A marker for neoplastic progression of human melanocytes is a cell surface ectopeptidase

doi:10.1084/jem.177.4.1135

This Article

	Full Text (PDF, 1021K)
	Alert me when this article is cited
	Citation Map

Services

	Email this article
	Similar articles in this journal
	Similar articles in PubMed
	Alert me to new content in the JEM
	Download to citation manager

Citing Articles

	Citing Articles via HighWire
	Citing Articles via CrossRef
	Citing Articles via Google Scholar

Google Scholar

	Articles by Morrison, M. E.
	Articles by Houghton, A. N.
	Search for Related Content

PubMed

	PubMed Citation
	Articles by Morrison, M. E.
	Articles by Houghton, A. N.


Social Bookmarking

	What's this?

ARTICLES

A marker for neoplastic progression of human melanocytes is a cell surface ectopeptidase

ME Morrison, S Vijayasaradhi, D Engelstein, AP Albino and AN Houghton
Memorial Sloan-Kettering Cancer Center, New York, New York 10021.

Adenosine deaminase binding protein (ADAbp) is a cell surface glycoprotein that is expressed by normal melanocytes but not by melanoma, the malignant counterpart. ADAbp is specifically downregulated during malignant transformation of melanocytes. Recently, we have developed a system that progressively transforms melanocytes in vitro in defined steps. Transduction with v-Ha-ras oncogene followed by long-term culture leads to a cell phenotype and genotype that specifically mimics human melanoma. Loss of ADAbp expression occurred concomitantly with the emergence of growth factor independence and appearance of specific chromosomal abnormalities. The cellular function of ADAbp has not been defined. To characterize ADAbp, the mature 110-kD form was purified from human kidney. Five tryptic peptides from purified human ADAbp revealed 100% homology to a serine protease, human dipeptidyl peptidase IV (DPP IV), also known as CD26. DPP IV activity was detected in lysates from human melanocytes and renal carcinoma cells but not melanoma cells, and DPP IV activity could be specifically isolated from melanocytes by binding to ADA or to S27 monoclonal antibody against ADAbp. These findings show that ADAbp is a cell surface ectopeptidase that is tightly regulated during neoplastic transformation of melanocytes.
Add to CiteULike CiteULike Add to Complore Complore Add to Connotea Connotea Add to Del.icio.us Del.icio.us Add to Digg Digg Add to Reddit Reddit Add to Technorati Technorati What's this?

This article has been cited by other articles:

Tan, E. Y., Richard, C. L., Zhang, H., Hoskin, D. W., Blay, J. (2006). Adenosine downregulates DPPIV on HT-29 colon cancer cells by stimulating protein tyrosine phosphatase(s) and reducing ERK1/2 activity via a novel pathway. Am. J. Physiol. Cell Physiol. 291: C433-C444 [Abstract] [Full Text]
Yamochi, T., Yamochi, T., Aytac, U., Sato, T., Sato, K., Ohnuma, K., McKee, K. S., Morimoto, C., Dang, N. H. (2005). Regulation of p38 Phosphorylation and Topoisomerase II{alpha} Expression in the B-Cell Lymphoma Line Jiyoye by CD26/Dipeptidyl Peptidase IV Is Associated with Enhanced In vitro and In vivo Sensitivity to Doxorubicin. Cancer Res. 65: 1973-1983 [Abstract] [Full Text]
Girardi, A. C. C., Knauf, F., Demuth, H.-U., Aronson, P. S. (2004). Role of dipeptidyl peptidase IV in regulating activity of Na+/H+ exchanger isoform NHE3 in proximal tubule cells. Am. J. Physiol. Cell Physiol. 287: C1238-C1245 [Abstract] [Full Text]
Tan, E. Y., Mujoomdar, M., Blay, J. (2004). Adenosine Down-Regulates the Surface Expression of Dipeptidyl Peptidase IV on HT-29 Human Colorectal Carcinoma Cells: Implications for Cancer Cell Behavior. Am. J. Pathol. 165: 319-330 [Abstract] [Full Text]
Gonzalez-Gronow, M., Hershfield, M. S., Arredondo-Vega, F. X., Pizzo, S. V. (2004). Cell Surface Adenosine Deaminase Binds and Stimulates Plasminogen Activation on 1-LN Human Prostate Cancer Cells. J. Biol. Chem. 279: 20993-20998 [Abstract] [Full Text]
Richard, E., Alam, S. M., Arredondo-Vega, F. X., Patel, D. D., Hershfield, M. S. (2002). Clustered Charged Amino Acids of Human Adenosine Deaminase Comprise a Functional Epitope for Binding the Adenosine Deaminase Complexing Protein CD26/Dipeptidyl Peptidase IV. J. Biol. Chem. 277: 19720-19726 [Abstract] [Full Text]
Cordero, O. J., Salgado, F. J., Fernandez-Alonso, C. M., Herrera, C., Lluis, C., Franco, R., Nogueira, M. (2001). Cytokines regulate membrane adenosine deaminase on human activated lymphocytes. J. Leukoc. Biol. 70: 920-930 [Abstract] [Full Text]
Aytac, U., Claret, F.-X., Ho, L., Sato, K., Ohnuma, K., Mills, G. B., Cabanillas, F., Morimoto, C., Dang, N. H. (2001). Expression of CD26 and Its Associated Dipeptidyl Peptidase IV Enzyme Activity Enhances Sensitivity to Doxorubicin-induced Cell Cycle Arrest at the G2/M Checkpoint. Cancer Res. 61: 7204-7210 [Abstract] [Full Text]
Ho, L., Aytac, U., Stephens, L. C., Ohnuma, K., Mills, G. B., McKee, K. S., Neumann, C., LaPushin, R., Cabanillas, F., Abbruzzese, J. L., Morimoto, C., Dang, N. H. (2001). In Vitro and in Vivo Antitumor Effect of the Anti-CD26 Monoclonal Antibody 1F7 on Human CD30+ Anaplastic Large Cell T-Cell Lymphoma Karpas 299. Clin. Cancer Res. 7: 2031-2040 [Abstract] [Full Text]
Richard, E., Arredondo-Vega, F. X., Santisteban, I., Kelly, S. J., Patel, D. D., Hershfield, M. S. (2000). The Binding Site of Human Adenosine Deaminase for CD26/Dipeptidyl Peptidase IV: The Arg142Gln Mutation Impairs Binding to CD26 but Does Not Cause Immune Deficiency. JEM 192: 1223-1236 [Abstract] [Full Text]
Ikushima, H., Munakata, Y., Ishii, T., Iwata, S., Terashima, M., Tanaka, H., Schlossman, S. F., Morimoto, C. (2000). Internalization of CD26 by mannose 6-phosphate/insulin-like growth factor II receptor contributes to T cell activation. Proc. Natl. Acad. Sci. USA 97: 8439-8444 [Abstract] [Full Text]
Iwata, S., Morimoto, C. (1999). CD26/Dipeptidyl Peptidase IV in Context: the Different Roles of a Multifunctional Ectoenzyme in Malignant Transformation. JEM 190: 301-306 [Full Text]
Wesley, U. V., Albino, A. P., Tiwari, S., Houghton, A. N. (1999). A Role for Dipeptidyl Peptidase IV in Suppressing the Malignant Phenotype of Melanocytic Cells. JEM 190: 311-322 [Abstract] [Full Text]
Iwata, S., Yamaguchi, N., Munakata, Y., Ikushima, H., Lee, J. F., Hosono, O., Schlossman, S. F., Morimoto, C. (1999). CD26/dipeptidyl peptidase IV differentially regulates the chemotaxis of T cells and monocytes toward RANTES: possible mechanism for the switch from innate to acquired immune response. Int Immunol 11: 417-426 [Abstract] [Full Text]
Duke-Cohan, J. S., Morimoto, C., Rocker, J. A., Schlossman, S. F. (1995). A Novel Form of Dipeptidylpeptidase IV Found in Human Serum. J. Biol. Chem. 270: 14107-14114 [Abstract] [Full Text]
Callebaut, C, Krust, B, Jacotot, E, Hovanessian, A. (1993). T cell activation antigen, CD26, as a cofactor for entry of HIV in CD4+ cells. Science 262: 2045-2050 [Abstract]
Kameoka, J, Tanaka, T, Nojima, Y, Schlossman, S., Morimoto, C (1993). Direct association of adenosine deaminase with a T cell activation antigen, CD26. Science 261: 466-469 [Abstract]