HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in ISI Web of Science Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via ISI Web of Science (15) Citing Articles via Google Scholar Google Scholar Articles by HARVEY, S. Articles by SMITH, J. W. Search for Related Content PubMed PubMed Citation Articles by HARVEY, S. Articles by SMITH, J. W.

Insights into a plasma membrane signature

Program on Cell Adhesion, Cancer Research Center, The Burnham Institute, La Jolla, California 92037

The plasma membrane (PM) is an organized biological system that serves as a structural barrier and communication interface with the extracellular environment. Many basic questions regarding the PM as a system remain unanswered. In particular, we do not understand the scope of similarity and differences in protein expression at the PM. This study takes an initial step toward addressing these questions by comparing the PM proteomes of fibroblasts and mammary carcinoma cells. Three sets of proteins were revealed by the study. The first set comprises between 9 and 23% of all proteins at the PM and appears to be common to both fibroblasts and mammary carcinoma. A second group of proteins, comprising 40% of the proteins at the PM, is tightly linked to cell lineage. The third set of proteins is unique to each cell line and is independent of cell lineage. It is reasonable to hypothesize then, that this third group of proteins is responsible for unique aspects of cell behavior. In an effort to find proteins linked to the metastatic phenotype, we identified several proteins that are uniquely expressed at the PM of the metastatic MDA-MB-435 cells. These proteins have functions ranging from cell adhesion to the regulation of translation and the control of oxidant stress.

proteome; expression profiling; breast cancer; metastasis

This article has been cited by other articles:

				I. Camby, M. Le Mercier, F. Lefranc, and R. Kiss Galectin-1: a small protein with major functions Glycobiology, November 1, 2006; 16(11): 137R - 157R. [Abstract] [Full Text] [PDF]

				L. M. Knowles, F. Axelrod, C. D. Browne, and J. W. Smith A Fatty Acid Synthase Blockade Induces Tumor Cell-cycle Arrest by Down-regulating Skp2 J. Biol. Chem., July 16, 2004; 279(29): 30540 - 30545. [Abstract] [Full Text] [PDF]

				A. Marmagne, M.-A. Rouet, M. Ferro, N. Rolland, C. Alcon, J. Joyard, J. Garin, H. Barbier-Brygoo, and G. Ephritikhine Identification of New Intrinsic Proteins in Arabidopsis Plasma Membrane Proteome Mol. Cell. Proteomics, July 1, 2004; 3(7): 675 - 691. [Abstract] [Full Text] [PDF]

				S. J. Kridel, F. Axelrod, N. Rozenkrantz, and J. W. Smith Orlistat Is a Novel Inhibitor of Fatty Acid Synthase with Antitumor Activity Cancer Res., March 15, 2004; 64(6): 2070 - 2075. [Abstract] [Full Text] [PDF]

				V. J. Dzau and S. Glueck Physiological Genomics: Who we are and where we're going Physiol Genomics, December 21, 2001; 7(2): 65 - 67. [Full Text] [PDF]

				R. J. Perrin, W. S. Woods, D. F. Clayton, and J. M. George Exposure to Long Chain Polyunsaturated Fatty Acids Triggers Rapid Multimerization of Synucleins J. Biol. Chem., November 2, 2001; 276(45): 41958 - 41962. [Abstract] [Full Text] [PDF]