Receptor clustering and activation by multivalent interaction through recognition peptides presented on exosomes

2017 ◽  
Vol 53 (2) ◽  
pp. 317-320 ◽  
Author(s):  
I. Nakase ◽  
N. Ueno ◽  
M. Katayama ◽  
K. Noguchi ◽  
T. Takatani-Nakase ◽  
...  
Keyword(s):  
Cell Surface ◽  
Receptor Activation ◽  
Cell Surface Receptors ◽  
Receptor Clustering ◽  
Surface Receptors ◽  
Peptide Segments

A system for inducing clustering of cell surface receptors via recognition peptide segments displayed on exosomes, leading to receptor activation.

scholarly journals Cyto-friendly polymerization at cell surfaces modulates cell fate by clustering cell-surface receptors

2020 ◽  
Vol 11 (16) ◽  
pp. 4221-4225 ◽  
Author(s):  
Jing Qi ◽  
Weishuo Li ◽  
Xiaoling Xu ◽  
Feiyang Jin ◽  
Di Liu ◽  
...  
Keyword(s):  
Cell Surface ◽  
Cell Fate ◽  
Cell Surface Receptors ◽  
Cell Surfaces ◽  
Receptor Clustering ◽  
Surface Polymerization ◽  
Surface Receptors ◽  
Anti Cd20 ◽  
In Cells

Cell-surface polymerization of anti-CD20 aptamer modified macromer to induce CD20 receptor clustering, and effectively initiate the apoptotic signals in cells.

scholarly journals Vav Family Proteins Couple to Diverse Cell Surface Receptors

2000 ◽  
Vol 20 (17) ◽  
pp. 6364-6373 ◽  
Author(s):  
Sheri L. Moores ◽  
Laura M. Selfors ◽  
Jessica Fredericks ◽  
Timo Breit ◽  
Keiko Fujikawa ◽  
...  
Keyword(s):  
Growth Factor ◽  
Cell Surface ◽  
Tyrosine Phosphorylation ◽  
Tyrosine Kinases ◽  
Protein Tyrosine Kinase ◽  
Receptor Activation ◽  
Cell Surface Receptors ◽  
Nucleotide Exchange ◽  
Surface Receptors ◽  
Downstream Signaling

ABSTRACT Vav proteins are guanine nucleotide exchange factors for Rho family GTPases which activate pathways leading to actin cytoskeletal rearrangements and transcriptional alterations. Vav proteins contain several protein binding domains which can link cell surface receptors to downstream signaling proteins. Vav1 is expressed exclusively in hematopoietic cells and tyrosine phosphorylated in response to activation of multiple cell surface receptors. However, it is not known whether the recently identified isoforms Vav2 and Vav3, which are broadly expressed, can couple with similar classes of receptors, nor is it known whether all Vav isoforms possess identical functional activities. We expressed Vav1, Vav2, and Vav3 at equivalent levels to directly compare the responses of the Vav proteins to receptor activation. Although each Vav isoform was tyrosine phosphorylated upon activation of representative receptor tyrosine kinases, integrin, and lymphocyte antigen receptors, we found unique aspects of Vav protein coupling in each receptor pathway. Each Vav protein coprecipitated with activated epidermal growth factor and platelet-derived growth factor (PDGF) receptors, and multiple phosphorylated tyrosine residues on the PDGF receptor were able to mediate Vav2 tyrosine phosphorylation. Integrin-induced tyrosine phosphorylation of Vav proteins was not detected in nonhematopoietic cells unless the protein tyrosine kinase Syk was also expressed, suggesting that integrin activation of Vav proteins may be restricted to cell types that express particular tyrosine kinases. In addition, we found that Vav1, but not Vav2 or Vav3, can efficiently cooperate with T-cell receptor signaling to enhance NFAT-dependent transcription, while Vav1 and Vav3, but not Vav2, can enhance NFκB-dependent transcription. Thus, although each Vav isoform can respond to similar cell surface receptors, there are isoform-specific differences in their activation of downstream signaling pathways.

scholarly journals Proteasomes Regulate the Duration of Erythropoietin Receptor Activation by Controlling Down-regulation of Cell Surface Receptors

2000 ◽  
Vol 275 (24) ◽  
pp. 18375-18381 ◽  
Author(s):  
Frédérique Verdier ◽  
Pierre Walrafen ◽  
Nathalie Hubert ◽  
Stany Chrétien ◽  
Sylvie Gisselbrecht ◽  
...  
Keyword(s):  
Cell Surface ◽  
Receptor Activation ◽  
Erythropoietin Receptor ◽  
Cell Surface Receptors ◽  
Down Regulation ◽  
Surface Receptors

Proteasomes regulate the duration of erythropoietin receptor activation by controlling down-regulation of cell surface receptors

2000 ◽  
Vol 28 (5) ◽  
pp. A284-A284
Author(s):  
F. Verdier ◽  
P. Walrafen ◽  
N. Hubert ◽  
S. Chretien ◽  
S. Gisselbrecht ◽  
...  
Keyword(s):  
Cell Surface ◽  
Receptor Activation ◽  
Erythropoietin Receptor ◽  
Cell Surface Receptors ◽  
Down Regulation ◽  
Surface Receptors

RECEPTOR-DEPENDENT SENSITIVITY OF NF-κB TO LOW PHYSIOLOGICAL LEVEL

2013 ◽  
Vol 21 (03) ◽  
pp. 1350018
Author(s):  
PANPAN YANG ◽  
TIANSHOU ZHOU
Keyword(s):  
Cell Surface ◽  
Receptor Activation ◽  
Cell Surface Receptors ◽  
High Dose ◽  
Physiological Level ◽  
Information Encoding ◽  
Surface Receptors ◽  
Receptor Number ◽  
Activation Rates

In the NFκB signaling pathway, cells respond to different concentrations of the TNFα signal by means of NFκB transcription factors. Previous studies showed that most cells are activated under high-dose stimulations and NFκB activation results in oscillations in nuclear NFκB abundance. Here, by analyzing sensitivity gain for the response of the nuclear NFκB to the number of cell-surface receptors under low-dose stimulations, we show that changes in the receptor number can give rise to significant changes in the nonsaturation part of the dose–response curve, where the receptor activation rates are very sensitive to stimulations. In addition, the number of the activated receptors tends to increase in a large range of stimulation dose and can significantly influence the expression of the downstream genes. These results imply that the number of cell-surface receptors plays a role of information encoding like frequency or amplitude encoding described in previous studies.

Interactions of VEGF isoforms with VEGFR-1, VEGFR-2, and neuropilin in vivo: a computational model of human skeletal muscle

2007 ◽  
Vol 292 (1) ◽  
pp. H459-H474 ◽  
Author(s):  
Feilim Mac Gabhann ◽  
Aleksander S. Popel
Keyword(s):  
Skeletal Muscle ◽  
Extracellular Matrix ◽  
Cell Surface ◽  
Computational Model ◽  
Receptor Activation ◽  
Cell Surface Receptors ◽  
Vastus Lateralis Muscle ◽  
Surface Receptors ◽  
Vegf Isoforms

The vascular endothelial growth factor (VEGF) family of cytokines is involved in the maintenance of existing adult blood vessels as well as in angiogenesis, the sprouting of new vessels. To study the proangiogenic activation of VEGF receptors (VEGFRs) by VEGF family members in skeletal muscle, we develop a computational model of VEGF isoforms (VEGF121, VEGF165), their cell surface receptors, and the extracellular matrix in in vivo tissue. We build upon our validated model of the biochemical interactions between VEGF isoforms and receptor tyrosine kinases (VEGFR-1 and VEGFR-2) and nonsignaling neuropilin-1 coreceptors in vitro. The model is general and could be applied to any tissue; here we apply the model to simulate the transport of VEGF isoforms in human vastus lateralis muscle, which is extensively studied in physiological experiments. The simulations predict the distribution of VEGF isoforms in resting (nonexercising) muscle and the activation of VEGFR signaling. Little of the VEGF protein in muscle is present as free, unbound extracellular cytokine; the majority is bound to the cell surface receptors or to the extracellular matrix. However, interstitial sequestration of VEGF165 does not affect steady-state receptor binding. In the absence of neuropilin, VEGF121 and VEGF165 behave similarly, but neuropilin enhances the binding of VEGF165 to VEGFR-2. This model is the first to study VEGF tissue distribution and receptor activation in human muscle, and it provides a platform for the design and evaluation of therapeutic approaches.

scholarly journals Cell Surface Receptors: Rapid Quantification of Live Cell Receptors Using Bioluminescence in a Flow-Based Microfluidic Device (Small 8/2015)

Small ◽  
2015 ◽  
Vol 11 (8) ◽  
pp. 1012-1012
Author(s):  
Ramesh Ramji ◽  
Cheong Fook Cheong ◽  
Hiroaki Hirata ◽  
Abdur Rub Abdur Rahman ◽  
Chwee Teck Lim
Keyword(s):  
Cell Surface ◽  
Microfluidic Device ◽  
Live Cell ◽  
Cell Surface Receptors ◽  
Cell Receptors ◽  
Surface Receptors ◽  
Rapid Quantification
Sign in / Sign up

Export Citation Format

Share Document