Sentences with phrase «ephrin receptor»

(h) Human phospho - receptor tyrosine kinase array for EphA2, EphB2 and EphB4 ephrin receptors from control BP (shCtr) and BP silenced for Tie2 (siTie2 I and siTie2 II).

For intance, GluA2 binds to PDZ domains 4 and 5 (Dong et al 1997), while ephrin receptors bind to domains 6 and 7 (Torres et al 1998).

Not exact matches

The team was successful in getting the drug to piggyback on 123B9, an agent they devised to target an oncogene called EphA2 (ephrin type - A receptor 2).

Recently, however, ephrins and Eph receptors have also been found in extracellular vesicles / exosomes — small droplets of fat released by cells, used as transport vehicles, signal transmitters or for eliminating cell components.

When an ephrin meets the Eph receptor of another cell, they join to form an ephrin - Eph complex.

One way this communication happens is through the ephrin / Eph - receptor system, which is able to guide cell migration and the growth of neuronal extensions.

Ephrins and Eph receptors have also been found in the exosomes of cancer cells.

Eph receptors and their binding partners, the ephrins, are found on the surface of almost all cell types.

«This is why it's so fundamentally important to understand how cells use this system to communicate,» says Rüdiger Klein, whose Department at the Max Planck Institute of Neurobiology is studying ephrins and Eph receptors.

Eph receptors and their partner proteins, the ephrins, are vital for intercellular communication.

However, Rüdiger Klein and his team at the Max Planck Institute of Neurobiology have now shown that cells can also pack and release active ephrins and Eph receptors through extracellular vesicles.

The ephrins and Eph receptors in angiogenesis.

Eph receptor and ephrin ligand signalling has been implicated in vascular development and in in vivo models of angiogenesis where bi-directional signalling mediates juxtracrine cell — cell contact, cell adhesion to extracellular matrix and cell migration30, 31,32.

Studies by ours and other groups have shown that a number of EphA2 and EphA3 mutations inactivate Eph receptor canonical signaling by disrupting ephrin binding or kinase activity, consistent with a role of canonical signaling in tumor suppression.

Certain Eph receptors and ephrins promote tumor angiogenesis.

This knowledge is useful for the development of disease treatments based on modulating Eph receptor / ephrin activities.

This leads to bidirectional signals emanating from Eph receptor - ephrin complexes positioned at sites of cell - cell contact.

Binding to ephrin ligands on the surface of neighboring cells induces canonical signaling involving receptor clustering, autophosphorylation on tyrosine residues, and kinase activity - dependent downstream signaling.

(A) Eph receptor - ephrin binding at cell - cell contact sites results in the dimerization / clustering of Eph receptor - ephrin complexes, and initiation of canonical signals through the receptor cytoplasmic domain.

We discovered several Eph receptors and ephrins, and research in our laboratory is dedicated to the characterization of Eph receptor signal transduction mechanisms and biological functions using biochemical, mass spectrometry, molecular biology and cell biology approaches in conjunction with animal models.

We also found that the EphB4 receptor expressed on the surface of breast cancer cells can promote tumor xenograft growth by enhancing blood vessel formation through interactions with its preferred ligand, ephrin - B2, present in tumor endothelial cells.

We found that canonical signaling by the EphB4 receptor is low in breast cancer cells and that ephrin - induced stimulation of EphB4 kinase activity inhibits breast cancer cell malignancy in culture and tumor growth in vivo (Figure 1A) through inhibition of the CRK proto - oncogene.

Receptor tyrosine kinases of the Eph family and their ligands, the ephrins, represent an important cell communication system that controls a vast array physiological and disease processes.

Most of the peptides are antagonists, but the peptides targeting EphA2 are agonists that activate receptor signaling and endocytosis similarly to the natural ephrin ligands.

These activities are independent of ephrin binding and / or kinase activity and their mechanism is not well understood but in some cases depends on Eph receptor phosphorylation on serine / threonine residues (red circle).

This is unlike the natural ephrin ligands, each of which promiscuously binds to multiple Eph receptors.

We have identified tyrosine and serine / threonine phosphorylation sites of Eph receptors and ephrins using mass spectrometry and investigated the signaling role of these phosphorylation sites.

Understanding the effects of Eph receptor mutations in cancer cells will help shed light on the role of the Eph receptor / ephrin system in cancer cell transformation, malignant progression and drug resistance.

Peptides can target the ephrin - binding pocket of Eph receptors with high affinity and specificity, affecting receptor function.

(A) Peptides targeting the Eph receptors can function as antagonists that inhibit ephrin binding and receptor signaling, or in some cases as agonists that mimic the ephrins by activating Eph receptor signaling.

Binding to the Eph receptors can also cause the ephrins, which have a cytoplasmic domain or a GPI - anchor, to transmit signals.