+ Site Statistics
+ Search Articles
+ PDF Full Text Service
How our service works
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ Translate
+ Recently Requested

Spatial and Temporal Relationships between Cadherins and PECAM-1 in Cell-Cell Junctions of Human Endothelial Cells



Spatial and Temporal Relationships between Cadherins and PECAM-1 in Cell-Cell Junctions of Human Endothelial Cells



Journal of Cell Biology 126(1): 247-258



The integrity of the endothelial layer, which lines the entire cavity of the vascular system, depends on tight adhesion of the cells to the underlying basement membrane as well as to each other. It has been previously shown that such interactions occur via membrane receptors that determine the specificity, topology, and mechanical properties of the surface adhesion. Cell-cell junctions between endothelial cells, in culture and in situ, involve both Ca(2+)-dependent and -independent mechanisms that are mediated by distinct adhesion molecules. Ca(2+)-dependent cell-cell adhesion occurs mostly via members of the cadherin family, which locally anchor the microfilament system to the plasma membrane, in adherens junctions. Ca(2+)-independent adhesions were reported to mainly involve members of the Ig superfamily. In this study, we performed three-dimensional microscopic analysis of the relative subcellular distributions of these two endothelial intercellular adhesion systems. We show that cadherins are located at adjacent (usually more apical), yet clearly distinct domains of the lateral plasma membrane, compared to PECAM-1. Moreover, cadherins were first organized in adherens junctions within 2 h after seeding of endothelial cells, forming multiple lateral patches which developed into an extensive belt-like structure over a period of 24 h. PECAM-1 became associated with surface adhesions significantly later and became progressively associated with the cadherin-containing adhesions. Cadherins and PECAM-1 also differed in their detergent extractability, reflecting differences in their mode of association with the cytoskeleton. Moreover, the two adhesion systems could be differentially modulated since short treatment with the Ca2+ chelator EGTA, disrupted the cadherin junctions leaving PECAM-1 apparently intact. These results confirm that endothelial cells possess distinct intercellular contact mechanisms that differ in their spatial and temporal organization as well as in their functional properties.

Please choose payment method:






(PDF emailed within 0-6 h: $19.90)

Accession: 009438188

Download citation: RISBibTeXText

PMID: 8027182

DOI: 10.2307/1616401


Related references

Escherichia coli K1 invasion increases human brain microvascular endothelial cell monolayer permeability by disassembling vascular-endothelial cadherins at tight junctions. Journal of Infectious Diseases 188(9): 1295-1309, 2003

Modulation of PECAM-1 cell surface expression, endothelial cell permeability and transendothelial migration of leukocytes in response to secretoneurin in human endothelial cells. European Heart Journal 18(ABSTR Suppl. ): 145, 1997

Molecular cloning of pecam 1 cd 31 a novel member of the immunoglobulin gene superfamily expressed on human platelets and at endothelial cell intercellular junctions. Journal of Cellular Biochemistry Suppl. (14 Part E): 195, 1990

Gaq-PECAM-1 complexes at endothelial cell junctions dissociate upon shear. FASEB Journal 17(4-5): Abstract No 864 12, 2003

Changes in the distribution of cadherins, PECAM-1, F-actin, and phospho-tyrosine during intercellular contact formation of human umbilical vein endothelial cells in culture. Molecular Biology of the Cell 8(Suppl. ): 203A, 1997

Cell-cell junctions of dermal microvascular endothelial cells contain tight and adherens junction proteins in spatial proximity. Biochemistry 43(18): 5360-5369, 2004

Platelet/endothelial cell adhesion molecule-1 (PECAM-1) expression by human brain microvessel endothelial cells in primary culture. Brain Research 731(1-2): 217-220, 1996

PECAM-1 regulates proangiogenic properties of endothelial cells through modulation of cell-cell and cell-matrix interactions. American Journal of Physiology. Cell Physiology 299(6): C1468-C1484, 2010

The Role of Sialylated Glycans in Human Platelet Endothelial Cell Adhesion Molecule 1 (PECAM-1)-mediated Trans Homophilic Interactions and Endothelial Cell Barrier Function. Journal of Biological Chemistry 291(50): 26216-26225, 2016

Genetic evidence for functional redundancy of Platelet/Endothelial cell adhesion molecule-1 (PECAM-1): CD31-deficient mice reveal PECAM-1-dependent and PECAM-1-independent functions. Journal of Immunology 162(5): 3022-3030, 1999

Regulation of TNF-a-induced reorganization of the actin cytoskeleton and cell-cell junctions by Rho, Rac, and Cdc42 in human endothelial cells. Journal of Cellular Physiology 176(1): 0-65, 1998

Alteration of cell-cell junctions in cultured human lymphatic endothelial cells with inflammatory cytokine stimulation. Lymphatic Research and Biology 12(3): 136-143, 2014

Regulation of TNF-alpha-induced reorganization of the actin cytoskeleton and cell-cell junctions by Rho, Rac, and Cdc42 in human endothelial cells. Journal of Cellular Physiology 176(1): 150-165, 1998

Antibody mediated ligation of platelet/endothelial cell adhesion molecule-1 (PECAM-1) on neutrophils enhances adhesion to cultured human dermal microvascular endothelial cells. Kobe Journal of Medical Sciences 42(4): 233-241, 1996

Asiatic acid stabilizes cytoskeletal proteins and prevents TNF-α-induced disorganization of cell-cell junctions in human aortic endothelial cells. Vascular Pharmacology 117: 15-26, 2019