., Guerin E., Thomas G., and Basset P. Structure and promoter characterization of the human stromelysin-3 gene. J Biol Chem 270 (1995) 20337-20344
    • (1995) J Biol Chem , vol.270 , pp. 20337-20344
    • Anglard, P.1    Melot, T.2    Guerin, E.3    Thomas, G.4    Basset, P.5
  • 10
    • 0031880124 scopus 로고    scopus 로고
    • The 67-kDa laminin receptor originated from a ribosomal protein that acquired a dual function during evolution
    • Ardini E., Pesole G., Tagliabue E., Magnifico A., Castronovo V., Sobel M.E., Colnaghi M.I., et al. The 67-kDa laminin receptor originated from a ribosomal protein that acquired a dual function during evolution. Mol Biol Evol 15 (1998) 1017-1025
    • (1998) Mol Biol Evol , vol.15 , pp. 1017-1025
    • Ardini, E.1    Pesole, G.2    Tagliabue, E.3    Magnifico, A.4    Castronovo, V.5    Sobel, M.E.6    Colnaghi, M.I.7
  • 11
    • 0026554288 scopus 로고
    • A 33-kDa polypeptide with homology to the laminin receptor: component of translation machinery
    • Auth D., and Brawerman G. A 33-kDa polypeptide with homology to the laminin receptor: component of translation machinery. PNAS 89 (1992) 4368-4372
    • (1992) PNAS , vol.89 , pp. 4368-4372
    • Auth, D.1    Brawerman, G.2
  • 14
    • 0025641098 scopus 로고
    • A novel metalloproteinase gene specifically expressed in stromal cells of breast carcinomas
    • Basset P., Bellocq J.P., Wolf C., Stoll I., Hutin P., Limacher J.M., et al. A novel metalloproteinase gene specifically expressed in stromal cells of breast carcinomas. Nature 348 (1990) 699-704
    • (1990) Nature , vol.348 , pp. 699-704
    • Basset, P.1    Bellocq, J.P.2    Wolf, C.3    Stoll, I.4    Hutin, P.5    Limacher, J.M.6
  • 15
    • 0032213732 scopus 로고    scopus 로고
    • The expression pattern of thyroid hormone response genes in remodeling tadpole tissues defines distinct growth and resorption gene expression programs
    • Berry D.L., Rose C.S., Remo B.F., and Brown D.D. The expression pattern of thyroid hormone response genes in remodeling tadpole tissues defines distinct growth and resorption gene expression programs. Dev Biol 203 (1998) 24-35
    • (1998) Dev Biol , vol.203 , pp. 24-35
    • Berry, D.L.1    Rose, C.S.2    Remo, B.F.3    Brown, D.D.4
  • 16
    • 0032211641 scopus 로고    scopus 로고
    • The expression pattern of thyroid hormone response genes in the tadpole tail identifies multiple resorption programs
    • Berry D.L., Schwartzman R.A., and Brown D.D. The expression pattern of thyroid hormone response genes in the tadpole tail identifies multiple resorption programs. Dev Biol 203 (1998) 12-23
    • (1998) Dev Biol , vol.203 , pp. 12-23
    • Berry, D.L.1    Schwartzman, R.A.2    Brown, D.D.3
  • 18
    • 0002811004 scopus 로고
    • The role of integrins during vertebrate development
    • Brown K.E., and Yamada K.M. The role of integrins during vertebrate development. Semin Dev Biol 6 (1995) 69-77
    • (1995) Semin Dev Biol , vol.6 , pp. 69-77
    • Brown, K.E.1    Yamada, K.M.2
  • 19
    • 0141781116 scopus 로고    scopus 로고
    • A dominant negative thyroid hormone receptor blocks amphibian metamorphosis by retaining corepressors at target genes
    • Buchholz D.R., Hsia V.S.-C., Fu L., and Shi Y.-B. A dominant negative thyroid hormone receptor blocks amphibian metamorphosis by retaining corepressors at target genes. Mol Cell Biol 23 (2003) 6750-6758
    • (2003) Mol Cell Biol , vol.23 , pp. 6750-6758
    • Buchholz, D.R.1    Hsia, V.S.-C.2    Fu, L.3    Shi, Y.-B.4
  • 20
    • 4744350780 scopus 로고    scopus 로고
    • Transgenic analysis reveals that thyroid hormone receptor is sufficient to mediate the thyroid hormone signal in frog metamorphosis
    • Buchholz D.R., Tomita A., Fu L., Paul B.D., and Shi Y.-B. Transgenic analysis reveals that thyroid hormone receptor is sufficient to mediate the thyroid hormone signal in frog metamorphosis. Mol Cell Biol 24 (2004) 9026-9037
    • (2004) Mol Cell Biol , vol.24 , pp. 9026-9037
    • Buchholz, D.R.1    Tomita, A.2    Fu, L.3    Paul, B.D.4    Shi, Y.-B.5
  • 22
    • 0027279623 scopus 로고
    • Laminin receptors and laminin-binding proteins during tumor invasion and metastasis
    • Castronovo V. Laminin receptors and laminin-binding proteins during tumor invasion and metastasis. Invasion Metasis 13 (1993) 1-30
    • (1993) Invasion Metasis , vol.13 , pp. 1-30
    • Castronovo, V.1
  • 23
    • 0025841906 scopus 로고
    • Functional domains of the 67-kDa laminin receptor precursor
    • Castronovo V., Taraboletti G., and ME Sobel M.E. Functional domains of the 67-kDa laminin receptor precursor. J Biol Chem 266 (1991) 20440-20446
    • (1991) J Biol Chem , vol.266 , pp. 20440-20446
    • Castronovo, V.1    Taraboletti, G.2    ME Sobel, M.E.3
  • 24
    • 0030467609 scopus 로고    scopus 로고
    • High levels of stromelysin-3 correlate with poor prognosis in patients with breast carcinoma
    • Chenard M.P., OSiorain L., Shering S., Rouyer N., Lutz Y., Wolf C., et al. High levels of stromelysin-3 correlate with poor prognosis in patients with breast carcinoma. Int J Cancer 69 (1996) 448-451
    • (1996) Int J Cancer , vol.69 , pp. 448-451
    • Chenard, M.P.1    OSiorain, L.2    Shering, S.3    Rouyer, N.4    Lutz, Y.5    Wolf, C.6
  • 25
    • 0031008068 scopus 로고    scopus 로고
    • Matrix metalloproteinases regulate morphogenesis, migration and remodeling of epithelium, tongue skeleta muscle and cartilage in the mandibular arch
    • Chin J.R., and Werb Z. Matrix metalloproteinases regulate morphogenesis, migration and remodeling of epithelium, tongue skeleta muscle and cartilage in the mandibular arch. Development 124 (1997) 1519-1530
    • (1997) Development , vol.124 , pp. 1519-1530
    • Chin, J.R.1    Werb, Z.2
  • 26
    • 0037192458 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors and cancer: trials and tribulations
    • Coussens L.M., Fingleton B.M., and Matrisian L.M. Matrix metalloproteinase inhibitors and cancer: trials and tribulations. Science 295 (2002) 2387-2392
    • (2002) Science , vol.295 , pp. 2387-2392
    • Coussens, L.M.1    Fingleton, B.M.2    Matrisian, L.M.3
  • 27
    • 0033142510 scopus 로고    scopus 로고
    • Spatial and temporal regulation of collagenases-3, -4, and stromelysin-3 implicates distinct functions in apoptosis and tissue remodeling during frog metamorphosis
    • Damjanovski S., Ishizuya-Oka A., and Shi Y.B. Spatial and temporal regulation of collagenases-3, -4, and stromelysin-3 implicates distinct functions in apoptosis and tissue remodeling during frog metamorphosis. Cell Res 9 (1999) 91-105
    • (1999) Cell Res , vol.9 , pp. 91-105
    • Damjanovski, S.1    Ishizuya-Oka, A.2    Shi, Y.B.3
  • 28
    • 0035035030 scopus 로고    scopus 로고
    • Overexpression of matrix metalloproteinases leads to lethality in transgenic Xenopus laevis: implications for tissue-dependent functions of matrix metalloproteinases during late embryonic development
    • Damjanovski S., Amano T., Li Q., Pei D., and Shi Y.-B. Overexpression of matrix metalloproteinases leads to lethality in transgenic Xenopus laevis: implications for tissue-dependent functions of matrix metalloproteinases during late embryonic development. Dev Dyn 221 (2001) 37-47
    • (2001) Dev Dyn , vol.221 , pp. 37-47
    • Damjanovski, S.1    Amano, T.2    Li, Q.3    Pei, D.4    Shi, Y.-B.5
  • 29
    • 0026938957 scopus 로고
    • Signal transduction by integrin receptors for extracellular matrix: cooperative processing of extracellular information
    • Damsky C.H., and Werb Z. Signal transduction by integrin receptors for extracellular matrix: cooperative processing of extracellular information. Curr Opin Cell Biol 4 (1992) 772-781
    • (1992) Curr Opin Cell Biol , vol.4 , pp. 772-781
    • Damsky, C.H.1    Werb, Z.2
  • 30
    • 0001368922 scopus 로고
    • The biology of metamorphosis
    • Lofts B. (Ed), Academic Press, New York
    • Dodd M.H.I., and Dodd J.M. The biology of metamorphosis. In: Lofts B. (Ed). Physiology of the Amphibia (1976), Academic Press, New York 467-599
    • (1976) Physiology of the Amphibia , pp. 467-599
    • Dodd, M.H.I.1    Dodd, J.M.2
  • 31
    • 0036019133 scopus 로고    scopus 로고
    • A novel double promoter approach for identification of transgenic animals: a tool for in vivo analysis of gene function and development of gene-based therapies
    • Fu L., Buchholz D., and Shi Y.-B. A novel double promoter approach for identification of transgenic animals: a tool for in vivo analysis of gene function and development of gene-based therapies. Mol Reprod Dev 62 (2002) 470-476
    • (2002) Mol Reprod Dev , vol.62 , pp. 470-476
    • Fu, L.1    Buchholz, D.2    Shi, Y.-B.3
  • 32
    • 23044481558 scopus 로고    scopus 로고
    • A causative role of stromelysin-3 in ECM remodeling and epithelial apoptosis during intestinal metamorphosis in Xenopus laevis
    • Fu L., Ishizuya-Oka A., Buchholz D.R., Amano T., and Shi Y.-B. A causative role of stromelysin-3 in ECM remodeling and epithelial apoptosis during intestinal metamorphosis in Xenopus laevis. J Biol Chem 280 (2005) 27856-27865
    • (2005) J Biol Chem , vol.280 , pp. 27856-27865
    • Fu, L.1    Ishizuya-Oka, A.2    Buchholz, D.R.3    Amano, T.4    Shi, Y.-B.5
  • 33
    • 33745184018 scopus 로고    scopus 로고
    • Transcriptional regulation of the Xenopus laevis stromelysin-3 gene by thyroid hormone is mediated by a DNA element in the first intron
    • Fu L., Tomita A., Wang H., Buchholz D.R., and Shi Y.-B. Transcriptional regulation of the Xenopus laevis stromelysin-3 gene by thyroid hormone is mediated by a DNA element in the first intron. J Biol Chem 281 (2006) 16870-16878
    • (2006) J Biol Chem , vol.281 , pp. 16870-16878
    • Fu, L.1    Tomita, A.2    Wang, H.3    Buchholz, D.R.4    Shi, Y.-B.5
  • 34
    • 33646010048 scopus 로고    scopus 로고
    • One of the duplicated matrix metalloproteinase-9 genes is expressed in regressing tail during anuran metamorphosis
    • Fujimoto K., Nakajima K., and Yaoita Y. One of the duplicated matrix metalloproteinase-9 genes is expressed in regressing tail during anuran metamorphosis. Dev Growth Differ 48 (2006) 223-241
    • (2006) Dev Growth Differ , vol.48 , pp. 223-241
    • Fujimoto, K.1    Nakajima, K.2    Yaoita, Y.3
  • 37
    • 0022004223 scopus 로고
    • Expression of laminin receptor in normal and carcinomatous human tissues as defined by a monoclonal antibody
    • Hand P.H., Thor A., Schlom J., Rao C.N., and Liotta L.A. Expression of laminin receptor in normal and carcinomatous human tissues as defined by a monoclonal antibody. Cancer Res 45 (1985) 2713-2719
    • (1985) Cancer Res , vol.45 , pp. 2713-2719
    • Hand, P.H.1    Thor, A.2    Schlom, J.3    Rao, C.N.4    Liotta, L.A.5
  • 38
    • 33644633826 scopus 로고    scopus 로고
    • Spatial and temporal expression profiles suggest the involvement of gelatinase A and membrane type 1 matrix metalloproteinase in amphibian metamorphosis
    • Hasebe T., Hartman R., Matsuda H., and Shi Y.B. Spatial and temporal expression profiles suggest the involvement of gelatinase A and membrane type 1 matrix metalloproteinase in amphibian metamorphosis. Cell Tissue Res 324 (2006) 105-116
    • (2006) Cell Tissue Res , vol.324 , pp. 105-116
    • Hasebe, T.1    Hartman, R.2    Matsuda, H.3    Shi, Y.B.4
  • 40
    • 0023377349 scopus 로고
    • Ultrastructural changes in the intestinal connective tissue of Xenopus laevis during metamorphosis
    • Ishizuya-Oka A., and Shimozawa A. Ultrastructural changes in the intestinal connective tissue of Xenopus laevis during metamorphosis. J Morphol 193 (1987) 13-22
    • (1987) J Morphol , vol.193 , pp. 13-22
    • Ishizuya-Oka, A.1    Shimozawa, A.2
  • 41
    • 0026356474 scopus 로고
    • Induction of metamorphosis by thyroid hormone in anuran small intestine cultured organotypically in vitro
    • Ishizuya-Oka A., and Shimozawa A. Induction of metamorphosis by thyroid hormone in anuran small intestine cultured organotypically in vitro. In Vitro Cell Dev Biol 27A (1991) 853-857
    • (1991) In Vitro Cell Dev Biol , vol.27 A , pp. 853-857
    • Ishizuya-Oka, A.1    Shimozawa, A.2
  • 42
    • 0030033962 scopus 로고    scopus 로고
    • Transient expression of stromelysin-3 mRNA in the amphibian small intestine during metamorphosis
    • Ishizuya-Oka A., Ueda S., and Shi Y.-B. Transient expression of stromelysin-3 mRNA in the amphibian small intestine during metamorphosis. Cell Tissue Res 283 (1996) 325-329
    • (1996) Cell Tissue Res , vol.283 , pp. 325-329
    • Ishizuya-Oka, A.1    Ueda, S.2    Shi, Y.-B.3
  • 43
    • 0034605046 scopus 로고    scopus 로고
    • Requirement for matrix metalloproteinase stromelysin-3 in cell migration and apoptosis during tissue remodeling in Xenopus laevis
    • Ishizuya-Oka A., Li Q., Amano T., Damjanovski S., Ueda S., and Shi Y.-B. Requirement for matrix metalloproteinase stromelysin-3 in cell migration and apoptosis during tissue remodeling in Xenopus laevis. J Cell Biol 150 (2000) 1177-1188
    • (2000) J Cell Biol , vol.150 , pp. 1177-1188
    • Ishizuya-Oka, A.1    Li, Q.2    Amano, T.3    Damjanovski, S.4    Ueda, S.5    Shi, Y.-B.6
  • 44
    • 0036193222 scopus 로고    scopus 로고
    • Matrix metalloproteinase mediate the dismantling of mesenchymal structures in the tadpole tail during thyroid hormone-induced tail resorption
    • Jung J.-C., Leco K.J., Edwards D.R., and Fini M.E. Matrix metalloproteinase mediate the dismantling of mesenchymal structures in the tadpole tail during thyroid hormone-induced tail resorption. Dev Dyn 223 (2002) 402-413
    • (2002) Dev Dyn , vol.223 , pp. 402-413
    • Jung, J.-C.1    Leco, K.J.2    Edwards, D.R.3    Fini, M.E.4
  • 45
  • 46
    • 0027683226 scopus 로고
    • Structural biochemistry and activation of matrix metalloproteases
    • Kleiner Jr. D.E., and Stetler-Stevenson W.G. Structural biochemistry and activation of matrix metalloproteases. Curr Opin Cell Biol 5 (1993) 891-897
    • (1993) Curr Opin Cell Biol , vol.5 , pp. 891-897
    • Kleiner Jr., D.E.1    Stetler-Stevenson, W.G.2
  • 47
    • 0029806183 scopus 로고    scopus 로고
    • Transgenic Xenopus embryos from sperm nuclear transplantations reveal FGF signaling requirements during gastrulation
    • Kroll K.L., and Amaya E. Transgenic Xenopus embryos from sperm nuclear transplantations reveal FGF signaling requirements during gastrulation. Development 122 (1996) 3173-3183
    • (1996) Development , vol.122 , pp. 3173-3183
    • Kroll, K.L.1    Amaya, E.2
  • 48
    • 0029154305 scopus 로고
    • Studies of the structure of the metastasis-associated 67 kDa laminin binding protein: fatty acid acylation and evidence supporting dimerization of the 32 kDa gene product to form the mature protein
    • Landowski T.H., Dratz E.A., and Starkey J.R. Studies of the structure of the metastasis-associated 67 kDa laminin binding protein: fatty acid acylation and evidence supporting dimerization of the 32 kDa gene product to form the mature protein. Biochemistry 34 (1995) 11276-11287
    • (1995) Biochemistry , vol.34 , pp. 11276-11287
    • Landowski, T.H.1    Dratz, E.A.2    Starkey, J.R.3
  • 49
    • 0026486192 scopus 로고
    • The breast cancer-associated stromelysin-3 gene is expressed during mouse mammary gland apoptosis
    • Lefebvre O., Wolf C., Limacher J.M., Hutin P., Wendling C., LeMeur M., et al. The breast cancer-associated stromelysin-3 gene is expressed during mouse mammary gland apoptosis. J Cell Biol 119 (1992) 997-1002
    • (1992) J Cell Biol , vol.119 , pp. 997-1002
    • Lefebvre, O.1    Wolf, C.2    Limacher, J.M.3    Hutin, P.4    Wendling, C.5    LeMeur, M.6
  • 51
    • 0032526634 scopus 로고    scopus 로고
    • Unique organization and involvement of GAGA factors in the transcriptional regulation of the Xenopus stromelysin-3 gene
    • Li J., Liang V.C.-T., Sedgwick T., Wong J., and Shi Y.-B. Unique organization and involvement of GAGA factors in the transcriptional regulation of the Xenopus stromelysin-3 gene. Nucleic Acids Res 26 (1998) 3018-3025
    • (1998) Nucleic Acids Res , vol.26 , pp. 3018-3025
    • Li, J.1    Liang, V.C.-T.2    Sedgwick, T.3    Wong, J.4    Shi, Y.-B.5
  • 52
    • 0033039398 scopus 로고    scopus 로고
    • An odyssey from breast to bone: multi-step control of mammary metastases and osteolysis by matrix metalloproteinases
    • Lochter A., and Bissell M.J. An odyssey from breast to bone: multi-step control of mammary metastases and osteolysis by matrix metalloproteinases. APMIS 107 (1999) 128-136
    • (1999) APMIS , vol.107 , pp. 128-136
    • Lochter, A.1    Bissell, M.J.2
  • 53
    • 0037067669 scopus 로고    scopus 로고
    • Alternative splicing and promoter usage generates an intracellular stromelysin-3 isoform directly translated as an active matrix metalloproteinase
    • Lu D., Mari B., Stoll I., and Anglard P. Alternative splicing and promoter usage generates an intracellular stromelysin-3 isoform directly translated as an active matrix metalloproteinase. J Biol Chem 277 (2002) 25527-25536
    • (2002) J Biol Chem , vol.277 , pp. 25527-25536
    • Lu, D.1    Mari, B.2    Stoll, I.3    Anglard, P.4
  • 54
    • 0034704133 scopus 로고    scopus 로고
    • Multiple regulator elements in the murine stromelysin-3 promoter: evidence for direct control by CCAAT/enhancer-binding protein beta and thyroid and retinoid receptors
    • Ludwig M.-G., Basset P., and Anglard P. Multiple regulator elements in the murine stromelysin-3 promoter: evidence for direct control by CCAAT/enhancer-binding protein beta and thyroid and retinoid receptors. J Biol Chem 275 (2000) 39981-39990
    • (2000) J Biol Chem , vol.275 , pp. 39981-39990
    • Ludwig, M.-G.1    Basset, P.2    Anglard, P.3
  • 55
    • 0020618286 scopus 로고
    • Isolation of a cell surface receptor protein for laminin from murine fibrosarcoma cells
    • Malinoff H.L., and Wicha M.S. Isolation of a cell surface receptor protein for laminin from murine fibrosarcoma cells. J Cell Biol 96 (1983) 1475-1479
    • (1983) J Cell Biol , vol.96 , pp. 1475-1479
    • Malinoff, H.L.1    Wicha, M.S.2
  • 56
    • 0040776938 scopus 로고    scopus 로고
    • Identification of insulin-like growth factor-binding protein-1 as a potential physiological substrate for human stromelysin-3
    • Manes S., Mira E., Barbacid M.D., Cipres A., FernandezResa P., Buesa J.M., et al. Identification of insulin-like growth factor-binding protein-1 as a potential physiological substrate for human stromelysin-3. J Biol Chem 272 (1997) 25706-25712
    • (1997) J Biol Chem , vol.272 , pp. 25706-25712
    • Manes, S.1    Mira, E.2    Barbacid, M.D.3    Cipres, A.4    FernandezResa, P.5    Buesa, J.M.6
  • 58
    • 0032559821 scopus 로고    scopus 로고
    • In vivo evidence that the stromelysin-3 metalloproteinase contributes in a paracrine manner to epithelial cell malignancy
    • Masson R., Lefebvre O., Noel A., Fahime M.E., Chenard M.P., Wendling C., et al. In vivo evidence that the stromelysin-3 metalloproteinase contributes in a paracrine manner to epithelial cell malignancy. J Cell Biol 140 (1998) 1535-1541
    • (1998) J Cell Biol , vol.140 , pp. 1535-1541
    • Masson, R.1    Lefebvre, O.2    Noel, A.3    Fahime, M.E.4    Chenard, M.P.5    Wendling, C.6
  • 59
    • 0001392033 scopus 로고
    • Cell proliferation and renewal in the small intestinal epithelium of metamorphosing and adult Xenopus laevis
    • McAvoy J.W., and Dixon K.E. Cell proliferation and renewal in the small intestinal epithelium of metamorphosing and adult Xenopus laevis. J Exp Zool 202 (1977) 129-138
    • (1977) J Exp Zool , vol.202 , pp. 129-138
    • McAvoy, J.W.1    Dixon, K.E.2
  • 60
    • 0035479845 scopus 로고    scopus 로고
    • Matrix metalloproteinases: they're not just for matrix anymore!
    • McCawley L.J., and Matrisian L.M. Matrix metalloproteinases: they're not just for matrix anymore!. Curr Opin Cell Biol 13 (2001) 534-540
    • (2001) Curr Opin Cell Biol , vol.13 , pp. 534-540
    • McCawley, L.J.1    Matrisian, L.M.2
  • 61
    • 0344247741 scopus 로고    scopus 로고
    • New insights into the metastasis-associated 67 kD laminin receptor
    • Menard S., Castronovo V., Tagliabue E., and Sobel M.E. New insights into the metastasis-associated 67 kD laminin receptor. J Cell Biochem 67 (1997) 155-165
    • (1997) J Cell Biochem , vol.67 , pp. 155-165
    • Menard, S.1    Castronovo, V.2    Tagliabue, E.3    Sobel, M.E.4
  • 62
    • 0027448423 scopus 로고
    • Increased stromelysin 3 gene expression is associated with increased local invasiveness in head and neck squamous cell carcinomas
    • Muller D., Wolf C., Abecassis J., Millon R., Engelmann A., Bronner G., et al. Increased stromelysin 3 gene expression is associated with increased local invasiveness in head and neck squamous cell carcinomas. Cancer Res 53 (1993) 165-169
    • (1993) Cancer Res , vol.53 , pp. 165-169
    • Muller, D.1    Wolf, C.2    Abecassis, J.3    Millon, R.4    Engelmann, A.5    Bronner, G.6
  • 63
    • 0025975419 scopus 로고
    • Morphologic changes of the basal lamina in the small intestine of Xenopus laevis during metamorphosis
    • Murata E., and Merker H.J. Morphologic changes of the basal lamina in the small intestine of Xenopus laevis during metamorphosis. Acta Anat 140 (1991) 60-69
    • (1991) Acta Anat , vol.140 , pp. 60-69
    • Murata, E.1    Merker, H.J.2
  • 64
    • 0027264485 scopus 로고
    • The 28-kDa N-terminal domain of mouse stromelysin-3 has the general properties of a weak metalloproteinase
    • Murphy G., Segain J.-P., O'Shea M., Cockett M., Ioannou C., Lefebvre O., et al. The 28-kDa N-terminal domain of mouse stromelysin-3 has the general properties of a weak metalloproteinase. J Biol Chem 268 (1993) 15435-15441
    • (1993) J Biol Chem , vol.268 , pp. 15435-15441
    • Murphy, G.1    Segain, J.-P.2    O'Shea, M.3    Cockett, M.4    Ioannou, C.5    Lefebvre, O.6
  • 66
    • 0032161747 scopus 로고    scopus 로고
    • Cell surface activation of progelatinase A (proMMP-2) and cell migration
    • Nagase H. Cell surface activation of progelatinase A (proMMP-2) and cell migration. Cell Res 8 (1998) 179-186
    • (1998) Cell Res , vol.8 , pp. 179-186
    • Nagase, H.1
  • 67
    • 0027014773 scopus 로고
    • Activation mechanisms of the precursors of matrix metalloproteinases 1, 2, and 3
    • Nagase J., Suzuki K., Morodomi T., Englhild J.J., and Salvesen G. Activation mechanisms of the precursors of matrix metalloproteinases 1, 2, and 3. Matrix Suppl 1 (1992) 237-244
    • (1992) Matrix Suppl , vol.1 , pp. 237-244
    • Nagase, J.1    Suzuki, K.2    Morodomi, T.3    Englhild, J.J.4    Salvesen, G.5
  • 70
    • 0034673675 scopus 로고    scopus 로고
    • Demonstration in vivo that stromelysin-3 functions through its proteolytic activity
    • Noel A., Boulay A., Kebers F., Kannan R., Hajitou A., Calberg-Bacq C.-M., et al. Demonstration in vivo that stromelysin-3 functions through its proteolytic activity. Oncogene 19 (2000) 1605-1612
    • (2000) Oncogene , vol.19 , pp. 1605-1612
    • Noel, A.1    Boulay, A.2    Kebers, F.3    Kannan, R.4    Hajitou, A.5    Calberg-Bacq, C.-M.6
  • 71
    • 0030031434 scopus 로고    scopus 로고
    • Thyroid hormone-dependent expression of bullfrog tadpole collagenase gene
    • Oofusa K., and Yoshizato K. Thyroid hormone-dependent expression of bullfrog tadpole collagenase gene. Roux's Arch Dev Biol 205 (1996) 241-251
    • (1996) Roux's Arch Dev Biol , vol.205 , pp. 241-251
    • Oofusa, K.1    Yoshizato, K.2
  • 72
    • 0028129092 scopus 로고
    • Regionally and hormonally regulated expression of genes of collagen and collagenase in the anuran larval skin
    • Oofusa K., Yomori S., and Yoshizato K. Regionally and hormonally regulated expression of genes of collagen and collagenase in the anuran larval skin. Int J Dev Biol 38 (1994) 345-350
    • (1994) Int J Dev Biol , vol.38 , pp. 345-350
    • Oofusa, K.1    Yomori, S.2    Yoshizato, K.3
  • 73
    • 0036741135 scopus 로고    scopus 로고
    • Molecular determinants of metalloproteinase substrate specificity
    • Overall C.M. Molecular determinants of metalloproteinase substrate specificity. Mol Biotechnol 22 (2002) 51-86
    • (2002) Mol Biotechnol , vol.22 , pp. 51-86
    • Overall, C.M.1
  • 75
    • 0028895584 scopus 로고
    • Transcriptional activation of the matrix metalloproteinase gene stromelysin-3 coincides with thyroid hormone-induced cell death during frog metamorphosis
    • Patterton D., Hayes W.P., and Shi Y.B. Transcriptional activation of the matrix metalloproteinase gene stromelysin-3 coincides with thyroid hormone-induced cell death during frog metamorphosis. Dev Biol 167 (1995) 252-262
    • (1995) Dev Biol , vol.167 , pp. 252-262
    • Patterton, D.1    Hayes, W.P.2    Shi, Y.B.3
  • 76
    • 0033256294 scopus 로고    scopus 로고
    • Leukolysin/MMP25/MT6-MMP: a novel matrix metalloproteinase specifically expressed in the leukocyte lineage
    • Pei D. Leukolysin/MMP25/MT6-MMP: a novel matrix metalloproteinase specifically expressed in the leukocyte lineage. Cell Res 9 (1999) 291-303
    • (1999) Cell Res , vol.9 , pp. 291-303
    • Pei, D.1
  • 77
    • 0029014101 scopus 로고
    • Furin-dependent intracellular activation of the human stromelysin-3 zymogen
    • Pei D., and Weiss S.J. Furin-dependent intracellular activation of the human stromelysin-3 zymogen. Nature 375 (1995) 244-247
    • (1995) Nature , vol.375 , pp. 244-247
    • Pei, D.1    Weiss, S.J.2
  • 78
    • 0028116127 scopus 로고
    • Hydrolytic inactivation of a breast carcinoma cell-derived serpin by human stromelysin-3
    • Pei D., Majmudar G., and Weiss S.J. Hydrolytic inactivation of a breast carcinoma cell-derived serpin by human stromelysin-3. J Biol Chem 269 (1994) 25849-25855
    • (1994) J Biol Chem , vol.269 , pp. 25849-25855
    • Pei, D.1    Majmudar, G.2    Weiss, S.J.3
  • 80
    • 0028335948 scopus 로고
    • Anchorage dependence, integrins, and apoptosis
    • Ruoslahti E., and Reed J.C. Anchorage dependence, integrins, and apoptosis. Cell 77 (1994) 477-478
    • (1994) Cell , vol.77 , pp. 477-478
    • Ruoslahti, E.1    Reed, J.C.2
  • 81
    • 0029793401 scopus 로고    scopus 로고
    • Overexpression of the 67-kD laminin receptor correlates with tumor progression in human colorectal carcinoma
    • Sanjuan X., Fernandez P.L., Miquel R., Munoz J., Castronovo V., Menard S., et al. Overexpression of the 67-kD laminin receptor correlates with tumor progression in human colorectal carcinoma. J Pathol 179 (1996) 376-380
    • (1996) J Pathol , vol.179 , pp. 376-380
    • Sanjuan, X.1    Fernandez, P.L.2    Miquel, R.3    Munoz, J.4    Castronovo, V.5    Menard, S.6
  • 82
    • 0030019731 scopus 로고    scopus 로고
    • Membrane-type matrix metallproteinases (MT-MMP) in tumor metastasis
    • Sato H., and Seiki M. Membrane-type matrix metallproteinases (MT-MMP) in tumor metastasis. J Biochem 119 (1996) 209-215
    • (1996) J Biochem , vol.119 , pp. 209-215
    • Sato, H.1    Seiki, M.2
  • 83
    • 0027614053 scopus 로고
    • Modulation of epithelial morphogenesis and cell fate by cell-to-cell signals and regulated cell adhesion
    • Schmidt J.W., Piepenhagen P.A., and Nelson W.J. Modulation of epithelial morphogenesis and cell fate by cell-to-cell signals and regulated cell adhesion. Semin Cell Biol 4 (1993) 161-173
    • (1993) Semin Cell Biol , vol.4 , pp. 161-173
    • Schmidt, J.W.1    Piepenhagen, P.A.2    Nelson, W.J.3
  • 84
    • 0039168853 scopus 로고    scopus 로고
    • Expression of stromelysin-3 in atherosclerotic lesions: regulation via CD40-CD40 ligand signaling in vitro and in vivo
    • Schonbeck U., Mach F., Sukhova G.K., Atkinson E., Levesque E., Herman M., et al. Expression of stromelysin-3 in atherosclerotic lesions: regulation via CD40-CD40 ligand signaling in vitro and in vivo. J Exp Med 189 (1999) 843-853
    • (1999) J Exp Med , vol.189 , pp. 843-853
    • Schonbeck, U.1    Mach, F.2    Sukhova, G.K.3    Atkinson, E.4    Levesque, E.5    Herman, M.6
  • 85
    • 0035845480 scopus 로고    scopus 로고
    • Diverse developmental programs of Xenopus laevis metamorphosis are inhibited by a dominant negative thyroid hormone receptor
    • Schreiber A.M., Das B., Huang H., Marsh-Armstrong N., and Brown D.D. Diverse developmental programs of Xenopus laevis metamorphosis are inhibited by a dominant negative thyroid hormone receptor. PNAS 98 (2001) 10739-10744
    • (2001) PNAS , vol.98 , pp. 10739-10744
    • Schreiber, A.M.1    Das, B.2    Huang, H.3    Marsh-Armstrong, N.4    Brown, D.D.5
  • 86
    • 14844359619 scopus 로고    scopus 로고
    • Remodeling of the intestine during metamorphosis of Xenopus laevis
    • Schreiber A.M., Cai L., and Brown D.D. Remodeling of the intestine during metamorphosis of Xenopus laevis. Proc Natl Acad Sci U S A 102 (2005) 3720-3725
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 3720-3725
    • Schreiber, A.M.1    Cai, L.2    Brown, D.D.3
  • 88
    • 0027182525 scopus 로고
    • The earliest changes in gene expression in tadpole intestine induced by thyroid hormone
    • Shi Y.-B., and Brown D.D. The earliest changes in gene expression in tadpole intestine induced by thyroid hormone. J Biol Chem 268 (1993) 20312-20317
    • (1993) J Biol Chem , vol.268 , pp. 20312-20317
    • Shi, Y.-B.1    Brown, D.D.2
  • 89
    • 0030042123 scopus 로고    scopus 로고
    • Biphasic intestinal development in amphibians: embryogensis and remodeling during metamorphosis
    • Shi Y.-B., and Ishizuya-Oka A. Biphasic intestinal development in amphibians: embryogensis and remodeling during metamorphosis. Curr Top Dev Biol 32 (1996) 205-235
    • (1996) Curr Top Dev Biol , vol.32 , pp. 205-235
    • Shi, Y.-B.1    Ishizuya-Oka, A.2
  • 90
    • 0035756689 scopus 로고    scopus 로고
    • Thyroid hormone regulation of apoptotic tissue remodeling during anuran metamorphosis
    • Shi Y.B., Fu L., Hsia S.C., Tomita A., and Buchholz D. Thyroid hormone regulation of apoptotic tissue remodeling during anuran metamorphosis. Cell Res 11 (2001) 245-252
    • (2001) Cell Res , vol.11 , pp. 245-252
    • Shi, Y.B.1    Fu, L.2    Hsia, S.C.3    Tomita, A.4    Buchholz, D.5
  • 91
    • 0027672251 scopus 로고
    • Differential expression of the 67 kDa laminin receptor in cancer
    • Sobel M.E. Differential expression of the 67 kDa laminin receptor in cancer. Semin Cancer Biol 4 (1993) 311-317
    • (1993) Semin Cancer Biol , vol.4 , pp. 311-317
    • Sobel, M.E.1
  • 92
    • 0032918582 scopus 로고    scopus 로고
    • Cell surface and substrate distribution of the 67-kDa laminin-binding protein determined by using a ligand photoaffinity probe
    • Starkey J.R., Uthanyakumar S., and Berglund D.L. Cell surface and substrate distribution of the 67-kDa laminin-binding protein determined by using a ligand photoaffinity probe. Cytometry 35 (1999) 37-47
    • (1999) Cytometry , vol.35 , pp. 37-47
    • Starkey, J.R.1    Uthanyakumar, S.2    Berglund, D.L.3
  • 93
    • 0029825963 scopus 로고    scopus 로고
    • Identification and characterization of a novel collagenase in Xenopus laevis: possible roles during frog development
    • Stolow M.A., Bauzon D.D., Li J., Sedgwick T., Liang V.C., Sang Q.A., et al. Identification and characterization of a novel collagenase in Xenopus laevis: possible roles during frog development. Mol Biol Cell 7 (1996) 1471-1483
    • (1996) Mol Biol Cell , vol.7 , pp. 1471-1483
    • Stolow, M.A.1    Bauzon, D.D.2    Li, J.3    Sedgwick, T.4    Liang, V.C.5    Sang, Q.A.6
  • 94
    • 0030972756 scopus 로고    scopus 로고
    • Cyclosporin A but not FK506 inhibits thyroid hormone-induced apoptosis in Xenopus tadpole intestinal epithelium
    • Su Y., Shi Y., and Shi Y.-B. Cyclosporin A but not FK506 inhibits thyroid hormone-induced apoptosis in Xenopus tadpole intestinal epithelium. FASEB J 11 (1997) 559-565
    • (1997) FASEB J , vol.11 , pp. 559-565
    • Su, Y.1    Shi, Y.2    Shi, Y.-B.3
  • 95
    • 0031455408 scopus 로고    scopus 로고
    • Thyroid hormone induces apoptosis in primary cell cultures of tadpole intestine: cell type specificity and effects of extracellular matrix
    • Su Y., Shi Y., Stolow M., and Shi Y.-B. Thyroid hormone induces apoptosis in primary cell cultures of tadpole intestine: cell type specificity and effects of extracellular matrix. J Cell Biol 139 (1997) 1533-1543
    • (1997) J Cell Biol , vol.139 , pp. 1533-1543
    • Su, Y.1    Shi, Y.2    Stolow, M.3    Shi, Y.-B.4
  • 96
    • 0031660713 scopus 로고    scopus 로고
    • Prognostic significance of stromelysin 3, gelatinase A, and urokinase expression in breast cancer
    • Tetu B., Brisson J., Lapointe H., and Bernard P. Prognostic significance of stromelysin 3, gelatinase A, and urokinase expression in breast cancer. Hum Pathol 29 (1998) 979-985
    • (1998) Hum Pathol , vol.29 , pp. 979-985
    • Tetu, B.1    Brisson, J.2    Lapointe, H.3    Bernard, P.4
  • 97
    • 0030087944 scopus 로고    scopus 로고
    • Supramolecular assembly of basement membranes
    • Timpl R., and Brown J.C. Supramolecular assembly of basement membranes. BioEssays 18 (1996) 123-132
    • (1996) BioEssays , vol.18 , pp. 123-132
    • Timpl, R.1    Brown, J.C.2
  • 98
    • 0032160115 scopus 로고    scopus 로고
    • Matrix metalloproteinases and their expression in mammary gland
    • Uria J.A., and Werb Z. Matrix metalloproteinases and their expression in mammary gland. Cell Res 8 (1998) 187-194
    • (1998) Cell Res , vol.8 , pp. 187-194
    • Uria, J.A.1    Werb, Z.2
  • 99
    • 0026701412 scopus 로고
    • Identification of multiple active growth factors in basement membrane Matrigel suggests caution in interpretation of cellular activity related to extracellular matrix components
    • Vukicevic S., Kleinman H.K., Luyten F.P., Roberts A.B., Roche N.S., and Reddi A.H. Identification of multiple active growth factors in basement membrane Matrigel suggests caution in interpretation of cellular activity related to extracellular matrix components. Exp Cell Res 202 (1992) 1-8
    • (1992) Exp Cell Res , vol.202 , pp. 1-8
    • Vukicevic, S.1    Kleinman, H.K.2    Luyten, F.P.3    Roberts, A.B.4    Roche, N.S.5    Reddi, A.H.6
  • 100
    • 0027220692 scopus 로고
    • Thyroid hormone-induced gene expression program for amphibian tail resorption
    • Wang Z., and Brown D.D. Thyroid hormone-induced gene expression program for amphibian tail resorption. J Biol Chem 268 (1993) 16270-16278
    • (1993) J Biol Chem , vol.268 , pp. 16270-16278
    • Wang, Z.1    Brown, D.D.2
  • 101
    • 11144298067 scopus 로고    scopus 로고
    • Matrix metalloproteinase stromelysin-3 in development and pathogenesis
    • Wei L., and Shi Y.-B. Matrix metalloproteinase stromelysin-3 in development and pathogenesis. Histol Histopathol 20 (2005) 177-185
    • (2005) Histol Histopathol , vol.20 , pp. 177-185
    • Wei, L.1    Shi, Y.-B.2
  • 102
    • 0029973269 scopus 로고    scopus 로고
    • Extracellular matrix remodeling and the regulation of epithelial-stromal interactions during differentiation and involution
    • Werb Z., Sympson C.J., Alexander C.M., Thomasset N., Lund L.R., MacAuley A., et al. Extracellular matrix remodeling and the regulation of epithelial-stromal interactions during differentiation and involution. Kidney Int Suppl 54 (1996) S68-S74
    • (1996) Kidney Int Suppl , vol.54
    • Werb, Z.1    Sympson, C.J.2    Alexander, C.M.3    Thomasset, N.4    Lund, L.R.5    MacAuley, A.6
  • 103
    • 0024892345 scopus 로고
    • Biochemistry and cell biology of amphibian metamorphosis with a special emphasis on the mechanism of removal of larval organs
    • Yoshizato K. Biochemistry and cell biology of amphibian metamorphosis with a special emphasis on the mechanism of removal of larval organs. Int Rev Cytol 119 (1989) 97-149
    • (1989) Int Rev Cytol , vol.119 , pp. 97-149
    • Yoshizato, K.1
  • 104
    • 0345518033 scopus 로고
    • Increased mRNA expression of a laminin-binding protein in human colon carcinoma: complete sequence of a full-length cDNA encoding the protein
    • Yow H.K., Wong J.M., Chen H.S., Lee C.G., Davis S., Steele Jr. G.D., and Chen L.B. Increased mRNA expression of a laminin-binding protein in human colon carcinoma: complete sequence of a full-length cDNA encoding the protein. Proc Natl Acad Sci U S A 85 (1988) 6394-6398
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 6394-6398
    • Yow, H.K.1    Wong, J.M.2    Chen, H.S.3    Lee, C.G.4    Davis, S.5    Steele Jr., G.D.6    Chen, L.B.7


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