UVB-Mediated Induction of Cytokines and Growth Factors in Pterygium Epithelial Cells Involves Cell Surface Receptors and Intracellular Signaling

2006 ◽  
Vol 47 (6) ◽  
pp. 2430 ◽  
Author(s):  
Nick Di Girolamo ◽  
Denis Wakefield ◽  
Minas T. Coroneo
Keyword(s):  
Growth Factors ◽  
Epithelial Cells ◽  
Cell Surface ◽  
Intracellular Signaling ◽  
Cell Surface Receptors ◽  
Surface Receptors

Biological specificity and measurable physical properties of cell surface receptors and their possible role in signal transduction through the cytoskeleton

1995 ◽  
Vol 73 (7-8) ◽  
pp. 317-326 ◽  
Author(s):  
G. Forgacs
Keyword(s):  
Cell Adhesion ◽  
Cell Surface ◽  
Physical Properties ◽  
Adhesion Molecules ◽  
Cell Adhesion Molecules ◽  
Intracellular Signaling ◽  
Genetically Engineered ◽  
Cell Surface Receptors ◽  
Adhesive Properties ◽  
Surface Receptors

It is proposed that the binding specificities of cell adhesion molecules are manifested in their measurable physical properties. A method specifically designed to measure the interfacial tension of cell aggregates is described. With the introduction of a statistical mechanical model, the measured values of tensions for aggregates consisting of genetically engineered cells with controlled adhesive properties are used to obtain information on the strength of individual receptor–ligand bonds. The strength of binding must depend on the receptor and its ligand and reflects the amino acid sequence of the binding proteins. Many of the cell surface receptors, being transmembrane proteins, are attached to the various macromolecular networks of the cytoskeleton; therefore, it is suggested that their ligation and ensuing conformational change may substantially affect the mechanical state of the cytoskeletal assemblies. Since these assemblies are believed to actively participate in intracellular signaling by transmitting signals from the cell membrane into the nucleus, the cell adhesion molecules may influence signaling in a predictable way through their measurable physical characteristics. In particular, varying bond strength at the cell surface may lead to differential gene regulation.Key words: cell adhesion, surface tension, signaling, network, filament.

scholarly journals Tyrosine phosphorylation of CD6 by stimulation of CD3: augmentation by the CD4 and CD2 coreceptors.

1993 ◽  
Vol 177 (1) ◽  
pp. 219-223 ◽  
Author(s):  
S Wee ◽  
G L Schieven ◽  
J M Kirihara ◽  
T T Tsu ◽  
J A Ledbetter ◽  
...  
Keyword(s):  
T Cells ◽  
T Cell ◽  
Cell Surface ◽  
T Cell Activation ◽  
Intracellular Signaling ◽  
Cell Activation ◽  
Cell Receptor ◽  
Surface Proteins ◽  
Cell Surface Receptors ◽  
Surface Receptors

When T cells are activated via the T cell receptor (TCR) complex a number of cellular substrates, including some cell surface proteins, become phosphorylated on tyrosine (Tyr) residues. Phosphorylation of cytoplasmic Tyr renders these cell surface receptors competent to interact with proteins that link cell surface receptors to protein in the intracellular signaling pathways. Here we show that Tyr residues in the cytoplasmic domain of CD6 become phosphorylated upon T cell activation via the TCR complex. Tyr phosphorylation was observed when the T cells were activated by crosslinking CD3 or by cocrosslinking CD3 with CD2 or CD4, but not when the cells were stimulated by crosslinking CD2, CD4, or CD28 alone. Unlike other Tyr kinase substrates, such as the phospholipase C gamma 1-associated pp35/36 protein, whose level of Tyr phosphorylation is highest when T cells are activated by cocrosslinking CD3 with CD2, the levels of CD6 Tyr phosphorylation are highest when T cells were activated by cocrosslinking CD3 with CD4.

3.6 A sensitive method to detect cell surface receptors using biotinylated growth factors

1992 ◽  
Vol 26 (1-4) ◽  
pp. 119-123 ◽  
Author(s):  
M.O. De Jong ◽  
H. Rozemuller ◽  
J.W.M. Visser ◽  
J.G.J. Bauman
Keyword(s):  
Growth Factors ◽  
Cell Surface ◽  
Cell Surface Receptors ◽  
Surface Receptors ◽  
Sensitive Method

scholarly journals Fibroblast Growth Factor Receptor 2 Phosphorylation on Serine 779 Couples to 14-3-3 and Regulates Cell Survival and Proliferation

2008 ◽  
Vol 28 (10) ◽  
pp. 3372-3385 ◽  
Author(s):  
Ana Lonic ◽  
Emma F. Barry ◽  
Cindy Quach ◽  
Bostjan Kobe ◽  
Neil Saunders ◽  
...  
Keyword(s):  
Cell Surface ◽  
Cell Survival ◽  
Intracellular Signaling ◽  
Mitogen Activated Protein Kinase ◽  
Cell Surface Receptors ◽  
Specific Cell ◽  
Fibroblast Growth ◽  
Surface Receptors ◽  
Biological Responses ◽  
Cell Survival And Proliferation

ABSTRACT The fibroblast growth factors (FGFs) exert their diverse (or pleiotropic) biological responses through the binding and activation of specific cell surface receptors (FGFRs). While FGFRs are known to initiate intracellular signaling through receptor tyrosine phosphorylation, the precise mechanisms by which the FGFRs regulate pleiotropic biological responses remain unclear. We now identify a new mechanism by which FGFR2 is able to regulate intracellular signaling and cellular responses. We show that FGFR2 is phosphorylated on serine 779 (S779) in response to FGF2. S779, which lies adjacent to the phospholipase Cγ binding site at Y766, provides a docking site for the 14-3-3 phosphoserine-binding proteins and is essential for the full activation of the phosphatidylinositol 3-kinase and Ras/mitogen-activated protein kinase pathways. Furthermore, S779 signaling is essential for promoting cell survival and proliferation in both Ba/F3 cells and BALB/c 3T3 fibroblasts. This new mode of FGFR2 phosphoserine signaling via the 14-3-3 proteins may provide an increased repertoire of signaling outputs to allow the regulation of pleiotropic biological responses. In this regard, we have identified conserved putative phosphotyrosine/phosphoserine motifs in the cytoplasmic domains of diverse cell surface receptors, suggesting that they may perform important functional roles beyond the FGFRs.

Sign in / Sign up

Export Citation Format

Share Document