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Blood, 1 November 2003, Vol. 102, No. 9, pp. 3371-3378. Prepublished online as a Blood First Edition Paper on July 17, 2003; DOI 10.1182/blood-2002-11-3462. This Article Full Text Full Text (PDF) All Versions of this Article: 2002-11-3462v1 102/9/3371    most recent 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 PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Moog-Lutz, C. Articles by Lutz, P. G. Search for Related Content PubMed PubMed Citation Articles by Moog-Lutz, C. Articles by Lutz, P. G. Related Collections Neoplasia Cell Adhesion and Motility Gene Expression Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  NEOPLASIA JAML, a novel protein with characteristics of a junctional adhesion molecule, is induced during differentiation of myeloid leukemia cells Christel Moog-Lutz, Florence Cavé-Riant, Florence C. Guibal, Marie A. Breau, Yolande Di Gioia, Pierre Olivier Couraud, Yvon E. Cayre, Sandrine Bourdoulous, and Pierre G. Lutz From Hôpital Robert Debré, Institut National de la Santé et de la Recherche Médicale (INSERM) Unité 417; and Institut Cochin, INSERM Unité 567, Centre National de la Recherche Scientifique (CNRS) UMR8104, Université Paris V, Paris, France. Retinoic acid induces clinical remission in acute promyelocytic leukemia (APL) by triggering differentiation of leukemia promyelocytes. Here, we have characterized a gene encoding a member of the immunoglobulin superfamily, among novel retinoic acid–induced genes identified in APL cells. This protein, which was named JAML (junctional adhesion molecule–like), contains 2 extracellular immunoglobulin-like domains, a transmembrane segment, and a cytoplasmic tail. JAML mRNA is expressed in hematopoietic tissues and is prominently expressed in granulocytes. The fact that JAML protein is localized at the cell plasma membrane in the areas of cell-cell contacts, whereas it is not detected at free cell borders, suggests that JAML is engaged in homophilic interactions. Furthermore, a conserved dimerization motif among JAM members was shown to be important for JAML localization at the cell membrane. Finally, exogenous expression of JAML in myeloid leukemia cells resulted in enhanced cell adhesion to endothelial cells. Altogether, our results point to JAML as a novel member of the JAM family expressed on leukocytes with a possible role in leukocyte transmigration. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: C. F. Burande, M. L. Heuze, I. Lamsoul, B. Monsarrat, S. Uttenweiler-Joseph, and P. G. Lutz A Label-free Quantitative Proteomics Strategy to Identify E3 Ubiquitin Ligase Substrates Targeted to Proteasome Degradation Mol. Cell. Proteomics, July 1, 2009; 8(7): 1719 - 1727. [Abstract] [Full Text] [PDF] R. L. Zemans, S. P. Colgan, and G. P. Downey Transepithelial Migration of Neutrophils: Mechanisms and Implications for Acute Lung Injury Am. J. Respir. Cell Mol. Biol., May 1, 2009; 40(5): 519 - 535. [Abstract] [Full Text] [PDF] A.-C. Luissint, P. G. Lutz, D. A. Calderwood, P.-O. Couraud, and S. Bourdoulous JAM-L-mediated leukocyte adhesion to endothelial cells is regulated in cis by {alpha}4{beta}1 integrin activation J. Cell Biol., December 15, 2008; 183(6): 1159 - 1173. [Abstract] [Full Text] [PDF] M. L. Heuze, I. Lamsoul, M. Baldassarre, Y. Lad, S. Leveque, Z. Razinia, C. Moog-Lutz, D. A. Calderwood, and P. G. Lutz ASB2 targets filamins A and B to proteasomal degradation Blood, December 15, 2008; 112(13): 5130 - 5140. [Abstract] [Full Text] [PDF] M. U. Naik, T. U. Naik, A. T. Suckow, M. K. Duncan, and U. P. Naik Attenuation of Junctional Adhesion Molecule-A Is a Contributing Factor for Breast Cancer Cell Invasion Cancer Res., April 1, 2008; 68(7): 2194 - 2203. [Abstract] [Full Text] [PDF] D. A. Ferguson, M. R. Muenster, Q. Zang, J. A. Spencer, J. J. Schageman, Y. Lian, H. R. Garner, R. B. Gaynor, J. W. Huff, A. Pertsemlidis, et al. Selective Identification of Secreted and Transmembrane Breast Cancer Markers using Escherichia coli Ampicillin Secretion Trap Cancer Res., September 15, 2005; 65(18): 8209 - 8217. [Abstract] [Full Text] [PDF] K. Zen, Y. Liu, I. C. McCall, T. Wu, W. Lee, B. A. Babbin, A. Nusrat, and C. A. Parkos Neutrophil Migration across Tight Junctions Is Mediated by Adhesive Interactions between Epithelial Coxsackie and Adenovirus Receptor and a Junctional Adhesion Molecule-like Protein on Neutrophils Mol. Biol. Cell, June 1, 2005; 16(6): 2694 - 2703. [Abstract] [Full Text] [PDF] K. Ebnet, A. Suzuki, S. Ohno, and D. Vestweber Junctional adhesion molecules (JAMs): more molecules with dual functions? J. Cell Sci., January 1, 2004; 117(1): 19 - 29. [Abstract] [Full Text] [PDF]

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