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Volumn 7, Issue 8, 2012, Pages

Novel processed form of syndecan-1 shed from SCC-9 cells plays a role in cell migration

Author keywords

[No Author keywords available]

Indexed keywords

GELATINASE; SYNDECAN 1;

EID: 84865054658     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0043521     Document Type: Article
Times cited : (41)

References (39)
  • 2
    • 39749182345 scopus 로고    scopus 로고
    • The mammary epithelial cell secretome and its regulation by signal transduction pathways
    • Jacobs JM, Waters KM, Kathmann LE, Camp II DG, Wiley HS, et al. (2008) The mammary epithelial cell secretome and its regulation by signal transduction pathways. J Proteome Res 2: 558-569.
    • (2008) J Proteome Res , vol.2 , pp. 558-569
    • Jacobs, J.M.1    Waters, K.M.2    Kathmann, L.E.3    Camp II, D.G.4    Wiley, H.S.5
  • 3
    • 49149097964 scopus 로고    scopus 로고
    • Proteomic analysis of ovarian cancer cells reveals dynamic processes of protein secretion and shedding of extra-cellular domains
    • Faça VM, Ventura AP, Fitzgibbon MP, Pereira-Faça SR, Pitteri SJ, et al. (2008) Proteomic analysis of ovarian cancer cells reveals dynamic processes of protein secretion and shedding of extra-cellular domains. PLoS One 3(6): e2425 Available: http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0002425.
    • (2008) PLoS One , vol.3 , Issue.6
    • Faça, V.M.1    Ventura, A.P.2    Fitzgibbon, M.P.3    Pereira-Faça, S.R.4    Pitteri, S.J.5
  • 4
    • 80052524240 scopus 로고    scopus 로고
    • Discovery of IL-18 as a novel secreted protein contributing to doxorubicin resistance by comparative secretome analysis of MCF-7 and MCF/Dox
    • Available, Accessed 2012 Jul 26
    • Yao L, Zhang Y, Chen K, Hu X, Xu L X (2011) Discovery of IL-18 as a novel secreted protein contributing to doxorubicin resistance by comparative secretome analysis of MCF-7 and MCF/Dox. PLoS One 6:e24684. Available: http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0024684. Accessed 2012 Jul 26.
    • (2011) PLoS One , vol.6
    • Yao, L.1    Zhang, Y.2    Chen, K.3    Hu, X.4    Xu, L.X.5
  • 5
    • 0033868818 scopus 로고    scopus 로고
    • A novel proteolytic cleavage involved in Notch signaling: the role of the disintegrin-metalloprotease TACE
    • Brou C, Logeat F, Gupta N, Bessia C, LeBail O, et al. (2000) A novel proteolytic cleavage involved in Notch signaling: the role of the disintegrin-metalloprotease TACE. Mol Cell 5: 207-16.
    • (2000) Mol Cell , vol.5 , pp. 207-216
    • Brou, C.1    Logeat, F.2    Gupta, N.3    Bessia, C.4    LeBail, O.5
  • 6
    • 0035956428 scopus 로고    scopus 로고
    • Proteolytic release of CD44 intracellular domain and its role in the CD44 signaling pathway
    • Okamoto I, Kawano Y, Murakami D, Sasayama T, Araki N, et al. (2001) Proteolytic release of CD44 intracellular domain and its role in the CD44 signaling pathway. J Cell Biol 155: 755-62.
    • (2001) J Cell Biol , vol.155 , pp. 755-762
    • Okamoto, I.1    Kawano, Y.2    Murakami, D.3    Sasayama, T.4    Araki, N.5
  • 7
    • 0036796421 scopus 로고    scopus 로고
    • The disintegrin/metalloprotease ADAM 10 is essential for Notch signaling but not for alpha-secretase activity in fibroblasts
    • Hartmann D, de Strooper B, Serneels L, Craessaerts K, Herreman A, et al. (2002) The disintegrin/metalloprotease ADAM 10 is essential for Notch signaling but not for alpha-secretase activity in fibroblasts. Hum Mol Genet 11: 2615-24.
    • (2002) Hum Mol Genet , vol.11 , pp. 2615-2624
    • Hartmann, D.1    de Strooper, B.2    Serneels, L.3    Craessaerts, K.4    Herreman, A.5
  • 8
    • 18344380083 scopus 로고    scopus 로고
    • A presenilin-1/gamma-secretase cleavage releases the E-cadherin intracellular domain and regulates disassembly of adherens junctions
    • Marambaud P, Shioi J, Serban G, Georgakopoulos A, Sarner S, et al. (2002) A presenilin-1/gamma-secretase cleavage releases the E-cadherin intracellular domain and regulates disassembly of adherens junctions. EMBO J 21: 1948-56.
    • (2002) EMBO J , vol.21 , pp. 1948-1956
    • Marambaud, P.1    Shioi, J.2    Serban, G.3    Georgakopoulos, A.4    Sarner, S.5
  • 9
    • 84857537977 scopus 로고    scopus 로고
    • Human platelet-rich plasma- and extracellular matrix-derived peptides promote impaired cutaneous wound healing in vivo
    • Available, Accessed 2012 Jul 26
    • Demidova-Rice TN, Wolf L, Deckenback J, Hamblin MR, Herman IM (2012) Human platelet-rich plasma- and extracellular matrix-derived peptides promote impaired cutaneous wound healing in vivo. PLoS One 7(2): e32146. Available: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3285658/pdf/pone.0032146.pdf. Accessed 2012 Jul 26.
    • (2012) PLoS One , vol.7 , Issue.2
    • Demidova-Rice, T.N.1    Wolf, L.2    Deckenback, J.3    Hamblin, M.R.4    Herman, I.M.5
  • 10
    • 77956646126 scopus 로고    scopus 로고
    • Proteoglycan in health and disease: the multiple roles of syndecan shedding
    • Manon-Jensen T, Itoh Y, Couchman JR, (2010) Proteoglycan in health and disease: the multiple roles of syndecan shedding. FEBS Journal 277: 3876-3889.
    • (2010) FEBS Journal , vol.277 , pp. 3876-3889
    • Manon-Jensen, T.1    Itoh, Y.2    Couchman, J.R.3
  • 13
    • 33645709062 scopus 로고    scopus 로고
    • Reduced syndecan-1 expression is correlated with the histological grade of malignancy at the deep invasive front in oral squamous cell carcinoma
    • Kurokawa H, Zhang M, Matsumoto S, Yamashita Y, Tanaka T, et al. (2006) Reduced syndecan-1 expression is correlated with the histological grade of malignancy at the deep invasive front in oral squamous cell carcinoma. J Oral Pathol Med. 35(5): 301-306.
    • (2006) J Oral Pathol Med , vol.35 , Issue.5 , pp. 301-306
    • Kurokawa, H.1    Zhang, M.2    Matsumoto, S.3    Yamashita, Y.4    Tanaka, T.5
  • 14
    • 31544459197 scopus 로고    scopus 로고
    • Correlation between reduction of syndecan-1 expression and clinico-pathological parameters in squamous cell carcinoma of tongue
    • Ro Y, Muramatsu T, Shima K, Yajima Y, Shibahara T, et al. (2006) Correlation between reduction of syndecan-1 expression and clinico-pathological parameters in squamous cell carcinoma of tongue. Int J Oral Maxillofac Surg. 35(3): 252-257.
    • (2006) Int J Oral Maxillofac Surg , vol.35 , Issue.3 , pp. 252-257
    • Ro, Y.1    Muramatsu, T.2    Shima, K.3    Yajima, Y.4    Shibahara, T.5
  • 15
    • 55049133250 scopus 로고    scopus 로고
    • Metadegradomics: toward in vivo quantitative degradomics of proteolytic post-translational modifications of the cancer proteome
    • Doucet A, Butler GS, Rodríguez D, Prudova A, Overall CM, (2008) Metadegradomics: toward in vivo quantitative degradomics of proteolytic post-translational modifications of the cancer proteome. Mol Cell Proteomics 7(10): 1925-1951.
    • (2008) Mol Cell Proteomics , vol.7 , Issue.10 , pp. 1925-1951
    • Doucet, A.1    Butler, G.S.2    Rodríguez, D.3    Prudova, A.4    Overall, C.M.5
  • 16
    • 78349311747 scopus 로고    scopus 로고
    • Cancer secretomics reveal pathophysiological pathways in cancer molecular oncology
    • Karagiannis GS, Pavlou MP, Diamandis EP, (2010) Cancer secretomics reveal pathophysiological pathways in cancer molecular oncology. Mol Oncol 4 (6): 496-510.
    • (2010) Mol Oncol , vol.4 , Issue.6 , pp. 496-510
    • Karagiannis, G.S.1    Pavlou, M.P.2    Diamandis, E.P.3
  • 17
    • 34250312341 scopus 로고    scopus 로고
    • The biochemical, biological, and pathological kaleidoscope of cell surface substrates processed by matrix metalloproteinases
    • Cauwe B, Van den Steen PE, Opdenakker G, (2007) The biochemical, biological, and pathological kaleidoscope of cell surface substrates processed by matrix metalloproteinases. Crit Rev Biochem Mol Biol 42(3): 113-185.
    • (2007) Crit Rev Biochem Mol Biol , vol.42 , Issue.3 , pp. 113-185
    • Cauwe, B.1    van den Steen, P.E.2    Opdenakker, G.3
  • 18
    • 77952909304 scopus 로고    scopus 로고
    • Candidate serological biomarkers for cancer identified from the secretomes of 23 cancer cell lines and the human protein atlas
    • Wu CC, Hsu CW, Chen CD, Yu CJ, Chang KP, et al. (2010) Candidate serological biomarkers for cancer identified from the secretomes of 23 cancer cell lines and the human protein atlas. Mol Cell Proteomics 9: 1100-1117.
    • (2010) Mol Cell Proteomics , vol.9 , pp. 1100-1117
    • Wu, C.C.1    Hsu, C.W.2    Chen, C.D.3    Yu, C.J.4    Chang, K.P.5
  • 21
    • 33645709062 scopus 로고    scopus 로고
    • Reduced syndecan-1 expression is correlated with the histological grade of malignancy at the deep invasive front in oral squamous cell carcinoma
    • Kurokawa H, Zhang M, Matsumoto S, Yamashita Y, Tanaka T, et al. (2006) Reduced syndecan-1 expression is correlated with the histological grade of malignancy at the deep invasive front in oral squamous cell carcinoma. J Oral Pathology & Medicine 35 (5): 301-306.
    • (2006) J Oral Pathology & Medicine , vol.35 , Issue.5 , pp. 301-306
    • Kurokawa, H.1    Zhang, M.2    Matsumoto, S.3    Yamashita, Y.4    Tanaka, T.5
  • 22
    • 70350668613 scopus 로고    scopus 로고
    • Active site determinants of substrate recognition by the metalloproteinases TACE and ADAM10
    • Caescu CI, Jeschke GR, Turk BE, (2010) Active site determinants of substrate recognition by the metalloproteinases TACE and ADAM10. Biochem J 424 (1): 79-88.
    • (2010) Biochem J , vol.424 , Issue.1 , pp. 79-88
    • Caescu, C.I.1    Jeschke, G.R.2    Turk, B.E.3
  • 23
    • 0142103466 scopus 로고    scopus 로고
    • Cleavage of syndecan-1 by membrane type matrix metalloproteinase-1 stimulates cell migration
    • Endo K, Takino T, Miyamori H Kinsen H, Yoshizaki T, et al. (2003) Cleavage of syndecan-1 by membrane type matrix metalloproteinase-1 stimulates cell migration. J Biol Chem 278 (42): 40764-40770.
    • (2003) J Biol Chem , vol.278 , Issue.42 , pp. 40764-40770
    • Endo, K.1    Takino, T.2    Miyamori, H.3    Kinsen, H.4    Yoshizaki, T.5
  • 24
    • 77950480108 scopus 로고    scopus 로고
    • Degradation of tropoelastin by matrix metalloproteinases -cleavage site specificities and release of matrikines
    • Heinz A, Jung M C, Duca L, Sippl W, Taddese S, et al. (2010) Degradation of tropoelastin by matrix metalloproteinases -cleavage site specificities and release of matrikines. FEBS J 277 (8): 1939-1956.
    • (2010) FEBS J , vol.277 , Issue.8 , pp. 1939-1956
    • Heinz, A.1    Jung, M.C.2    Duca, L.3    Sippl, W.4    Taddese, S.5
  • 25
    • 62349114465 scopus 로고    scopus 로고
    • Differential roles for membrane-bound and soluble syndecan-1 (CD138) in breast cancer progression
    • Nikolova V, Koo CY, Ibrahim SA, Wang Z, Spillmann D, et al. (2009) Differential roles for membrane-bound and soluble syndecan-1 (CD138) in breast cancer progression. Carcinogenesis. 30(3): 397-407.
    • (2009) Carcinogenesis , vol.30 , Issue.3 , pp. 397-407
    • Nikolova, V.1    Koo, C.Y.2    Ibrahim, S.A.3    Wang, Z.4    Spillmann, D.5
  • 26
    • 0037100282 scopus 로고    scopus 로고
    • Soluble syndecan-1 promotes growth of myeloma tumors in vivo
    • Yang Y, Yaccoby S, Liu W, Langford JK, Pumphrey CY, et al. (2002) Soluble syndecan-1 promotes growth of myeloma tumors in vivo. Blood. 100(2): 610-617.
    • (2002) Blood , vol.100 , Issue.2 , pp. 610-617
    • Yang, Y.1    Yaccoby, S.2    Liu, W.3    Langford, J.K.4    Pumphrey, C.Y.5
  • 28
    • 0037622031 scopus 로고    scopus 로고
    • Syndecan-1-mediated cell spreading requires signaling by αvβ3 integrins in human breast carcinoma cells
    • Beauvais DM, Rapraeger AC, (2003) Syndecan-1-mediated cell spreading requires signaling by αvβ3 integrins in human breast carcinoma cells. Exp Cell Res 286 (2): 219-232.
    • (2003) Exp Cell Res , vol.286 , Issue.2 , pp. 219-232
    • Beauvais, D.M.1    Rapraeger, A.C.2
  • 29
    • 33746067151 scopus 로고    scopus 로고
    • Syndecan-1 regulates αvβ5 integrin activity in B82L fibroblasts
    • McQuade KJ, Beauvais DM, Burbach BJ, Rapraeger AC, (2006) Syndecan-1 regulates αvβ5 integrin activity in B82L fibroblasts. J Cell Sci 119 (12): 2445-2456.
    • (2006) J Cell Sci , vol.119 , Issue.12 , pp. 2445-2456
    • McQuade, K.J.1    Beauvais, D.M.2    Burbach, B.J.3    Rapraeger, A.C.4
  • 30
    • 0023852747 scopus 로고
    • Normal keratinization in a spontaneously immortalized aneuploid human keratinocyte cell line
    • Boukamp P, Petrussevska RT, Breitkreutz D, Hornung J, Markham A, et al. (1988) Normal keratinization in a spontaneously immortalized aneuploid human keratinocyte cell line. J Cell Biol 106 (3): 761-771.
    • (1988) J Cell Biol , vol.106 , Issue.3 , pp. 761-771
    • Boukamp, P.1    Petrussevska, R.T.2    Breitkreutz, D.3    Hornung, J.4    Markham, A.5
  • 31
    • 67649804558 scopus 로고    scopus 로고
    • Analysis of Intracellular substrates and products of thimet oligopeptidase in human embryonic kidney 293 cells
    • Berti DA, Morano C, Russo LC, Castro LM, Cunha FM, et al. (2009) Analysis of Intracellular substrates and products of thimet oligopeptidase in human embryonic kidney 293 cells. J Biol Chem 284 (21): 14105-14116.
    • (2009) J Biol Chem , vol.284 , Issue.21 , pp. 14105-14116
    • Berti, D.A.1    Morano, C.2    Russo, L.C.3    Castro, L.M.4    Cunha, F.M.5
  • 32
    • 84984933087 scopus 로고    scopus 로고
    • The SCX/IMAC enrichment approach for global phosphorylation analysis by mass spectrometry
    • Villén J, Gygi SP, (2008) The SCX/IMAC enrichment approach for global phosphorylation analysis by mass spectrometry. Nat Protocol 3 (10): 1630-1638.
    • (2008) Nat Protocol , vol.3 , Issue.10 , pp. 1630-1638
    • Villén, J.1    Gygi, S.P.2
  • 33
    • 84855544503 scopus 로고    scopus 로고
    • Hemorrhagic activity of HF3, a snake venom metalloproteinase: insights from the proteomic analysis of mouse skin and blood plasma
    • Paes Leme AF, Sherman NE, Smalley DM, Sizukusa LO, Oliveira AK, et al. (2012) Hemorrhagic activity of HF3, a snake venom metalloproteinase: insights from the proteomic analysis of mouse skin and blood plasma. J Proteome Res 11(1): 279-291.
    • (2012) J Proteome Res , vol.11 , Issue.1 , pp. 279-291
    • Paes Leme, A.F.1    Sherman, N.E.2    Smalley, D.M.3    Sizukusa, L.O.4    Oliveira, A.K.5
  • 34
    • 70449428630 scopus 로고    scopus 로고
    • Wound exudate as a proteomic window to reveal different mechanisms of tissue damage by snake venom toxins
    • Escalante T, Rucavado A, Pinto AFM, Terra RMS, Gutirrez JM, et al. (2009) Wound exudate as a proteomic window to reveal different mechanisms of tissue damage by snake venom toxins. J Proteome Res 8 (11): 5120-5131.
    • (2009) J Proteome Res , vol.8 , Issue.11 , pp. 5120-5131
    • Escalante, T.1    Rucavado, A.2    Pinto, A.F.M.3    Terra, R.M.S.4    Gutirrez, J.M.5
  • 35
    • 77956298562 scopus 로고    scopus 로고
    • Differential proteomic analysis distinguishes tissue repair biomarker signatures in wound exudates obtained from normal healing and chronic wounds
    • Eming SA, Koch M, Krieger A, Brachvogel B, Kreft S, et al. (2010) Differential proteomic analysis distinguishes tissue repair biomarker signatures in wound exudates obtained from normal healing and chronic wounds. J Proteome Res 9 (9): 4758-4766.
    • (2010) J Proteome Res , vol.9 , Issue.9 , pp. 4758-4766
    • Eming, S.A.1    Koch, M.2    Krieger, A.3    Brachvogel, B.4    Kreft, S.5
  • 36
    • 3242731195 scopus 로고    scopus 로고
    • A model for random sampling and estimation of relative protein abundance in shotgun proteomics
    • Liu H, Sadygov RG, Yates JR III, (2004) a model for random sampling and estimation of relative protein abundance in shotgun proteomics. Anal Chem 76 (14): 4193-4201.
    • (2004) Anal Chem , vol.76 , Issue.14 , pp. 4193-4201
    • Liu, H.1    Sadygov, R.G.2    Yates III, J.R.3
  • 37
    • 34347218991 scopus 로고    scopus 로고
    • In vitro scratch assay: a convenient and inexpensive method for analysis of cell migration in vitro
    • Liang CC, Park AY, Guan JL, (2007) In vitro scratch assay: a convenient and inexpensive method for analysis of cell migration in vitro. Nat Protocol 2(2): 329-33.
    • (2007) Nat Protocol , vol.2 , Issue.2 , pp. 329-333
    • Liang, C.C.1    Park, A.Y.2    Guan, J.L.3
  • 38
    • 40349089672 scopus 로고    scopus 로고
    • Cell-Substrate Adhesion Assays
    • 2001 John Wiley & Sons, Inc. DOI 10.1002/0471143030.cb0901s00
    • Humphries MJ (2001) Cell-Substrate Adhesion Assays. Current Protocols in Cell Biology. 2001 John Wiley & Sons, Inc. DOI 10.1002/0471143030.cb0901s00.
    • (2001) Current Protocols in Cell Biology
    • Humphries, M.J.1
  • 39
    • 60549104248 scopus 로고    scopus 로고
    • Analysis of the subproteomes of proteinases and heparin-binding toxins of eight bothrops venoms
    • Paes Leme AF, Kitano E, Furtado MF, Valente R, Camargo ACM, et al. (2009) Analysis of the subproteomes of proteinases and heparin-binding toxins of eight bothrops venoms. Proteomics 9: 733-745.
    • (2009) Proteomics , vol.9 , pp. 733-745
    • Paes Leme, A.F.1    Kitano, E.2    Furtado, M.F.3    Valente, R.4    Camargo, A.C.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.