메뉴 건너뛰기




Volumn 190, Issue 3, 1999, Pages 311-322

A role for dipeptidyl peptidase IV in suppressing the malignant phenotype of melanocytic cells

Author keywords

Differentiation; Fibroblast activating protein ; Melanoma; Serine protease; Tumorigenicity

Indexed keywords

ALANINE; DIPEPTIDYL PEPTIDASE IV; SERINE; SERINE PROTEINASE;

EID: 0033517124     PISSN: 00221007     EISSN: None     Source Type: Journal    
DOI: 10.1084/jem.190.3.311     Document Type: Article
Times cited : (169)

References (38)
  • 1
    • 0017650796 scopus 로고
    • Purification and subunit structure of adenosine deaminase from human kidney
    • Schrader, W.P., and A.R. Stacy. 1977. Purification and subunit structure of adenosine deaminase from human kidney. J. Biol. Chem. 252:6409-6415.
    • (1977) J. Biol. Chem. , vol.252 , pp. 6409-6415
    • Schrader, W.P.1    Stacy, A.R.2
  • 2
    • 0023926392 scopus 로고
    • Cell surface antigens of human melanocytes and melanoma. Expression of adenosine deaminase binding protein is extinguished with melanocyte transformation
    • Houghton, A.N., A. Albino, C. Cordon-Cardo, L.J. Davis, and M. Eisinger. 1988. Cell surface antigens of human melanocytes and melanoma. Expression of adenosine deaminase binding protein is extinguished with melanocyte transformation. J. Exp. Med. 167:197-212.
    • (1988) J. Exp. Med. , vol.167 , pp. 197-212
    • Houghton, A.N.1    Albino, A.2    Cordon-Cardo, C.3    Davis, L.J.4    Eisinger, M.5
  • 3
    • 0031908130 scopus 로고    scopus 로고
    • The structure and function of CD26 in the T-cell immune response
    • Morimoto, C., and S. Schlossman. 1998. The structure and function of CD26 in the T-cell immune response. Immunol. Rev. 61:55-70.
    • (1998) Immunol. Rev. , vol.61 , pp. 55-70
    • Morimoto, C.1    Schlossman, S.2
  • 4
    • 0025093094 scopus 로고
    • Characterization of the adenosine deaminase-adenosine deaminase complexing protein binding reaction
    • Schrader, W.P., C.A. West, A.D. Miczek, and E.K. Norton. 1990. Characterization of the adenosine deaminase-adenosine deaminase complexing protein binding reaction. J. Biol. Chem. 265:19312-19318.
    • (1990) J. Biol. Chem. , vol.265 , pp. 19312-19318
    • Schrader, W.P.1    West, C.A.2    Miczek, A.D.3    Norton, E.K.4
  • 5
    • 0018084442 scopus 로고
    • Localization of an adenosine deaminase-binding protein in human kidney
    • Schrader, W.P., and B. Pollara. 1978. Localization of an adenosine deaminase-binding protein in human kidney. J. Lab. Clin. Med. 92:656-662.
    • (1978) J. Lab. Clin. Med. , vol.92 , pp. 656-662
    • Schrader, W.P.1    Pollara, B.2
  • 7
    • 0020611223 scopus 로고
    • Adenosine deaminase complexing protein: A transformation sensitive protein with potentials of a cancer marker
    • Herbschleb-Voogt, E., J. Ten Kate, and P. Meera Khan. 1983. Adenosine deaminase complexing protein: a transformation sensitive protein with potentials of a cancer marker. Anticancer Res. 3:95-100.
    • (1983) Anticancer Res. , vol.3 , pp. 95-100
    • Herbschleb-Voogt, E.1    Kate J. X2    Meera Khan, P.3
  • 9
    • 0030782738 scopus 로고    scopus 로고
    • Expression and localization of aminopeptidase A, aminopeptidase N, and dipeptidyl peptidase IV in benign and malignant human prostate tissue
    • Bogenrieder, T., C.L. Finstad, R.H. Freeman, C.N. Papandreou, H.I. Scher, A.P. Albino, V.E. Reuter, and D.M. Nanus. 1997. Expression and localization of aminopeptidase A, aminopeptidase N, and dipeptidyl peptidase IV in benign and malignant human prostate tissue. Prostate. 33:225-232.
    • (1997) Prostate , vol.33 , pp. 225-232
    • Bogenrieder, T.1    Finstad, C.L.2    Freeman, R.H.3    Papandreou, C.N.4    Scher, H.I.5    Albino, A.P.6    Reuter, V.E.7    Nanus, D.M.8
  • 11
    • 0022570216 scopus 로고
    • Adenosine deaminase complexing protein (ADCP) immunoreactivity in colorectal adenocarcinoma
    • Ten Kate, J., H.F. van den Ingh, P.M. Khan, and F.T. Bosman. 1986. Adenosine deaminase complexing protein (ADCP) immunoreactivity in colorectal adenocarcinoma. Int. J. Cancer. 37:479-485.
    • (1986) Int. J. Cancer. , vol.37 , pp. 479-485
    • Kate J. X1    Van Den Ingh, H.F.2    Khan, P.M.3    Bosman, F.T.4
  • 12
    • 0027523145 scopus 로고
    • Distribution of adenosine deaminase binding protein in normal and malignant tissues of the gastrointestinal tract studied by monoclonal antibodies
    • Sakamoto, J., T. Watanabe, S. Teramukai, S. Akiyama, T. Morimoto, H. Takagi, H. Nakazato, R. Ueda, and T. Takahashi. 1993. Distribution of adenosine deaminase binding protein in normal and malignant tissues of the gastrointestinal tract studied by monoclonal antibodies. J. Surg. Oncol. 52: 124-143.
    • (1993) J. Surg. Oncol. , vol.52 , pp. 124-143
    • Sakamoto, J.1    Watanabe, T.2    Teramukai, S.3    Akiyama, S.4    Morimoto, T.5    Takagi, H.6    Nakazato, H.7    Ueda, R.8    Takahashi, T.9
  • 13
    • 0027401263 scopus 로고
    • A marker for neoplastic progression of human melanocytes is a cell surface ectopeptidase
    • Morrison, M.E., S. Vijayasaradhi, D. Engelstein, A.P. Albino, and A.N. Houghton. 1993. A marker for neoplastic progression of human melanocytes is a cell surface ectopeptidase. J. Exp. Med. 177:1135-1143.
    • (1993) J. Exp. Med. , vol.177 , pp. 1135-1143
    • Morrison, M.E.1    Vijayasaradhi, S.2    Engelstein, D.3    Albino, A.P.4    Houghton, A.N.5
  • 14
    • 0026487199 scopus 로고
    • Malignant transformation of human melanocytes: Induction of a complete melanoma phenotype and genotype
    • Albino, A.P., Z. Sozi, D.M. Nanus, C.S. Jhanwar, and A.N. Houghton. 1992. Malignant transformation of human melanocytes: induction of a complete melanoma phenotype and genotype. Oncogene. 7:2315-2321.
    • (1992) Oncogene , vol.7 , pp. 2315-2321
    • Albino, A.P.1    Sozi, Z.2    Nanus, D.M.3    Jhanwar, C.S.4    Houghton, A.N.5
  • 15
    • 0027302568 scopus 로고
    • Regulation and heteromeric structure of the fibroblast activation protein in normal and transformed cells of mesenchymal and neuroectodermal origin
    • Rettig, W.J., P. Garin-Chesa, J.H. Healey, S.L Su, H.L. Ozer, M. Schwab, A.P. Albino, and L.J. Old. 1993. Regulation and heteromeric structure of the fibroblast activation protein in normal and transformed cells of mesenchymal and neuroectodermal origin. Cancer Res. 53:3327-3335.
    • (1993) Cancer Res. , vol.53 , pp. 3327-3335
    • Rettig, W.J.1    Garin-Chesa, P.2    Healey, J.H.3    Su, S.L.4    Ozer, H.L.5    Schwab, M.6    Albino, A.P.7    Old, L.J.8
  • 16
  • 17
    • 0020443979 scopus 로고
    • Surface antigens of melanocytes and melanomas: Markers of melanocyte differentiation and melanoma subsets
    • Houghton, A.N., M. Eisinger, A.P. Albino, J.G. Cairncross, and L.J. Old. 1982. Surface antigens of melanocytes and melanomas: markers of melanocyte differentiation and melanoma subsets. J. Exp. Med. 156:1755-1766.
    • (1982) J. Exp. Med. , vol.156 , pp. 1755-1766
    • Houghton, A.N.1    Eisinger, M.2    Albino, A.P.3    Cairncross, J.G.4    Old, L.J.5
  • 18
    • 0023243241 scopus 로고
    • Phenotypic heterogeneity of melanoma. Relation to the differentiation program of melanoma cells
    • Houghton, A.N., F.X. Real, L.J. Davis, C. Cordon-Cardo, and L.J. Old. 1987. Phenotypic heterogeneity of melanoma. Relation to the differentiation program of melanoma cells. J. Exp. Med. 164:812-829.
    • (1987) J. Exp. Med. , vol.164 , pp. 812-829
    • Houghton, A.N.1    Real, F.X.2    Davis, L.J.3    Cordon-Cardo, C.4    Old, L.J.5
  • 19
    • 0001418906 scopus 로고
    • Selective proliferation of normal human melanocytes in vitro in the presence of phorbol ester and cholera toxin
    • Eisinger, M., and O. Marko. 1982. Selective proliferation of normal human melanocytes in vitro in the presence of phorbol ester and cholera toxin. Proc. Natl. Acad. Sci. USA. 79: 2018-2022.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 2018-2022
    • Eisinger, M.1    Marko, O.2
  • 20
    • 0025083528 scopus 로고
    • Cell surface glycoprotein of reactive stromal fibroblasts as a potential antibody target in human epithelial cancers
    • Garin-Chesa, P., L.J. Old, and W.J. Rettig. 1990. Cell surface glycoprotein of reactive stromal fibroblasts as a potential antibody target in human epithelial cancers. Proc. Natl. Acad. Sci. USA. 87:7235-7239.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 7235-7239
    • Garin-Chesa, P.1    Old, L.J.2    Rettig, W.J.3
  • 21
    • 0031944640 scopus 로고    scopus 로고
    • The cytoplasmic tail of the mouse brown locus product determines intracellular stability and export from the endoplasmic reticulum
    • Xu, Y., S. Vijayasaradhi, and A.N. Houghton. 1998. The cytoplasmic tail of the mouse brown locus product determines intracellular stability and export from the endoplasmic reticulum. J. Invest. Dermatol. 110:324-331.
    • (1998) J. Invest. Dermatol. , vol.110 , pp. 324-331
    • Xu, Y.1    Vijayasaradhi, S.2    Houghton, A.N.3
  • 22
    • 0018836136 scopus 로고
    • Rapid chromatographic purification of dipeptidyl peptidase IV in human submaxillary gland
    • Kojima, K., T. Hama, T. Kato, and T. Nagatsu. 1980. Rapid chromatographic purification of dipeptidyl peptidase IV in human submaxillary gland. J. Chromatogr. 189:233-240.
    • (1980) J. Chromatogr. , vol.189 , pp. 233-240
    • Kojima, K.1    Hama, T.2    Kato, T.3    Nagatsu, T.4
  • 23
    • 0023929513 scopus 로고
    • Differentiation antigens of melanocytes and melanoma: Analysis of melanosome and cell surface markers of human pigmented cells with monoclonal antibodies
    • Thomson, T.M., F.X. Real, S. Murakami, C. Cordon-Cardo, L.J. Old, and A.N. Houghton. 1988. Differentiation antigens of melanocytes and melanoma: analysis of melanosome and cell surface markers of human pigmented cells with monoclonal antibodies. J. Invest. Dermatol. 4:459-466.
    • (1988) J. Invest. Dermatol. , vol.4 , pp. 459-466
    • Thomson, T.M.1    Real, F.X.2    Murakami, S.3    Cordon-Cardo, C.4    Old, L.J.5    Houghton, A.N.6
  • 24
    • 0019320348 scopus 로고
    • Autocrine secretion and malignant transformation of cells
    • Sporn, M.B., and G.J. Todaro. 1980. Autocrine secretion and malignant transformation of cells. N. Engl. J. Med. 303: 878-880.
    • (1980) N. Engl. J. Med. , vol.303 , pp. 878-880
    • Sporn, M.B.1    Todaro, G.J.2
  • 25
    • 0023500107 scopus 로고
    • Metastatic but not primary melanoma cell lines grow in vitro independently of exogenous growth factors
    • Rodeck, U., M. Herlyn, H.D. Menssen, R.W. Furlanetto, and H. Koprowski. 1987. Metastatic but not primary melanoma cell lines grow in vitro independently of exogenous growth factors. Int. J. Cancer. 40:687-690.
    • (1987) Int. J. Cancer , vol.40 , pp. 687-690
    • Rodeck, U.1    Herlyn, M.2    Menssen, H.D.3    Furlanetto, R.W.4    Koprowski, H.5
  • 26
    • 0023829808 scopus 로고
    • Surface antigens of human melanoma cells cultured in serum free medium: Induction of expression of major histocompatibility complex class II antigen
    • Real, F.X., B. Fliegel, and A.N. Houghton. 1988. Surface antigens of human melanoma cells cultured in serum free medium: induction of expression of major histocompatibility complex class II antigen. Cancer Res. 48:686-693.
    • (1988) Cancer Res. , vol.48 , pp. 686-693
    • Real, F.X.1    Fliegel, B.2    Houghton, A.N.3
  • 27
    • 0030715322 scopus 로고    scopus 로고
    • ECM and cell surface proteolysis: Regulating cellular ecology
    • Werb, Z. 1997. ECM and cell surface proteolysis: regulating cellular ecology. Cell. 191:439-442.
    • (1997) Cell , vol.191 , pp. 439-442
    • Werb, Z.1
  • 30
    • 0028905806 scopus 로고
    • bcl-2 protein expression in melanocytic neoplasms of the skin
    • Ramsay, J.A., L. From, and H.J. Kahn. 1995. bcl-2 protein expression in melanocytic neoplasms of the skin. Mod. Pathol. 8:150-154.
    • (1995) Mod. Pathol. , vol.8 , pp. 150-154
    • Ramsay, J.A.1    From, L.2    Kahn, H.J.3
  • 32
    • 0030819309 scopus 로고    scopus 로고
    • Regulation of the receptor specificity and function of the chemokine RANTES (regulated on activation, normal T cell expressed and secreted) by dipeptidyl peptidase IV (CD26)-mediated cleavage
    • Oravecz, T., M. Pall, G. Roderiquez, M.D. Gorrell, M. Ditto, N.Y. Nguyen, R. Boykins, E. Unsworth, and M.A. Norcross. 1997. Regulation of the receptor specificity and function of the chemokine RANTES (regulated on activation, normal T cell expressed and secreted) by dipeptidyl peptidase IV (CD26)-mediated cleavage J. Exp. Med. 186:1865-1872.
    • (1997) J. Exp. Med. , vol.186 , pp. 1865-1872
    • Oravecz, T.1    Pall, M.2    Roderiquez, G.3    Gorrell, M.D.4    Ditto, M.5    Nguyen, N.Y.6    Boykins, R.7    Unsworth, E.8    Norcross, M.A.9
  • 33
    • 0032497366 scopus 로고    scopus 로고
    • Functional comparison of two human monocyte chemotactic protein-2 isoforms. Role of the aminoterminal pyroglutamic acid and processing by CD26/dipeptidyl peptidase IV
    • Van Coillie, E., P. Proost, I. Van Aelst, S. Struyf, M. Polfliet, I. De Meester, D.J. Harvey, J. Van Damme, and G. Opdenakker. 1998. Functional comparison of two human monocyte chemotactic protein-2 isoforms. Role of the aminoterminal pyroglutamic acid and processing by CD26/dipeptidyl peptidase IV. Biochemistry. 37:12672-12680.
    • (1998) Biochemistry , vol.37 , pp. 12672-12680
    • Van Coillie, E.1    Proost, P.2    Van Aelst, I.3    Struyf, S.4    Polfliet, M.5    De Meester, I.6    Harvey, D.J.7    Van Damme, J.8    Opdenakker, G.9
  • 34
    • 0032571360 scopus 로고    scopus 로고
    • Amino-terminal truncation of chemokines by CD26/dipeptidyl-peptidase IV. Conversion of RANTES into a potent inhibitor of monocyte chemotaxis and HIV-1-infection
    • Proost, P., I. De Meester, D. Schols, S. Struyf, A.M. Lambeir, A. Wuyts, G. Opdenakker, E. De Clercq, S. Scharpe, and J. Van Damme. 1998. Amino-terminal truncation of chemokines by CD26/dipeptidyl-peptidase IV. Conversion of RANTES into a potent inhibitor of monocyte chemotaxis and HIV-1-infection. J. Biol. Chem. 273:7222-7227.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7222-7227
    • Proost, P.1    De Meester, I.2    Schols, D.3    Struyf, S.4    Lambeir, A.M.5    Wuyts, A.6    Opdenakker, G.7    De Clercq, E.8    Scharpe, S.9    Van Damme, J.10
  • 35
  • 36
    • 13144283654 scopus 로고    scopus 로고
    • Anti-HIV-1 and chemotactic activities of human stromal cell-derived factor 1α (SDF-1α) and SDF-1β are abolished by CD26/dipeptidyl peptidase IV-mediated cleavage
    • Shioda, T., H. Kato, Y. Ohnishi, K. Tashiro, M. Ikegawa, E.E. Nakayama, H. Hu, A. Kato, Y. Sakai, H. Liu, et al. 1998. Anti-HIV-1 and chemotactic activities of human stromal cell-derived factor 1α (SDF-1α) and SDF-1β are abolished by CD26/dipeptidyl peptidase IV-mediated cleavage. Proc. Natl. Acad. Sci. USA. 95:6331-6336.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6331-6336
    • Shioda, T.1    Kato, H.2    Ohnishi, Y.3    Tashiro, K.4    Ikegawa, M.5    Nakayama, E.E.6    Hu, H.7    Kato, A.8    Sakai, Y.9    Liu, H.10
  • 38
    • 0027965353 scopus 로고
    • Post-secretory processing of regulatory peptides: The pancreatic polypeptide family as a model example
    • Medeiros, M.S., and A.J. Turner. 1994. Post-secretory processing of regulatory peptides: the pancreatic polypeptide family as a model example. Biochimie. 76:283-287.
    • (1994) Biochimie. , vol.76 , pp. 283-287
    • Medeiros, M.S.1    Turner, A.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.