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Development, Vol 120, Issue 9 2539-2553, Copyright © 1994 by Company of Biologists


JOURNAL ARTICLES

Platelet endothelial cell adhesion molecule-1 (PECAM-1/CD31): alternatively spliced, functionally distinct isoforms expressed during mammalian cardiovascular development

HS Baldwin, HM Shen, HC Yan, HM DeLisser, A Chung, C Mickanin, T Trask, NE Kirschbaum, PJ Newman, SM Albelda and al. et
Department of Pediatrics, Children's Hospital of Philadelphia, PA 19104.

The establishment of the cardiovascular system represents an early, critical event essential for normal embryonic development. An important component of vascular ontogeny is the differentiation and development of the endothelial and endocardial cell populations. This involves, at least in part, the expression and function of specific cell surface receptors required to mediate cell-cell and cell-matrix adhesion. Platelet endothelial cell adhesion molecule-1 (PECAM-1, CD31) may well serve such a function. It is a member of the immunoglobulin superfamily expressed by the entire vascular endothelium in the adult. It is capable of mediating adhesion by a heterophilic mechanism requiring glycosaminoglycans, as well as by a homophilic, glycosaminoglycan independent, mechanism. It has been shown to regulate the expression of other adhesion molecules on naive T cells. This report documents by RT-PCR and immunohistochemical analysis the expression of PECAM-1 during early post implantation mouse embryo development. PECAM-1 was expressed by early endothelial precursors first within the yolk sac and subsequently within the embryo itself. Interestingly, embryonic PECAM-1 was expressed as multiple isoforms in which one or more clusters of polypeptides were missing from the cytoplasmic domain. The sequence and location of the deleted polypeptides corresponded to exons found in the human PECAM-1 gene. The alternatively spliced isoforms were capable of mediating cell-cell adhesion when transfected into L-cells. The isoforms differed, however, in their sensitivity to a panel of anti-PECAM-1 monoclonal antibodies. These data suggest that changes in the cytoplasmic domain of PECAM-1 may affect its function during cardiovascular development, and are consistent with our earlier report that systematic truncation of the cytoplasmic domain of human PECAM-1 resulted in changes in its ligand specificity, divalent cation and glycosaminoglycan dependence, as well as its susceptibility to adhesion blocking monoclonal antibodies. This is the first report of naturally occurring alternatively spliced forms of PECAM-1 having possible functional implications.
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JCBHome page
J. Famiglietti, J. Sun, H. M. DeLisser, and S. M. Albelda
Tyrosine Residue in Exon 14 of the Cytoplasmic Domain of Platelet Endothelial Cell Adhesion Molecule-1 (PECAM-1/CD31) Regulates Ligand Binding Specificity
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B. Delorme, E. Dahl, T. Jarry-Guichard, J.-P. Briand, K. Willecke, D. Gros, and M. Theveniau-Ruissy
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J. P. Newton, C. D. Buckley, E. Y. Jones, and D. L. Simmons
Residues on Both Faces of the First Immunoglobulin Fold Contribute to Homophilic Binding Sites of PECAM-1/CD31
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Genes Dev.Home page
G E Winnier, L Hargett, and B L Hogan
The winged helix transcription factor MFH1 is required for proliferation and patterning of paraxial mesoderm in the mouse embryo.
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D. E. Jackson, C. M. Ward, R. Wang, and P. J. Newman
The Protein-tyrosine Phosphatase SHP-2 Binds Platelet/Endothelial Cell Adhesion Molecule-1 (PECAM-1) and Forms a Distinct Signaling Complex during Platelet Aggregation. EVIDENCE FOR A MECHANISTIC LINK BETWEEN PECAM-1- AND INTEGRIN-MEDIATED CELLULAR SIGNALING
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DevelopmentHome page
P Soriano
The PDGF alpha receptor is required for neural crest cell development and for normal patterning of the somites
Development, January 7, 1997; 124(14): 2691 - 2700.
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Flk-1, a Receptor for Vascular Endothelial Growth Factor (VEGF), Is Expressed by Retinal Progenitor Cells
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J. Sun, J. Williams, H.-C. Yan, K. M. Amin, S. M. Albelda, and H. M. DeLisser
Platelet Endothelial Cell Adhesion Molecule-1 (PECAM-1) Homophilic Adhesion Is Mediated by Immunoglobulin-like Domains 1and 2and Depends on the Cytoplasmic Domain and the Level of Surface Expression
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C. Alexander, E. Hansell, O Behrendtsen, M. Flannery, N. Kishnani, S. Hawkes, and Z Werb
Expression and function of matrix metalloproteinases and their inhibitors at the maternal-embryonic boundary during mouse embryo implantation
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C. Buckley, R Doyonnas, J. Newton, S. Blystone, E. Brown, S. Watt, and D. Simmons
Identification of alpha v beta 3 as a heterotypic ligand for CD31/PECAM-1
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H.-C. Yan, H. S. Baldwin, J. Sun, C. A. Buck, S. M. Albelda, and H. M. DeLisser
Alternative Splicing of a Specific Cytoplasmic Exon Alters the Binding Characteristics of Murine Platelet/Endothelial Cell Adhesion Molecule-1 (PECAM-1)
J. Biol. Chem., October 6, 1995; 270(40): 23672 - 23680.
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DevelopmentHome page
L Kwee, H. Baldwin, H. Shen, C. Stewart, C Buck, C. Buck, and M. Labow
Defective development of the embryonic and extraembryonic circulatory systems in vascular cell adhesion molecule (VCAM-1) deficient mice
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K.-i. Hirata, T. Ishida, K. Penta, M. Rezaee, E. Yang, J. Wohlgemuth, and T. Quertermous
Cloning of an Immunoglobulin Family Adhesion Molecule Selectively Expressed by Endothelial Cells
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J. Peng, L. Zhang, L. Drysdale, and G.-H. Fong
The transcription factor EPAS-1/hypoxia-inducible factor 2alpha plays an important role in vascular remodeling
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G. Cao, C. D. O'Brien, Z. Zhou, S. M. Sanders, J. N. Greenbaum, A. Makrigiannakis, and H. M. DeLisser
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