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1

Role of intercellular interactions in tumor progression and metastasis

100%
Dus D.
Postępy Higieny i Medycyny Doświadczalnej
|
1995
|
vol. 49
|
issue 1
67-75
2

Mouse Ly-6 proteins and their extended family: markers of cell differentiation and regulators of cell signaling

88%
Bamezai A.
Archivum Immunologiae et Therapiae Experimentalis
|
2004
|
vol. 52
|
issue 4
255-266
EN
The Ly-6 locus on mouse chromosome 15 encodes a family of 10?12 kDa proteins that are linked to the cell surface by a glycosylphosphatidyl-inositol anchor and have cell signaling and cell adhesion properties. Expression of Ly-6 proteins is tightly regulated during development; these proteins continue to serve as excellent differentiation surface markers on normal and abnormal cells, but their role in driving cellular differentiation is still emerging. Recent studies suggest that Ly-6 gene products participate in regulating signaling through other cell type-specific receptors, perhaps by virtue of these proteins being localized in lipid rafts that play a key role in relaying signals from the membrane to the nucleus. Ligands for some Ly-6 proteins have been reported; the consequence of their interactions with the Ly-6 receptor remains to be fully uncovered. Mouse Ly-6-like proteins have also been reported from a variety of life forms ranging from Caenorhabditis elegans to humans that show a limited amino acid identity and share structural features with members of mouse Ly-6. Despite these similarities, the non-murine Ly-6 proteins bind distinct ligands and appear to have different cellular functions. All members of the Ly-6 super gene family perhaps evolved from an ancestral gene by a gene duplication mechanism.
3

P-selectin mediates adhesion of leukocytes, platelets, and cancer cells in inflammation, thrombosis, and cancer growth and metastasis

51%
Chen M., Geng J.-G.
Archivum Immunologiae et Therapiae Experimentalis
|
2006
|
vol. 54
|
issue 2
75-84
EN
Stimulated endothelial cells and activated platelets express P-selectin (CD62P), a member of the selectin family of cell adhesion molecules, which interacts with P-selectin glycoprotein ligand-1 (PSGL-1, CD162) for leukocyte rolling on stimulated endothelial cells and heterotypic aggregation of activated platelets onto leukocytes. Cross-linking of PSGL-1 by P-selectin also primes leukocytes intracellularly for cytokine and chemoattractant-induced 2-integrin activation for firm adhesion of leukocytes. Furthermore, P-selectin mediates heterotypic aggregation of activated platelets to cancer cells and adhesion of cancer cells to stimulated endothelial cells. Here we provide a comprehensive summary of the functional roles and the biological importance of P-selectin-mediated cell adhesive interactions in the pathogeneses of inflammation, thrombosis, and the growth and metastasis of cancers.
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