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Volumn 11, Issue 11, 2012, Pages 1320-1339

Secretomic analysis identifies alpha-1 antitrypsin (A1AT) as a required protein in cancer cell migration, invasion, and pericellular fibronectin assembly for facilitating lung colonization of lung adenocarcinoma cells

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA 1 ANTITRYPSIN; DIPEPTIDYL PEPTIDASE IV; FIBRONECTIN;

EID: 84869232807     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M112.017384     Document Type: Article
Times cited : (62)

References (107)
  • 1
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • Hanahan, D., and Weinberg, R. A. (2000) The hallmarks of cancer. Cell. 100, 57-70 (Pubitemid 30046295)
    • (2000) Cell , vol.100 , Issue.1 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 3
    • 77954321859 scopus 로고    scopus 로고
    • Metastatic non-small-cell lung cancer: ESMO Clinical Practice Guidelines for diagnosis, treatment and follow-up
    • ESMO Guidelines Working Group
    • D'Addario, G., Früh, M., Reck, M., Baumann, P., Klepetko, W., Felip, E., and ESMO Guidelines Working Group. (2010) Metastatic non-small-cell lung cancer: ESMO Clinical Practice Guidelines for diagnosis, treatment and follow-up. Ann. Oncol. 21, 116-119
    • (2010) Ann. Oncol. , vol.21 , pp. 116-119
    • D'Addario, G.1    Früh, M.2    Reck, M.3    Baumann, P.4    Klepetko, W.5    Felip, E.6
  • 4
    • 0030769477 scopus 로고    scopus 로고
    • General mechanisms of metastasis
    • Woodhouse, E. C., Chuaqui, R. F., and Liotta, L. A. (1997) General mechanisms of metastasis. Cancer 80, 1529-1537 (Pubitemid 27444024)
    • (1997) Cancer , vol.80 , Issue.8 SUPPL. , pp. 1529-1537
    • Woodhouse, E.C.1    Chuaqui, R.F.2    Liotta, L.A.3
  • 5
    • 79960898490 scopus 로고    scopus 로고
    • Simple experimental and spontaneous metastasis assays in mice
    • Box, G. M., and Eccles, S. A. (2011) Simple experimental and spontaneous metastasis assays in mice. Methods Mol Biol. 769, 311-329
    • (2011) Methods Mol Biol. , vol.769 , pp. 311-329
    • Box, G.M.1    Eccles, S.A.2
  • 6
    • 16244367163 scopus 로고    scopus 로고
    • Modeling metastasis in vivo
    • DOI 10.1093/carcin/bgh261
    • Khanna, C., and Hunter, K. (2005) Modeling metastasis in vivo. Carcinogenesis 26, 513-523 (Pubitemid 41214139)
    • (2005) Carcinogenesis , vol.26 , Issue.3 , pp. 513-523
    • Khanna, C.1    Hunter, K.2
  • 7
    • 33750316225 scopus 로고    scopus 로고
    • Models for spontaneous metastasis
    • Fidler, I. J., (2006) Models for spontaneous metastasis. Cancer Res. 66, 9787
    • (2006) Cancer Res. , vol.66 , pp. 9787
    • Fidler, I.J.1
  • 8
    • 0033818171 scopus 로고    scopus 로고
    • Signal peptide-dependent protein transport in Bacillus subtilis: A genome-based survey of the secretome
    • Tjalsma, H., Bolhuis, A., Jongbloed, J. D., Bron, S., and van Dijl, J. M. (2000) Signal peptide-dependent protein transport in Bacillus subtilis: a genome-based survey of the secretome. Microbiol. Mol. Biol. Rev. 64, 515-547
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 515-547
    • Tjalsma, H.1    Bolhuis, A.2    Jongbloed, J.D.3    Bron, S.4    Van Dijl, J.M.5
  • 9
    • 22044442559 scopus 로고    scopus 로고
    • Differential proteome analysis of conditioned media to detect Smad4 regulated secreted biomarkers in colon cancer
    • DOI 10.1002/pmic.200401188
    • Volmer, M. W., Stühler, K., Zapatka, M., Schöneck, A., Klein-Scory, S., Schmiegel, W., Meyer, H. E., and Schwarte-Waldhoff, I. (2005) Differential proteome analysis of conditioned media to detect Smad4 regulated secreted biomarkers in colon cancer. Proteomics. 5, 2587-2601 (Pubitemid 40966486)
    • (2005) Proteomics , vol.5 , Issue.10 , pp. 2587-2601
    • Volmer, M.W.1    Stuhler, K.2    Zapatka, M.3    Schoneck, A.4    Klein-Scory, S.5    Schmiegel, W.6    Meyer, H.E.7    Schwarte-Waldhoff, I.8
  • 11
    • 76649094917 scopus 로고    scopus 로고
    • Proteomics analysis of A33 immunoaffinity-purified exosomes released from the human colon tumor cell line LIM1215 reveals a tissue-specific protein signature
    • Mathivanan, S., Lim, J. W., Tauro, B. J., Ji, H., Moritz, R. L., and Simpson, R. J. (2010) Proteomics analysis of A33 immunoaffinity-purified exosomes released from the human colon tumor cell line LIM1215 reveals a tissue-specific protein signature. Mol. Cell. Proteomics 9, 197-208
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 197-208
    • Mathivanan, S.1    Lim, J.W.2    Tauro, B.J.3    Ji, H.4    Moritz, R.L.5    Simpson, R.J.6
  • 12
    • 0035902141 scopus 로고    scopus 로고
    • The microenvironment of the tumour-host interface
    • Liotta, L. A., and Kohn, E. C. (2001) The microenvironment of the tumour-host interface. Nature 411, 375-379
    • (2001) Nature , vol.411 , pp. 375-379
    • Liotta, L.A.1    Kohn, E.C.2
  • 13
    • 15544384612 scopus 로고    scopus 로고
    • Involvement of cathepsins in the invasion, metastasis and proliferation of cancer cells
    • Nomura, T., and Katunuma, N. (2005) Involvement of cathepsins in the invasion, metastasis and proliferation of cancer cells. J. Med. Invest. 52, 1-9
    • (2005) J. Med. Invest. , vol.52 , pp. 1-9
    • Nomura, T.1    Katunuma, N.2
  • 14
    • 23444459571 scopus 로고
    • The biology of SPARC, a protein that modulates cell-matrix interactions
    • Lane, T. F., and Sage, E. H. (1994) The biology of SPARC, a protein that modulates cell-matrix interactions. FASEB J. 8, 163-173 (Pubitemid 24067139)
    • (1994) FASEB Journal , vol.8 , Issue.2 , pp. 163-173
    • Lane, T.F.1    Helene, S.E.2
  • 16
    • 71549131311 scopus 로고    scopus 로고
    • Cell secretome analysis using hollow fiber culture system leads to the discovery of CLIC1 protein as a novel plasma marker for nasopharyngeal carcinoma
    • Chang, Y. H., Wu, C. C., Chang, K. P., Yu, J. S., Chang, Y. C., and Liao, P. C. (2009) Cell secretome analysis using hollow fiber culture system leads to the discovery of CLIC1 protein as a novel plasma marker for nasopharyngeal carcinoma. J. Proteome Res. 8, 5465-5474
    • (2009) J. Proteome Res. , vol.8 , pp. 5465-5474
    • Chang, Y.H.1    Wu, C.C.2    Chang, K.P.3    Yu, J.S.4    Chang, Y.C.5    Liao, P.C.6
  • 17
    • 0035503379 scopus 로고    scopus 로고
    • Proteomics in neuroscience: From protein to network
    • Grant, S. G., and Blackstock, W. P. (2001) Proteomics in neuroscience: from protein to network. J. Neurosci. 21, 8315-8318 (Pubitemid 33051427)
    • (2001) Journal of Neuroscience , vol.21 , Issue.21 , pp. 8315-8318
    • Grant, S.G.N.1    Blackstock, W.P.2
  • 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, C. C., Hsu, C. W., Chen, C. D., Yu, C. J., Chang, K. P., Tai, D. I., Liu, H. P., Su, W. H., Chang, Y. S., and Yu, J. S. (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    Tai, D.I.6    Liu, H.P.7    Su, W.H.8    Chang, Y.S.9    Yu, J.S.10
  • 20
    • 73649116726 scopus 로고    scopus 로고
    • Identification of serum biomarkers for colorectal cancer metastasis using a differential secretome approach
    • Xue, H., Lü, B., Zhang, J., Wu, M., Huang, Q., Wu, Q., Sheng, H., Wu, D., Hu, J., and Lai, M. (2010) Identification of serum biomarkers for colorectal cancer metastasis using a differential secretome approach. J. Proteome Res. 9, 545-555
    • (2010) J. Proteome Res. , vol.9 , pp. 545-555
    • Xue, H.1    Lü, B.2    Zhang, J.3    Wu, M.4    Huang, Q.5    Wu, Q.6    Sheng, H.7    Wu, D.8    Hu, J.9    Lai, M.10
  • 21
    • 72149118728 scopus 로고    scopus 로고
    • Alterations in cellular proteome and secretome upon differentiation from monocyte to macrophage by treatment with phorbol myristate acetate: Insights into biological processes
    • Sintiprungrat, K., Singhto, N., Sinchaikul, S., Chen, S. T., and Thongboonkerd, V. (2010) Alterations in cellular proteome and secretome upon differentiation from monocyte to macrophage by treatment with phorbol myristate acetate: insights into biological processes. J. Proteomics 73, 602-618
    • (2010) J. Proteomics , vol.73 , pp. 602-618
    • Sintiprungrat, K.1    Singhto, N.2    Sinchaikul, S.3    Chen, S.T.4    Thongboonkerd, V.5
  • 22
    • 39749084641 scopus 로고    scopus 로고
    • Active Caspase-1 Is a Regulator of Unconventional Protein Secretion
    • DOI 10.1016/j.cell.2007.12.040, PII S0092867408001116
    • Keller, M., Rüegg, A., Werner, S., and Beer, H. D. (2008) Active caspase-1 is a regulator of unconventional protein secretion. Cell 132, 818-831 (Pubitemid 351312798)
    • (2008) Cell , vol.132 , Issue.5 , pp. 818-831
    • Keller, M.1    Ruegg, A.2    Werner, S.3    Beer, H.-D.4
  • 23
    • 77952722630 scopus 로고    scopus 로고
    • Quantitative proteomics approach for identifying protein-drug interactions in complex mixtures using protein stability measurements
    • West, G. M., Tucker, C. L., Xu, T., Park, S. K., Han, X., Yates, J. R. 3rd, and Fitzgerald, M. C. (2010) Quantitative proteomics approach for identifying protein-drug interactions in complex mixtures using protein stability measurements. Proc. Natl. Acad. Sci. U.S.A. 107, 9078-9082
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 9078-9082
    • West, G.M.1    Tucker, C.L.2    Xu, T.3    Park, S.K.4    Han, X.5    Yates III, J.R.6    Fitzgerald, M.C.7
  • 24
    • 0026904364 scopus 로고
    • Characterization of the mucin differentiation in human lung adenocarcinoma cell lines
    • Yang, P. C., Luh, K. T., Wu, R., and Wu, C. W. (1992) Characterization of the mucin differentiation in human lung adenocarcinoma cell lines. Am. J. Respir. Cell Mol. Biol. 7, 161-171
    • (1992) Am. J. Respir. Cell Mol. Biol. , vol.7 , pp. 161-171
    • Yang, P.C.1    Luh, K.T.2    Wu, R.3    Wu, C.W.4
  • 27
    • 21244488593 scopus 로고    scopus 로고
    • The transcriptional factor YY1 upregulates the novel invasion suppressor HLJ1 expression and inhibits cancer cell invasion
    • DOI 10.1038/sj.onc.1208573
    • Wang, C. C., Tsai, M. F., Hong, T. M., Chang, G. C., Chen, C. Y., Yang, W. M., Chen, J. J., and Yang, P. C. (2005) The transcriptional factor YY1 upregulates the novel invasion suppressor HLJ1 expression and inhibits cancer cell invasion. Oncogene 24, 4081-4093 (Pubitemid 40897054)
    • (2005) Oncogene , vol.24 , Issue.25 , pp. 4081-4093
    • Wang, C.-C.1    Tsai, M.-F.2    Hong, T.-M.3    Chang, G.-C.4    Chen, C.-Y.5    Yang, W.-M.6    Chen, J.J.W.7    Yang, P.-C.8
  • 28
    • 32644448252 scopus 로고    scopus 로고
    • The tumor suppressor DAPK inhibits cell motility by blocking the integrin-mediated polarity pathway
    • Kuo, J. C., Wang, W. J., Yao, C. C., Wu, P. R., and Chen, R. H. (2006) The tumor suppressor DAPK inhibits cell motility by blocking the integrin-mediated polarity pathway. J. Cell Biol. 172, 619-631
    • (2006) J. Cell Biol. , vol.172 , pp. 619-631
    • Kuo, J.C.1    Wang, W.J.2    Yao, C.C.3    Wu, P.R.4    Chen, R.H.5
  • 29
    • 60849139466 scopus 로고    scopus 로고
    • Proteomics analysis of nasopharyngeal carcinoma cell secretome using a hollow fiber culture system and mass spectrometry
    • Wu, H. Y., Chang, Y. H., Chang, Y. C., and Liao, P. C. (2009) Proteomics analysis of nasopharyngeal carcinoma cell secretome using a hollow fiber culture system and mass spectrometry. J. Proteome Res. 8, 380-389
    • (2009) J. Proteome Res. , vol.8 , pp. 380-389
    • Wu, H.Y.1    Chang, Y.H.2    Chang, Y.C.3    Liao, P.C.4
  • 30
    • 79952382501 scopus 로고    scopus 로고
    • Quantitative secretome analysis reveals that COL6A1 is a metastasis-associated protein using stacking gel-aided purification combined with iTRAQ labeling
    • Chiu, K. H., Chang, Y. H., Wu, Y. S., Lee, S. H., and Liao, P. C. (2011) Quantitative secretome analysis reveals that COL6A1 is a metastasis-associated protein using stacking gel-aided purification combined with iTRAQ labeling. J. Proteome Res. 10, 1110-1125
    • (2011) J. Proteome Res. , vol.10 , pp. 1110-1125
    • Chiu, K.H.1    Chang, Y.H.2    Wu, Y.S.3    Lee, S.H.4    Liao, P.C.5
  • 31
    • 85047688517 scopus 로고    scopus 로고
    • Minimum formalin fixation time for consistent estrogen receptor immunohistochemical staining of invasive breast carcinoma
    • DOI 10.1309/QPHD-RB00-QXGM-UQ9N
    • Goldstein, N. S., Ferkowicz, M., Odish, E., Mani, A., and Hastah, F. (2003) Minimum formalin fixation time for consistent estrogen receptor immunohistochemical staining of invasive breast carcinoma. Am. J. Clin. Pathol. 120, 86-92 (Pubitemid 37046374)
    • (2003) American Journal of Clinical Pathology , vol.120 , Issue.1 , pp. 86-92
    • Goldstein, N.S.1    Ferkowicz, M.2    Odish, E.3    Mani, A.4    Hastah, F.5
  • 32
    • 0032508633 scopus 로고    scopus 로고
    • Lung endothelial dipeptidyl peptidase IV promotes adhesion and metastasis of rat breast cancer cells via tumor cell surface-associated fibronectin
    • DOI 10.1074/jbc.273.37.24207
    • Cheng, H. C., Abdel-Ghany, M., Elble, R. C., and Pauli, B. U. (1998) Lung endothelial dipeptidyl peptidase IV promotes adhesion and metastasis of rat breast cancer cells via tumor cell surface-associated fibronectin. J. Biol. Chem. 273, 24207-24215 (Pubitemid 28435768)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.37 , pp. 24207-24215
    • Cheng, H.-C.1    Abdel-Ghany, M.2    Elble, R.C.3    Pauli, B.U.4
  • 33
    • 0043092068 scopus 로고    scopus 로고
    • A Novel Consensus Motif in Fibronectin Mediates Dipeptidyl Peptidase IV Adhesion and Metastasis
    • DOI 10.1074/jbc.M303424200
    • Cheng, H. C., Abdel-Ghany, M., and Pauli, B. U. (2003) A novel consensus motif in fibronectin mediates dipeptidyl peptidase IV adhesion and metastasis. J. Biol. Chem. 278, 24600-24607 (Pubitemid 37548613)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.27 , pp. 24600-24607
    • Cheng, H.-C.1    Abdel-Ghany, M.2    Pauli, B.U.3
  • 35
    • 0002294347 scopus 로고
    • A simple sequentially rejective multiple test procedure
    • Holm, S. (1979) A simple sequentially rejective multiple test procedure. Scand. J. Statist. 6, 65-70
    • (1979) Scand. J. Statist. , vol.6 , pp. 65-70
    • Holm, S.1
  • 36
    • 80053345905 scopus 로고    scopus 로고
    • SignalP 4.0: Discriminating signal peptides from transmembrane regions
    • Thomas N. P., Søren, B., Gunnar, V. H., and Henrik, N. (2011) SignalP 4.0: discriminating signal peptides from transmembrane regions. Nat. Methods 8, 785-786
    • (2011) Nat. Methods , vol.8 , pp. 785-786
    • Thomas, N.P.1    Søren, B.2    Gunnar, V.H.3    Henrik, N.4
  • 38
    • 0034899781 scopus 로고    scopus 로고
    • Evaluation of methods for the prediction of membrane spanning regions
    • Möller, S., Croning, M. D., and Apweiler, R. Evaluation of methods for the prediction of membrane spanning regions. (2001) Bioinformatics 17, 646-653 (Pubitemid 32707587)
    • (2001) Bioinformatics , vol.17 , Issue.7 , pp. 646-653
    • Moller, S.1    Croning, M.D.R.2    Apweiler, R.3
  • 39
    • 70350449455 scopus 로고    scopus 로고
    • ExoCarta: A compendium of exosomal proteins and RNA
    • Mathivanan, S., and Simpson, R. J. (2009) ExoCarta: A compendium of exosomal proteins and RNA. Proteomics 9, 4997-5000
    • (2009) Proteomics , vol.9 , pp. 4997-5000
    • Mathivanan, S.1    Simpson, R.J.2
  • 40
    • 77956404647 scopus 로고    scopus 로고
    • Exosomes: Extracellular organelles important in intercellular communication
    • Mathivanan, S., Ji, H., and Simpson, R. J. (2010) Exosomes: extracellular organelles important in intercellular communication. J. Proteomics 73, 1907-1920
    • (2010) J. Proteomics , vol.73 , pp. 1907-1920
    • Mathivanan, S.1    Ji, H.2    Simpson, R.J.3
  • 43
    • 7644224191 scopus 로고    scopus 로고
    • Extracellular proteases as targets for treatment of cancer metastases
    • DOI 10.1039/b209224g
    • Lee, M., Fridman, R., and Mobashery, S. (2004) Extracellular proteases as targets for treatment of cancer metastases. Chem. Soc. Rev. 33, 401-409 (Pubitemid 39456998)
    • (2004) Chemical Society Reviews , vol.33 , Issue.7 , pp. 401-409
    • Lee, M.1    Fridman, R.2    Mobashery, S.3
  • 44
    • 33344467274 scopus 로고    scopus 로고
    • KAI1/CD82 suppresses tumor invasion by MMP9 inactivation via TIMP1 up-regulation in the H1299 human lung carcinoma cell line
    • DOI 10.1016/j.bbrc.2006.01.153, PII S0006291X06002439
    • Jee, B. K., Park, K. M., Surendran, S., Lee, W. K., Han, C. W., Kim, Y. S., and Lim, Y. (2006) KAI1/CD82 suppresses tumor invasion by MMP9 inactivation via TIMP1 up-regulation in the H1299 human lung carcinoma cell line. Biochem. Biophys. Res. Commun. 342, 655-661 (Pubitemid 43289040)
    • (2006) Biochemical and Biophysical Research Communications , vol.342 , Issue.2 , pp. 655-661
    • Jee, B.K.1    Park, K.M.2    Surendran, S.3    Lee, W.K.4    Han, C.W.5    Kim, Y.S.6    Lim, Y.7
  • 45
    • 33646576169 scopus 로고    scopus 로고
    • Matrix metalloproteinases and tumor metastasis
    • DOI 10.1007/s10555-006-7886-9, Metalloproteinases and Cancer
    • Deryugina, E. I., and Quigley, J. P. (2006) Matrix metalloproteinases and tumor metastasis. Cancer Metastasis Rev. 25, 9-34 (Pubitemid 43723979)
    • (2006) Cancer and Metastasis Reviews , vol.25 , Issue.1 , pp. 9-34
    • Deryugina, E.I.1    Quigley, J.P.2
  • 47
    • 0038049137 scopus 로고    scopus 로고
    • Tumour-cell invasion and migration: Diversity and escape mechanisms
    • DOI 10.1038/nrc1075
    • Friedl, P., and Wolf, K. (2003) Tumour-cell invasion and migration: diversity and escape mechanisms. Nat. Rev. Cancer 3, 362-374 (Pubitemid 37328856)
    • (2003) Nature Reviews Cancer , vol.3 , Issue.5 , pp. 362-374
    • Friedl, P.1    Wolf, K.2
  • 48
    • 43149096710 scopus 로고    scopus 로고
    • Protein kinase Cepsilon mediates polymeric fibronectin assembly on the surface of blood-borne rat breast cancer cells to promote pulmonary metastasis
    • Huang, L., Cheng, H. C., Isom, R., Chen, C. S., Levine, R. A., and Pauli, B. U. (2008) Protein kinase Cepsilon mediates polymeric fibronectin assembly on the surface of blood-borne rat breast cancer cells to promote pulmonary metastasis. J. Biol. Chem. 283, 7616-7627
    • (2008) J. Biol. Chem. , vol.283 , pp. 7616-7627
    • Huang, L.1    Cheng, H.C.2    Isom, R.3    Chen, C.S.4    Levine, R.A.5    Pauli, B.U.6
  • 49
    • 38849168162 scopus 로고    scopus 로고
    • Oncogenic BRAF Induces Senescence and Apoptosis through Pathways Mediated by the Secreted Protein IGFBP7
    • DOI 10.1016/j.cell.2007.12.032, PII S0092867408000536
    • Wajapeyee, N., Serra, R. W., Zhu, X., Mahalingam, M., and Green, M. R. (2008) Oncogenic BRAF induces senescence and apoptosis through pathways mediated by the secreted protein IGFBP7. Cell 132, 363-374 (Pubitemid 351191995)
    • (2008) Cell , vol.132 , Issue.3 , pp. 363-374
    • Wajapeyee, N.1    Serra, R.W.2    Zhu, X.3    Mahalingam, M.4    Green, M.R.5
  • 50
    • 33846874575 scopus 로고    scopus 로고
    • The role of the IGF system in cancer growth and metastasis: Overview and recent insights
    • DOI 10.1210/er.2006-0001
    • Samani, A. A., Yakar, S., LeRoith, D., and Brodt, P. (2007) The role of the IGF system in cancer growth and metastasis: overview and recent insights. Endocr. Rev. 28, 20-47 (Pubitemid 46220849)
    • (2007) Endocrine Reviews , vol.28 , Issue.1 , pp. 20-47
    • Samani, A.A.1    Yakar, S.2    LeRoith, D.3    Brodt, P.4
  • 52
    • 33748273867 scopus 로고    scopus 로고
    • Genetic screen for signal peptides in Hydra reveals novel secreted proteins and evidence for non-classical protein secretion
    • DOI 10.1016/j.ejcb.2006.05.007, PII S0171933506000999, A special issue dedicated to Guenter Gerisch on the occasion of his 75th birthday
    • Böttger, A., Strasser, D., Alexandrova, O., Levin, A., Fischer, S., Lasi, M., Rudd, S., and David, C. N. (2006) Genetic screen for signal peptides in Hydra reveals novel secreted proteins and evidence for non-classical protein secretion. Eur. J. Cell Biol. 85, 1107-1117 (Pubitemid 44317606)
    • (2006) European Journal of Cell Biology , vol.85 , Issue.9-10 , pp. 1107-1117
    • Bottger, A.1    Strasser, D.2    Alexandrova, O.3    Levin, A.4    Fischer, S.5    Lasi, M.6    Rudd, S.7    David, C.N.8
  • 55
    • 0038701886 scopus 로고    scopus 로고
    • The mystery of nonclassical protein secretion. A current view on cargo proteins and potential export routes
    • Nickel, W. (2003) The mystery of nonclassical protein secretion. A current view on cargo proteins and potential export routes. Eur. J. Biochem. 270, 2109-2119
    • (2003) Eur. J. Biochem. , vol.270 , pp. 2109-2119
    • Nickel, W.1
  • 56
    • 68849129712 scopus 로고    scopus 로고
    • Membrane vesicles as conveyors of immune responses
    • Théry, C., Ostrowski, M., and Segura, E. (2009) Membrane vesicles as conveyors of immune responses. Nat. Rev. Immunol. 9, 581-593
    • (2009) Nat. Rev. Immunol. , vol.9 , pp. 581-593
    • Théry, C.1    Ostrowski, M.2    Segura, E.3
  • 57
    • 70350593773 scopus 로고    scopus 로고
    • Exosomes in tumour immunity
    • Clayton, A., and Mason, M. D. (2009) Exosomes in tumour immunity. Curr. Oncol. 16, 46-49
    • (2009) Curr. Oncol. , vol.16 , pp. 46-49
    • Clayton, A.1    Mason, M.D.2
  • 59
    • 77953142134 scopus 로고    scopus 로고
    • Hypoxic tumor cell modulates its microenvironment to enhance angiogenic and metastatic potential by secretion of proteins and exosomes
    • Park, J. E., Tan, H. S., Datta, A., Lai, R. C., Zhang, H., Meng, W., Lim, S. K., and Sze, S. K. (2010) Hypoxic tumor cell modulates its microenvironment to enhance angiogenic and metastatic potential by secretion of proteins and exosomes. Mol. Cell. Proteomics 9, 1085-1099
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 1085-1099
    • Park, J.E.1    Tan, H.S.2    Datta, A.3    Lai, R.C.4    Zhang, H.5    Meng, W.6    Lim, S.K.7    Sze, S.K.8
  • 60
    • 0036882395 scopus 로고    scopus 로고
    • Serpin structure, mechanism, and function
    • Gettins, P. G. (2002) Serpin structure, mechanism, and function. Chem. Rev. 102, 4751-4804
    • (2002) Chem. Rev. , vol.102 , pp. 4751-4804
    • Gettins, P.G.1
  • 62
    • 20744450475 scopus 로고    scopus 로고
    • Alpha1-antitrypsin deficiency
    • Stoller, J. K., and Aboussouan, L. S. (2005) Alpha1-antitrypsin deficiency. Lancet 365, 2225-2236
    • (2005) Lancet , vol.365 , pp. 2225-2236
    • Stoller, J.K.1    Aboussouan, L.S.2
  • 64
    • 0020362023 scopus 로고
    • 1-antitrypsin in primary cultures of rat hepatocytes. Characterization of differently glycosylated intracellular and extracellular forms
    • DOI 10.1111/j.1432-1033.1982.tb07054.x
    • Gross, V., Geiger, T., Tran-Thi, T. A., Gauthier, F., and Heinrich, P. C. (1982) Biosynthesis and secretion of alpha 1-antitrypsin in primary cultures of rat hepatocytes. Characterization of differently glycosylated intracellular and extracellular forms. Eur J Biochem. 129, 317-323 (Pubitemid 13153727)
    • (1982) European Journal of Biochemistry , vol.129 , Issue.2 , pp. 317-323
    • Gross, V.1    Geiger, T.2    Tran, T.T.A.3
  • 65
    • 0022529160 scopus 로고
    • 1-antitrypsin deficiency
    • Bolmer, S., and Kleinerman, J. (1986) Isolation and characterization of alpha 1-antitrypsin in PAS-positive hepatic granules from rats with experimental alpha 1-antitrypsin deficiency. Am J Pathol. 123, 377-389 (Pubitemid 16072538)
    • (1986) American Journal of Pathology , vol.123 , Issue.2 , pp. 377-389
    • Bolmer, S.1    Kleinerman, J.2
  • 66
    • 80051635385 scopus 로고    scopus 로고
    • Oxidation of Z α1-antitrypsin by cigarette smoke induces polymerization: A novel mechanism of early-onset emphysema
    • Alam, S., Li, Z., Janciauskiene, S., and Mahadeva, R. (2011) Oxidation of Z α1-antitrypsin by cigarette smoke induces polymerization: a novel mechanism of early-onset emphysema. Am. J. Respir. Cell Mol. Biol. 245, 261-269
    • (2011) Am. J. Respir. Cell Mol. Biol. , vol.245 , pp. 261-269
    • Alam, S.1    Li, Z.2    Janciauskiene, S.3    Mahadeva, R.4
  • 67
    • 14044279288 scopus 로고    scopus 로고
    • 1-antitrypsin polymerization: A fluorescence correlation spectroscopic study
    • DOI 10.1021/bi048662e
    • Purkayastha, P., Klemke, J. W., Lavender, S., Oyola, R., Cooperman, B. S., and Gai, F. (2005) Alpha 1-antitrypsin polymerization: a fluorescence correlation spectroscopic study. Biochemistry 44, 2642-2649 (Pubitemid 40279568)
    • (2005) Biochemistry , vol.44 , Issue.7 , pp. 2642-2649
    • Purkayastha, P.1    Klemke, J.W.2    Lavender, S.3    Oyola, R.4    Cooperman, B.S.5    Gai, F.6
  • 68
    • 77950179576 scopus 로고    scopus 로고
    • Genetic variants of alpha1-antitrypsin
    • Salahuddin, P. (2010) Genetic variants of alpha1-antitrypsin. Curr Protein Pept Sci. 11, 101-117
    • (2010) Curr Protein Pept Sci. , vol.11 , pp. 101-117
    • Salahuddin, P.1
  • 69
    • 62649174885 scopus 로고    scopus 로고
    • Crystallographic and cellular characterisation of two mechanisms stabilising the native fold of alpha1-antitrypsin: Implications for disease and drug design
    • Gooptu, B., Miranda, E., Nobeli, I., Mallya, M., Purkiss, A., Brown, S. C., Summers, C., Phillips, R. L., Lomas, D. A., and Barrett, T. E. (2009) Crystallographic and cellular characterisation of two mechanisms stabilising the native fold of alpha1-antitrypsin: implications for disease and drug design. J. Mol. Biol. 387, 857-868
    • (2009) J. Mol. Biol. , vol.387 , pp. 857-868
    • Gooptu, B.1    Miranda, E.2    Nobeli, I.3    Mallya, M.4    Purkiss, A.5    Brown, S.C.6    Summers, C.7    Phillips, R.L.8    Lomas, D.A.9    Barrett, T.E.10
  • 70
    • 54349093030 scopus 로고    scopus 로고
    • Alpha-1 antitrypsin (alpha1-AT) plasma levels in lung, prostate and breast cancer patients
    • El-Akawi, Z. J., Al-Hindawi, F. K., and Bashir, N. A. (2008) Alpha-1 antitrypsin (alpha1-AT) plasma levels in lung, prostate and breast cancer patients. Neuroendocrinol. Lett. 29, 482-484
    • (2008) Neuroendocrinol. Lett. , vol.29 , pp. 482-484
    • El-Akawi, Z.J.1    Al-Hindawi, F.K.2    Bashir, N.A.3
  • 71
    • 77749330082 scopus 로고    scopus 로고
    • The importance of alpha-1 antitrypsin (alpha1-AT) and neopterin serum levels in the evaluation of non-small cell lung and prostate cancer patients
    • El-Akawi, Z. J., Abu-Awad, A. M., Sharara, A. M., and Khader, Y. (2010) The importance of alpha-1 antitrypsin (alpha1-AT) and neopterin serum levels in the evaluation of non-small cell lung and prostate cancer patients. Neuroendocrinol. Lett. 31, 113-116
    • (2010) Neuroendocrinol. Lett. , vol.31 , pp. 113-116
    • El-Akawi, Z.J.1    Abu-Awad, A.M.2    Sharara, A.M.3    Khader, Y.4
  • 72
    • 77957887133 scopus 로고    scopus 로고
    • Linkage specific fucosylation of alpha-1-antitrypsin in liver cirrhosis and cancer patients: Implications for a biomarker of hepatocellular carcinoma
    • Comunale, M. A., Rodemich-Betesh, L., Hafner, J., Wang, M., Norton, P., Di Bisceglie, A. M., Block, T., and Mehta, A. (2010) Linkage specific fucosylation of alpha-1-antitrypsin in liver cirrhosis and cancer patients: implications for a biomarker of hepatocellular carcinoma. PLoS One. 5, e12419
    • (2010) PLoS One , vol.5
    • Comunale, M.A.1    Rodemich-Betesh, L.2    Hafner, J.3    Wang, M.4    Norton, P.5    Di Bisceglie, A.M.6    Block, T.7    Mehta, A.8
  • 73
    • 84869226410 scopus 로고    scopus 로고
    • Fibrolamellar hepatocellular carcinoma with alpha-one antitrypsin liver disease
    • Al Bugami, M. M., Farahat, K. L., Al-Ashgar, H. I., and Hainau, B. (2004) Fibrolamellar hepatocellular carcinoma with alpha-one antitrypsin liver disease. Saudi J. Gastroenterol. 10, 92-95
    • (2004) Saudi J. Gastroenterol. , vol.10 , pp. 92-95
    • Al Bugami, M.M.1    Farahat, K.L.2    Al-Ashgar, H.I.3    Hainau, B.4
  • 77
    • 34548182124 scopus 로고    scopus 로고
    • Identification of differentially secreted biomarkers using LC-MS/MS in isogenic cell lines representing a progression of breast cancer
    • DOI 10.1021/pr060629m
    • Mbeunkui, F., Metge, B. J., Shevde, L. A., and Pannell, L. K. (2007) Identification of differentially secreted biomarkers using LC-MS/MS in isogenic cell lines representing a progression of breast cancer. Proteome Res. 6, 2993-3002 (Pubitemid 47310184)
    • (2007) Journal of Proteome Research , vol.6 , Issue.8 , pp. 2993-3002
    • Mbeunkui, F.1    Metge, B.J.2    Shevde, L.A.3    Pannell, L.K.4
  • 78
    • 1442301638 scopus 로고    scopus 로고
    • Increased Plasma Levels of Serine Proteinase Inhibitors in Lung Cancer Patients
    • Zelvyte, I., Wallmark, A., Piitulainen, E., Westin, U., and Janciauskiene, S. (2004) Increased plasma levels of serine proteinase inhibitors in lung cancer patients. Anticancer Res. 24, 241-247 (Pubitemid 38279714)
    • (2004) Anticancer Research , vol.24 , Issue.1 , pp. 241-247
    • Zelvyte, I.1    Wallmark, A.2    Piitulainen, E.3    Westin, U.4    Janciauskiene, S.5
  • 79
    • 47749131186 scopus 로고    scopus 로고
    • TWIST activation by hypoxia inducible factor-1 (HIF-1): Implications in metastasis and development
    • Yang, M. H., and Wu, K. J. (2008) TWIST activation by hypoxia inducible factor-1 (HIF-1): implications in metastasis and development. Cell Cycle. 7, 2090-2096
    • (2008) Cell Cycle , vol.7 , pp. 2090-2096
    • Yang, M.H.1    Wu, K.J.2
  • 80
    • 39649102143 scopus 로고    scopus 로고
    • Epithelial-to-mesenchymal transition is important to metastasis, but questions remain
    • Garber K. (2008) Epithelial-to-mesenchymal transition is important to metastasis, but questions remain. J. Natl. Cancer Inst. 100, 232-239
    • (2008) J. Natl. Cancer Inst. , vol.100 , pp. 232-239
    • Garber, K.1
  • 81
    • 44449144396 scopus 로고    scopus 로고
    • Epithelial-Mesenchymal Transition: At the Crossroads of Development and Tumor Metastasis
    • DOI 10.1016/j.devcel.2008.05.009, PII S1534580708002098
    • Yang, J., and Weinberg, R.A. (2008) Epithelial-mesenchymal transition: at the crossroads of development and tumor metastasis. Dev Cell. 14, 818-829 (Pubitemid 351757205)
    • (2008) Developmental Cell , vol.14 , Issue.6 , pp. 818-829
    • Yang, J.1    Weinberg, R.A.2
  • 82
    • 47549106286 scopus 로고    scopus 로고
    • EMT and MET in carcinoma-clinical observations, regulatory pathways and new models
    • Thompson, E. W., and Williams, E. D. (2008) EMT and MET in carcinoma-clinical observations, regulatory pathways and new models. Clin. Exp. Metastasis 25, 591-592
    • (2008) Clin. Exp. Metastasis , vol.25 , pp. 591-592
    • Thompson, E.W.1    Williams, E.D.2
  • 83
    • 53349177489 scopus 로고    scopus 로고
    • Biomarkers for the lung cancer diagnosis and their advances in proteomics
    • Sung, H. J., and Cho, J. Y. (2008) Biomarkers for the lung cancer diagnosis and their advances in proteomics. BMB Rep. 41, 615-625
    • (2008) BMB Rep. , vol.41 , pp. 615-625
    • Sung, H.J.1    Cho, J.Y.2
  • 84
    • 70350514636 scopus 로고    scopus 로고
    • NFAT proteins: Emerging roles in cancer progression
    • Mancini, M., and Toker, A. (2009) NFAT proteins: emerging roles in cancer progression. Nat. Rev. Cancer 9, 810-820
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 810-820
    • Mancini, M.1    Toker, A.2
  • 85
    • 0036512208 scopus 로고    scopus 로고
    • New functions for the matrix metalloproteinases in cancer progression
    • Egeblad, M., and Werb, Z. (2002) New functions for the matrix metalloproteinases in cancer progression. Nat. Rev. Cancer 2, 161-174 (Pubitemid 37328786)
    • (2002) Nature Reviews Cancer , vol.2 , Issue.3 , pp. 161-174
    • Egeblad, M.1    Werb, Z.2
  • 86
    • 33645845151 scopus 로고    scopus 로고
    • Protein kinase C (PKC) family in cancer progression
    • Koivunen, J., Aaltonen, V., and Peltonen, J. (2006) Protein kinase C (PKC) family in cancer progression. Cancer Lett. 235, 1-10
    • (2006) Cancer Lett. , vol.235 , pp. 1-10
    • Koivunen, J.1    Aaltonen, V.2    Peltonen, J.3
  • 87
    • 63049090100 scopus 로고    scopus 로고
    • Metastasis: From dissemination to organ-specific colonization
    • Nguyen, D. X., Bos, P. D., and Massagué, J. (2009) Metastasis: from dissemination to organ-specific colonization. Nat. Rev. Cancer 9, 274-284
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 274-284
    • Nguyen, D.X.1    Bos, P.D.2    Massagué, J.3
  • 88
    • 33746605711 scopus 로고    scopus 로고
    • Lymphatic or hematogenous dissemination: How does a metastatic tumor cell decide?
    • Wong, S. Y., and Hynes, R. O. (2006) Lymphatic or hematogenous dissemination: how does a metastatic tumor cell decide? Cell Cycle 5, 812-817 (Pubitemid 44149486)
    • (2006) Cell Cycle , vol.5 , Issue.8 , pp. 812-817
    • Wong, S.Y.1    Hynes, R.O.2
  • 89
    • 0036674501 scopus 로고    scopus 로고
    • Dissemination and growth of cancer cells in metastatic sites
    • DOI 10.1038/nrc865
    • Chambers, A. F., Groom, A. C., and MacDonald, I. C. (2002) Dissemination and growth of cancer cells in metastatic sites. Nature Rev. Cancer 2, 563-572 (Pubitemid 37328923)
    • (2002) Nature Reviews Cancer , vol.2 , Issue.8 , pp. 563-572
    • Chambers, A.F.1    Groom, A.C.2    MacDonald, I.C.3
  • 90
    • 0032695271 scopus 로고    scopus 로고
    • Small bowel metastases in non-small cell lung cancer
    • DOI 10.1016/S0169-5002(99)00075-6, PII S0169500299000756
    • Stenbygaard, L. E., and Sørensen, J. B. (1999) Small bowel metastases in non-small cell lung cancer. Lung Cancer 26, 95-101 (Pubitemid 29492897)
    • (1999) Lung Cancer , vol.26 , Issue.2 , pp. 95-101
    • Stenbygaard, L.E.1    Sorensen, J.B.2
  • 91
    • 29844458158 scopus 로고    scopus 로고
    • Expression of chymase-positive cells in gastric cancer and its correlation with the angiogenesis
    • DOI 10.1002/jso.20394
    • Kondo, K., Muramatsu, M., Okamoto, Y., Jin, D., Takai, S., Tanigawa, N., and Miyazaki, M. (2006) Expression of chymase-positive cells in gastric cancer and its correlation with the angiogenesis. J. Surg. Oncol. 93, 36-42 (Pubitemid 43038424)
    • (2006) Journal of Surgical Oncology , vol.93 , Issue.1 , pp. 36-42
    • Kondo, K.1    Muramatsu, M.2    Okamoto, Y.3    Jin, D.4    Takai, S.5    Tanigawa, N.6    Miyazaki, M.7
  • 92
    • 0042819735 scopus 로고    scopus 로고
    • Modulation of enzymatic activity of human mast cell tryptase and chymase by protease inhibitors
    • He, S. H., Chen, P., and Chen, H. Q. (2003) Modulation of enzymatic activity of human mast cell tryptase and chymase by protease inhibitors. Acta Pharmacol. Sin. 24, 923-929
    • (2003) Acta Pharmacol. Sin. , vol.24 , pp. 923-929
    • He, S.H.1    Chen, P.2    Chen, H.Q.3
  • 93
    • 0035865351 scopus 로고    scopus 로고
    • Mast cell tissue inhibitor of metalloproteinase-1 is cleaved and inactivated extracellularly by alpha-chymase
    • Frank, B. T., Rossall, J. C., Caughey, G. H., and Fang, K. C. (2001) Mast cell tissue inhibitor of metalloproteinase-1 is cleaved and inactivated extracellularly by agr-chymase. J. Immunol. 166, 2783-2792 (Pubitemid 32173519)
    • (2001) Journal of Immunology , vol.166 , Issue.4 , pp. 2783-2792
    • Frank, B.T.1    Rossall, J.C.2    Caughey, G.H.3    Fang, K.C.4
  • 94
    • 15744388309 scopus 로고    scopus 로고
    • A key role for mast cell chymase in the activation of pro-matrix metalloprotease-9 and pro-matrix metalloprotease-2
    • DOI 10.1074/jbc.M410396200
    • Tchougounova, E., Lundequist, A., Fajardo, I., Winberg, J. O., Abrink, M., and Pejler, G. (2005) A key role for mast cell chymase in the activation of pro-matrix metalloprotease-9 and pro-matrix metalloprotease-2. J. Biol. Chem. 280, 9291-9296 (Pubitemid 40409621)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.10 , pp. 9291-9296
    • Tchougounova, E.1    Lundequist, A.2    Fajardo, I.3    Winberg, J.-O.4    Abrink, M.5    Pejler, G.6
  • 96
    • 0039410419 scopus 로고
    • Metastasis: A review of recent advances
    • Zeidman, I. (1957) Metastasis: a review of recent advances. Cancer Res. 17, 157-162
    • (1957) Cancer Res. , vol.17 , pp. 157-162
    • Zeidman, I.1
  • 97
    • 0019408002 scopus 로고
    • Influence of microenvironment and vascular anatomy on 'metastatic' colonization potential of mammary tumors
    • Tarin, D., and Price, J. E. (1981) Influence of microenvironment and vascular anatomy on "metastatic" colonization potential of mammary tumors. Cancer Res. 41, 3604-3609 (Pubitemid 11063644)
    • (1981) Cancer Research , vol.41 , Issue.9 I , pp. 3604-3609
    • Tarin, D.1    Price, J.E.2
  • 98
    • 70350437711 scopus 로고    scopus 로고
    • Epitope analysis of the rat dipeptidyl peptidase IV monoclonal antibody 6A3 that blocks pericellular fibronectin-mediated cancer cell adhesion
    • Hung, T. T., Wu, J. Y., Liu, J. F., and Cheng, H. C. (2009) Epitope analysis of the rat dipeptidyl peptidase IV monoclonal antibody 6A3 that blocks pericellular fibronectin-mediated cancer cell adhesion. FEBS J. 276, 6548-6559
    • (2009) FEBS J. , vol.276 , pp. 6548-6559
    • Hung, T.T.1    Wu, J.Y.2    Liu, J.F.3    Cheng, H.C.4
  • 100
    • 0021926873 scopus 로고
    • Interaction of the 70,000-mol-wt amino-terminal fragment of fibronectin with the matrix-assembly receptor of fibroblasts
    • McKeown-Longo, P. J., and Mosher, D. F. (1985) Interaction of the 70,000-mol-wt amino-terminal fragment of fibronectin with the matrix-assembly receptor of fibroblasts. J. Cell Biol. 100, 364-374
    • (1985) J. Cell Biol. , vol.100 , pp. 364-374
    • McKeown-Longo, P.J.1    Mosher, D.F.2
  • 101
    • 0032476055 scopus 로고    scopus 로고
    • Control of cell cycle progression by fibronectin matrix architecture
    • DOI 10.1074/jbc.273.40.25533
    • Sechler, J. L., and Schwarzbauer, J. E. (1998) Control of cell cycle progression by fibronectin matrix architecture. J. Biol. Chem. 273, 25533-25536 (Pubitemid 28475767)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.40 , pp. 25533-25536
    • Sechler, J.L.1    Schwarzbauer, J.E.2
  • 102
    • 58149473116 scopus 로고    scopus 로고
    • Display of cell surface sites for fibronectin assembly is modulated by cell adherence to (1)F3 and C-terminal modules of fibronectin
    • Xu, J., Bae, E., Zhang, Q., Annis, D. S., Erickson, H. P., and Mosher, D. F. (2009) Display of cell surface sites for fibronectin assembly is modulated by cell adherence to (1)F3 and C-terminal modules of fibronectin. PLoS One. 4, e4113
    • (2009) PLoS One , vol.4
    • Xu, J.1    Bae, E.2    Zhang, Q.3    Annis, D.S.4    Erickson, H.P.5    Mosher, D.F.6
  • 104
    • 77952958193 scopus 로고    scopus 로고
    • Protein kinase Cvarepsilon mediates Stat3Ser727 phosphorylation, Stat3-regulated gene expression, and cell invasion in various human cancer cell lines through integration with MAPK cascade (RAF-1, MEK1/2, and ERK1/2)
    • Aziz, M. H., Hafeez, B. B., Sand, J. M., Pierce, D. B., Aziz, S. W., Dreckschmidt, N. E., and Verma, A. K. (2010) Protein kinase Cvarepsilon mediates Stat3Ser727 phosphorylation, Stat3-regulated gene expression, and cell invasion in various human cancer cell lines through integration with MAPK cascade (RAF-1, MEK1/2, and ERK1/2). Oncogene 29, 3100-3109
    • (2010) Oncogene , vol.29 , pp. 3100-3109
    • Aziz, M.H.1    Hafeez, B.B.2    Sand, J.M.3    Pierce, D.B.4    Aziz, S.W.5    Dreckschmidt, N.E.6    Verma, A.K.7
  • 105
    • 0037101781 scopus 로고    scopus 로고
    • 1-antitrypsin (AAT) gene expression in Hep G2 cells is mediated by a 3′ enhancer
    • DOI 10.1042/BJ20011312
    • Morgan, K., Marsters, P., Morley, S., van Gent, D., Hejazi, A., Backx, M., Thorpe, E. R., and Kalsheker, N. (2002) Oncostatin M induced alpha1-antitrypsin (AAT) gene expression in Hep G2 cells is mediated by a 3′enhancer. Biochem. J. 365, 555-560 (Pubitemid 36135328)
    • (2002) Biochemical Journal , vol.365 , Issue.2 , pp. 555-560
    • Morgan, K.1    Marsters, P.2    Morley, S.3    Van Gent, D.4    Hejazi, A.5    Backx, M.6    Thorpe, E.R.K.7    Kalsheker, N.8
  • 106
    • 0042819735 scopus 로고    scopus 로고
    • Modulation of enzymatic activity of human mast cell tryptase and chymase by protease inhibitors
    • He, S. H., Chen, P., and Chen, H. Q. (2003) Modulation of enzymatic activity of human mast cell tryptase and chymase by protease inhibitors. Acta Pharmacol. Sin. 24, 923-929
    • (2003) Acta Pharmacol. Sin. , vol.24 , pp. 923-929
    • He, S.H.1    Chen, P.2    Chen, H.Q.3


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