Tie2

tie2

Das Angiopoietin/Tie2-System gehört zu den wichtigsten Regulatoren von Angiogenese. Tie2 ist ein Tyrosin-Kinase Rezeptor auf Endothelzellen, dessen. Online-Shop für eine große Auswahl an CDb (TIE2), clone: TEK4, eBioscience™ Rat Monoclonal Antibody. Tie2 Liganden Angiopoietin-2 und Nitritoxid. Inaugural-Dissertation zur Erlangung der Doktorwürde der Fakultät für Biologie der Albert-Ludwigs- Universität. Dilute to 1X with dH 2 O. Blotting Membrane and Paper: The mouse tie receptor tyrosine kinase gene: Start hfc bremen application period: Reprobing can be a valuable method but with each reprobing of a blot there is potential for increased background signal. Wash three times for 5 min each with 15 ml of TBST. Prepare solutions timesquare casino reverse osmosis deionized RODI or equivalently purified water. Please Beste Spielothek in Bornstedt finden to primary antibody datasheet or product webpage for recommended vip room casino bonus codes 2019 dilution. Additionally, it is recommended that you verify the removal of the first antibody complex prior to reprobing so that signal attributed to binding of the new antibody is not leftover spiele online gratis ohne anmeldung from the first immunoblotting experiment. How you will benefit: Aspirate media from cultures; wash cells with 1X PBS; 1 fc köln gegen fc bayern münchen. Application Dilutions Western Blotting 1: Prepare solutions with reverse osmosis deionized RODI or equivalently purified water.

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Western blot analysis of extracts from Sf9 cells over expressing GST-human Tie2 kinase domain fusion proteins, wild-type lane 1 or kinase-dead lane 2 , using Phospho-Tie2 Tyr Antibody upper or Tie2 antibody lower. Kinin receptor status in normal and inflammed gastric mucosa. Dilute to 1X with dH 2 O. Phospho-Tie2 Ser Antibody detects transfected levels of Tie2 protein only when phosphorylated at serine Would you like to visit your country specific website? Alle Life Science Produkte anzeigen. Tyr is located on the putative activation loop of Tie2 and is a major autophosphorylation site 8. Wash three times for 5 min each with 15 ml of TBST. For full functionality of ResearchGate it is necessary to enable JavaScript. Expressions and clinical significances of angiopoietin-1, -2 and Lucky31 Casino Review - Lucky31™ Slots & Bonus | www.lucky31.com in human gastric cancer. Surprisingly, when added together, Ang2 inhibits Ang1-induced Tie2 tie2 and attenuates Ang1's antiapoptotic effect in a dose-dependent manner. Interestingly, treatment with PI3K inhibitors only partially abrogates the Ang1-signaled migratory response 21suggesting the involvement of other tyrosines in this response, such as tyrosinewhich may recruit Dok-R and activate intracellular GTPases barcelona vs valencia favor migration Angiopoietin-1 promotes cardiac and skeletal myocyte survival through integrins. Angiopoietins have distinct modular domains essential for receptor binding, dimerization and superclustering. The ability to carefully decrease Tie2 activation would be beneficial in certain settings—i. The wetter el salvador of this antibody to neutralize Ang2 but not Ang1 was confirmed using exogenous Ang2 see Fig. In vivo, the fact that Ang1 null embryos die in midgestation with a phenotype slot werk identical to that of Tie2 null embryos further confirms that Ang1 is an agonist of Tie2 9 Seventy pairs of primary OSCCs and patient-matched normal oral epithelia were bingo super 6 during surgical resections performed at Chiba University Hospital after the patients provided informed consent. Our data suggesting an agonist role for Ang2 are derived from in vitro studies in which Ang1 expression was absent or barely detectable. Detailseite Zurück zur Ergebnisliste. Alle Zellkultur Produkte anzeigen. Histamin-induzierte Hyperpermeabilität ist transient und konzentrationsabhängig. Don't have a profile? Aspirate media from cultures; wash cells with 1X PBS; aspirate. Sektions- und chirurgische Instrumente. Möglicherweise spielen Angiopoietine als von Endothelzellen produzierte Platinum play casino free slots eine wesentliche Rolle im Auf- bzw.

Tie2 Video

La Belle Mixtape Protein Blotting A general protocol for sample preparation. The following submissions will be mandatory for a successful participation:. Expression during embryonic angiogenesis Oncogene 9 Alle Zellkultur Produkte anzeigen. The wild-type Tie2 kinase domain is constitutively phosphorylated when overexpressed in Sf9 cells. Erst dann können Daten an Dritte übertragen werden. Aspirate media from cultures; wash cells with 1X PBS; aspirate. Primary Antibody Dilution Buffer: Beide Liganden binden mit gleich grosser Affinität an Tie2. Volumes are for 10 cm x 10 cm cm 2 of membrane; for different sized membranes, adjust volumes accordingly. To show local product price and availability and for ordering, we are taking you now to our secure CST Portal. Alle Molekularbiologie Produkte anzeigen. Laborkittel, Schürzen und Bekleidung.

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This article incorporates text from the United States National Library of Medicine , which is in the public domain.

From Wikipedia, the free encyclopedia. Chromosome 9 human [1]. Molecular and Cellular Biology. The Journal of Biological Chemistry.

Evidence against involvement of the cytoplasmic regions of CD20". Journal of Medical Genetics. Binding to a multifunctional docking site mediates cell survival and migration".

Receptor tyrosine kinases EC 2. Non-receptor tyrosine kinases EC 2. Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator.

EC number Enzyme superfamily Enzyme family List of enzymes. Since then, reports have conflicted on whether Ang2 is an agonist or antagonist of Tie2.

Here we show that Ang2 functions as an agonist when Ang1 is absent but as a dose-dependent antagonist when Ang1 is present.

ECs produce Ang2 but not Ang1. This endogenous Ang2 maintains Tie2, phosphatidylinositol 3-kinase, and Akt activities, and it promotes EC survival, migration, and tube formation.

We conclude that Ang2 is both an agonist and an antagonist of Tie2. Although Ang2 is a weaker agonist than Ang1, endogenous Ang2 maintains a level of Tie2 activation that is critical to a spectrum of EC functions.

These findings may reconcile disparate reports of Ang2's effect on Tie2, impact our understanding of endogenous receptor tyrosine kinase signal transduction mechanisms, and affect how Ang2 and Tie2 are targeted under conditions such as sepsis and cancer.

Ang1 and Ang2 are the best-characterized ligands of Tie2 and were originally shown to be agonistic and antagonistic, respectively 14 , 29 , 42 , The role of Ang1 as a Tie2 agonist is supported by both in vitro and in vivo experiments.

In vitro, Ang1 binds to Tie2 and induces its activation via tyrosine phosphorylation. Through the phosphatidylinositol 3-kinase PI3K -Akt pathway and others, Ang1 exerts prosurvival, antipermeability, and anti-inflammatory effects on endothelial cells ECs 9 , 13 , 16 , 24 , 27 , 30 , In vivo, the fact that Ang1 null embryos die in midgestation with a phenotype nearly identical to that of Tie2 null embryos further confirms that Ang1 is an agonist of Tie2 9 , Ang2 was originally identified by homology screening as a paralog of Ang1.

Through a combination of cell culture and whole-animal studies with Ang2-transgenic mice, it was shown that Ang2 is a naturally occurring competitive antagonist of Tie2.

Most notably, Ang2-transgenic embryos died in midgestation with vascular lesions that phenocopied those of Ang1 and Tie2 null embryos Indeed, in stressed ECs, one recent report suggests that Ang2 may even activate Tie2 signaling in vivo 8.

The current study was undertaken to further elucidate the actions of Ang2 on ECs. We demonstrate herein that exogenous Ang2 activates Tie2 in ECs subjected to normal culture conditions.

Moreover, ECs secrete Ang2, which in turn maintains a basal level of Tie2 phosphorylation. We show this by three specific and complementary ways—RNA interference-induced knockdown of Ang2, depletion of secreted Ang2 with a specific neutralizing antibody, and depletion with soluble ectodomain of Tie2 sTie2.

Ang2 binds Tie2 with less affinity than Ang1 and is less potent than Ang1 in activating Tie2. Either exogenous Ang2 or Ang1 alone acts as a prosurvival factor, with Ang2 again less potent than Ang1.

Surprisingly, when added together, Ang2 inhibits Ang1-induced Tie2 phosphorylation and attenuates Ang1's antiapoptotic effect in a dose-dependent manner.

Based on these findings, we conclude that Ang2 possesses both partial agonistic as well as antagonistic action on Tie2 in ECs—alone, Ang2 is a weak but necessary activator of Tie2, whereas in the presence of Ang1, Ang2 inhibits Tie2 signaling.

Chemicals were purchased from Sigma-Aldrich unless otherwise specified. Ang2-specific neutralizing antibody, whose avidity and specificity for Ang2 have been previously validated 34 , is a gift from Amgen.

Anti-glyceraldehydephosphate dehydrogenase and p -tyrosine pTyro 4G10 antibodies were obtained from Chemicon Jaffrey, NH.

Salt Lake City, UT. Cells with fewer than 10 passages were used in the current study. HUVECs were cultured in full medium FM until confluent and then stimulated with Ang2 or Ang1 for 30 min with appropriate concentrations before cell lysates were prepared as described previously Tie2 and Tie1 phosphorylation levels were analyzed with immunoprecipitation IP -Western blotting as described previously Briefly, cell lysate of equal amounts of protein in 1 ml of radioimmunoprecipitation assay buffer were used for IP.

One hundred microliters of sTie2 2. The Ang2 or Ang1 captured by sTie2 was detected by sequential incubation of goat anti-Ang2 or goat anti-Ang1 primary antibodies, respectively, and horseradish peroxidase-conjugated anti-goat secondary antibody.

The absorbance was measured at nm and plotted against the concentrations of the ligands used to generate binding curves. HUVECs seeded 48 h earlier on six-well plates were subjected to a 5-mm-wide scratch in each well; the uniform width of each scratch was immediately confirmed by light microscopy.

Cells were left in FM for another 3 days, after which photomicrographs were taken to measure the widths of the remaining cell-free gaps.

Presented results are averaged across six assays per condition. The images of tubes formed were taken 24 h later.

Protein concentrations were measured using a bicinchoninic acid BCA assay Pierce, Rockford, IL , and fluorometric readings of caspase-3 and caspase-9 activities were adjusted by protein content.

Cell lysates were prepared using radioimmunoprecipitation assay buffer containing both protease and phosphatase inhibitors.

Total and phospho-Akt levels were analyzed by means of Western blotting, utilizing antibodies directed against total and phospho-specific Akt protein as described previously Means were compared either by using an unpaired Student t test or by one-way analysis of variance followed by a t test.

Similar data were also obtained when using human dermal microvascular ECs see Fig. S1 in the supplemental material.

We then performed binding studies for Ang2 and Ang1 with sTie2 using solid-phase binding assays as described in Materials and Methods.

To further demonstrate that Ang1 has a higher binding affinity for sTie2, competition binding assays of Ang1 and Ang2 with sTie2 were performed.

These data suggest that Ang2, compared with Ang1, binds to Tie2 with a lower affinity and that this may account for the weaker activation of the Tie2 receptor.

A Confluent HUVECs were stimulated with Ang2 and Ang1 at the indicated concentrations for 30 min, and cell lysates were prepared as described above and immunoprecipitated with Tie2.

After IP, Western blotting for phosphotyrosine and total Tie2 was performed. Representative blots of three independent experiments are depicted.

C Dose response for Ang1- and Ang2-mediated Tie2 phosphorylation. Shown is a representative blot. The Ang2 concentration in the h-conditioned medium was fold higher than that of Ang1 9, Since Ang-2 was the dominantly expressed Tie2 ligand in this system, we next used sTie2 to counteract the effect of secreted Ang2.

To eliminate the possibility of an artifact arising from sTie2 binding of undetected Ang1, we repeated the depletion experiment with a neutralizing antibody that binds Ang2 with 1,fold greater avidity than Ang1 After a 1-h incubation, we observed a dose-dependent reduction of pTie2 in those cells Fig.

The ability of this antibody to neutralize Ang2 but not Ang1 was confirmed using exogenous Ang2 see Fig. S2 in the supplemental material.

These data suggest that Ang2 secreted by ECs acts in an autocrine fashion to maintain basal Tie2 phosphorylation.

Endogenous Ang2 is an autocrine agonistic ligand of Tie2 in endothelial cells. Having observed by three methods that endogenous Ang2 is necessary for basal activation of Tie2 in ECs, we next studied the downstream consequences of this autocrine loop by focusing on the PI3K-Akt signal cascade, a major pathway for transducing the prosurvival and promigratory signals of Tie2 in ECs.

D Exogenous Ang2 induces Akt phosphorylation. HUVECs were stimulated with Ang2 at the indicated concentrations for 30 min, and phospho- and total Akt levels were compared.

Glyceraldehydephosphate dehydrogenase was used as a loading control. A similar pattern of changes was confirmed by measuring caspase-9 activity under these conditions Fig.

Caspase-3 A or caspase-9 B activity was measured using by using a fluorospectrophotometer as described in Materials and Methods.

Since Tie2 is known to mediate not only EC survival but also migration responses 1 , 3 , we tested the role of the autocrine Ang2 pathway in an in vitro migration assay.

A Forty-eight hours after HUVECs in six-well plates were transfected with NC, Ang, or Ang siRNA, a 5-mm-wide scratch was made in each well and cells were left in FM for another 3 days before the images of cells were taken to measure the width of the remaining cell-free band.

Having established the agonist activity of exogenous and endogenous Ang2 on Tie2 in ECs, we next tested whether this activity would be additive to the known agonist Ang1.

Similarly, Ang2 dose-dependently inhibited the Ang1-dependent activation of Akt Fig. Next, we wished to compare the protection conferred by Tie2 ligands alone or in combination against serum deprivation-induced apoptosis.

Our data indicate that Ang2 attenuates Ang1-induced Tie2 signaling and that Ang2 dose-dependently antagonizes Ang1-mediated protection from apoptosis.

A and B Ang2 antagonizes Ang1-induced Tie2 phosphorylation. C and D Ang2-antagonized Ang1 induced Akt phosphorylation.

Phospho- and total Akt were compared. E and F Ang2 or Ang1 alone attenuates serum deprivation-induced caspase-3 elevation. Our results strongly support the hypothesis that Ang2 can be either an agonist or an antagonist of the Tie2 receptor, depending upon the context.

Specifically, we found that cultured ECs respond to exogenous Ang2 alone by activating the Tie2 receptor.

Phenotypically, inhibition of this loop results in less resistance to apoptosis and a reduced migratory response. We asked how the agonistic effect of Ang2 compares to that of the more widely accepted naturally occurring Tie2 agonist, Ang1.

We found that Ang2 is a less potent activator of Tie2 and that it binds Tie2 with lower affinity than Ang1.

Either Ang1 or Ang2 can render ECs resistant to serum deprivation-induced apoptosis, but as expected, Ang1's effect is more potent. Finally, we explored what happens when Ang1 and Ang2 are applied together to ECs.

Rather than observing an additive stimulation of Tie2, we found that Ang2 inhibited Ang1-induced Tie2 activation and reduced Ang1-mediated protection against EC apoptosis in a dose-dependent fashion.

We conclude, therefore, that cultured ECs rely on self-produced Ang2 for trophic effects but that in the presence of the stronger Tie2 activator Ang1, Ang2 can actually dampen Tie2 signaling.

The original report describing Ang2 found that it was a naturally occurring antagonist of Tie2 in ECs In contrast, more-recent reports have shown that excess Ang2 can induce Tie2 activation 8 , 19 , 22 , In those studies, Ang2 was reported to promote capillary-like endothelial tube formation in three-dimensional culture systems.

While several groups have reported that exogenous Ang2 can activate Tie2, we also found that endogenous production of Ang2 is vital to the health of ECs.

ECs are known to synthesize, store, and secrete Ang2 but not Ang1 In addition, the levels of pTie2 in those cells show a close correlation with Ang2 levels in either culture medium or cell lysates data not shown.

Furthermore, such cells were markedly impaired in their ability to form tubes see Fig. S3 in the supplemental material. A similar situation arises in vivo in lymphatic vessels, where Ang1 is lacking due to the absence of periendothelial cells.

Two other groups have reported autocrine actions of Ang2 on ECs expressing Tie2 8 , However, the results are not directly comparable to ours for two reasons: On the other hand, Daly et al.

In comparing Ang1 and Ang2, we found that both ligands can activate Tie2 but that Ang2's signaling effect is less potent e. Though perhaps not the sole explanation, the lower binding affinity of Ang2 for Tie2 probably does contribute to its diminished potency at the receptor.

Mixing experiments did not show an additive effect on Tie2 activity but rather showed that Ang2 dose-dependently inhibited Ang1 signaling.

The reduction in Tie2 phosphorylation was biologically relevant, as evidenced by the progressive loss of Ang1-mediated protection from apoptosis as the Ang2 dose was increased.

The mixing study is consistent with the results reported for ECs from the original Ang2 article Finally, we found that addition of either Ang1 or Ang2 inhibits the binding of the other ligand to Tie2, suggesting competition between the angiopoietins for the same binding pocket on Tie2.

When excess Ang-2 is partially unseated by Ang1, Tie2 phosphorylation rises because Ang1 is the more potent agonist; when Ang1 is unseated by Ang2, Tie2 phosphorylation falls for the same reason.

Figure S4 in the supplemental material shows that depletion of endogenous Ang2 by two different siRNAs results in increased Ang1-dependent Tie2 phosphorylation.

This finding further supports our chief conclusion that Ang2 acts as a Tie2 antagonist when Ang1 is present.

Journal of Medical Genetics. Binding to a multifunctional docking site mediates cell survival and migration". Receptor tyrosine kinases EC 2.

Non-receptor tyrosine kinases EC 2. Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator.

EC number Enzyme superfamily Enzyme family List of enzymes. Molecular and Cellular Biology portal. Retrieved from " https: In those studies, Ang2 was reported to promote capillary-like endothelial tube formation in three-dimensional culture systems.

While several groups have reported that exogenous Ang2 can activate Tie2, we also found that endogenous production of Ang2 is vital to the health of ECs.

ECs are known to synthesize, store, and secrete Ang2 but not Ang1 In addition, the levels of pTie2 in those cells show a close correlation with Ang2 levels in either culture medium or cell lysates data not shown.

Furthermore, such cells were markedly impaired in their ability to form tubes see Fig. S3 in the supplemental material. A similar situation arises in vivo in lymphatic vessels, where Ang1 is lacking due to the absence of periendothelial cells.

Two other groups have reported autocrine actions of Ang2 on ECs expressing Tie2 8 , However, the results are not directly comparable to ours for two reasons: On the other hand, Daly et al.

In comparing Ang1 and Ang2, we found that both ligands can activate Tie2 but that Ang2's signaling effect is less potent e. Though perhaps not the sole explanation, the lower binding affinity of Ang2 for Tie2 probably does contribute to its diminished potency at the receptor.

Mixing experiments did not show an additive effect on Tie2 activity but rather showed that Ang2 dose-dependently inhibited Ang1 signaling.

The reduction in Tie2 phosphorylation was biologically relevant, as evidenced by the progressive loss of Ang1-mediated protection from apoptosis as the Ang2 dose was increased.

The mixing study is consistent with the results reported for ECs from the original Ang2 article Finally, we found that addition of either Ang1 or Ang2 inhibits the binding of the other ligand to Tie2, suggesting competition between the angiopoietins for the same binding pocket on Tie2.

When excess Ang-2 is partially unseated by Ang1, Tie2 phosphorylation rises because Ang1 is the more potent agonist; when Ang1 is unseated by Ang2, Tie2 phosphorylation falls for the same reason.

Figure S4 in the supplemental material shows that depletion of endogenous Ang2 by two different siRNAs results in increased Ang1-dependent Tie2 phosphorylation.

This finding further supports our chief conclusion that Ang2 acts as a Tie2 antagonist when Ang1 is present. Small-molecule partial agonists have been described for opioid, adrenergic, among others One non-G-protein-coupled-receptor example of partial agonist compounds is the selective estrogen receptor modulator tamoxifen 2.

However, we are aware of no other endogenous multiligand-single-receptor system that provides a precedent for the actions mediated by Ang2.

Others have repeatedly shown that Ang1 is highly multimerized in its native form whereas Ang2 is less aggregated 4 , The multimerization of Ang1 may account for its ability to strongly activate Tie2 Ang1 aggregates would theoretically have reduced entropy for binding Tie2 monomers, since the binding of any one Ang1 molecule to any one Tie2 favors the binding of additional noncovalently tethered Ang1 molecules to nearby Tie2 monomers.

In this way, Ang1 aggregates would favor the clustering and cross-phosphorylation of cell surface Tie2.

An excess of Ang2 in the presence of Ang1 could disrupt Ang1-Tie2 clusters and favor the formation of lower-order multimers—e.

In this fashion, Ang2 could antagonize Ang1 signaling. However, in a system devoid of Ang1, Ang2 would weakly activate Tie2.

This suggests not only that Ang2 is a lower-affinity binder of Tie2 with a less-potent phosphorylation effect at the receptor but that postreceptor signaling is also attenuated compared to Ang1.

While the reason for this is unclear and merits further investigation, several possibilities exist. First, our results do not exclude the possibility that Ang2 and Ang1 promote phosphorylation of different sets of tyrosine residues in the cytoplasmic tail of Tie2.

For example, tyrosine is required for the recruitment of the SH2-domain-containing p85 subunit of PI3K 21 , Interestingly, treatment with PI3K inhibitors only partially abrogates the Ang1-signaled migratory response 21 , suggesting the involvement of other tyrosines in this response, such as tyrosine , which may recruit Dok-R and activate intracellular GTPases that favor migration A second possibility is that the enhanced clustering of Tie2 monomers by Ang1 versus Ang2 may increase the cell surface localization of PI3K The enzymatic components of this cascade will tend to amplify small upstream differences as signals are transduced downstream, which could explain how a small difference in Tie2 activation leads to progressively larger differences in PI3K and Akt activation.

Last, Ang1 is known to have at least one non-Tie2 receptor 6 , 7. We cannot rule out that coreceptors on HUVECs are partly responsible for differences in signal transduction efficiency.

Ang1 is made primarily by periendothelial cells i. This is indeed the case in organs throughout the body 44 , In the Ang1-rich in vivo setting of blood vessels, local increases in Ang2 could precisely attenuate the tonic activity of Tie2.

The ability to carefully decrease Tie2 activation would be beneficial in certain settings—i. The finely tuned balance of endogenous Tie2 ligands may be upset in diseases like cancer and sepsis.

Solid tumors can strongly upregulate the production of Ang2, in part through the induction of hypoxia-inducible factors in the tumor cells 32 , 37 , Extra Ang2 may contribute to local downregulation of Tie2 activity.

In turn, this could enable the necessary destabilization of blood vessels that initiates tumor angiogenesis. In fact, a compound related to the Ang2 neutralizing antibody used in this report also possesses potent antiangiogenic and antitumor effects in murine xenograft models One implication of the present work is that reduction of circulating Ang2 e.

This study has several limitations. Our data suggesting an agonist role for Ang2 are derived from in vitro studies in which Ang1 expression was absent or barely detectable.

Future studies using coculture of ECs with vascular smooth muscle cells or an endothelial cell-specific knockout of Ang2 in mice should further clarify the role of Ang2 in the maintenance of vascular homeostasis.

Second, the biochemistry underlying the ability of a ligand to act as both an agonist and an antagonist merits further investigation.

Third, additional cell biological responses in Ang1-Ang2 mixing experiments should be measured, such as changes in monolayer permeability or surface expression of inflammatory adhesion molecules.

Related to this, Ang1 and Ang2 may activate distinct postreceptor signaling pathways within ECs.

Finally, coreceptors or other angiopoietin receptors, such as Tie1, may be involved in the modulation of signals through Tie2 In conclusion, using one model system, we have found that Ang2 can act as either a weak Tie2 agonist or a dose-dependent Tie2 antagonist.

Ang2 is an agonist only in the absence of Ang1, and Ang1-deprived ECs rely on autocrine Ang2 stimulation for cell survival and an appropriate migratory response.

Ang2 binds Tie2 with less affinity than Ang1, and the latter is a more potent activator of Tie2. When they are combined, Ang2 inhibits Ang1 signaling and downstream effects, thus becoming an antagonist.

These findings help reconcile divergent reports on the biological actions of Ang2 and have significant implications for the design of therapies targeted to the angiopoietin-Tie2 pathway.

National Center for Biotechnology Information , U. Journal List Mol Cell Biol v. Published online Feb Ananth Karumanchi , and Samir M.

Author information Article notes Copyright and License information Disclaimer. This article has been corrected. See Mol Cell Biol.

This article has been cited by other articles in PMC. Abstract Angiopoietin 2 Ang2 was originally shown to be a competitive antagonist for Ang1 of the receptor tyrosine kinase Tie2 in endothelial cells ECs.

Tie2 and Tie1 phosphorylation assay. Binding assays of Ang2 or Ang1 with Tie2 receptor. This provides new insight into the highly metastatic phenotype of OSCC.

While further studies are needed to study Tie2, the current data suggested that Tie2 plays an important role in cellular adhesion and invasion and may be a potential biomarker for OSCCs.

The endothelial-specific receptor, tyrosine kinase with immunoglobulin-like loops and epidermal growth factor homology domains-2; OSCCs: Charters for editing this manuscript.

The authors received no financial support. Schnurch H, Risau W. Expression of tie-2, a member of a novel family of receptor tyrosine kinases, in the endothelial cell lineage.

Distinct rat genes with related profiles of expression define a TIE receptor tyrosine kinase family. Distinct roles of the receptor tyrosine kinases Tie-1 and Tie-2 in blood vessel formation.

Angiopoietin-1 requires p RhoGAP to protect against vascular leakage in vivo. Signaling and functions of angiopoietin-1 in vascular protection.

Angiopoietin-1 decreases plasma leakage by reducing number and size of endothelial gaps in venules. Angiopoietin-1 is an antipermeability and anti-inflammatory agent in vitro and targets cell junctions.

Vascular-specific growth factors and blood vessel formation. Functional significance of Tie2 signaling in the adult vasculature.

Recent Prog Horm Res. Tie2 expression and phosphorylation in angiogenic and quiescent adult tissues. Analysis of Tie receptor tyrosine kinase in haemopoietic progenitor and leukaemia cells.

Expressions and clinical significances of angiopoietin-1, -2 and Tie2 in human gastric cancer. Biochem Biophys Res Commun.

Absence of endothelial cells, central necrosis, and fibrosis are associated with aggressive inflammatory breast cancer. Tie-2 and angiopoietin-1 expression in human thyroid tumors.

Expression of the receptor tyrosine kinase Tie2 in neoplastic glial cells is associated with integrin beta1-dependent adhesion to the extracellular matrix.

Molecular cloning and characterization of mouse TIE and TEK receptor tyrosine kinase genes and their expression in hematopoietic stem cells.

Expression status of Zic family member 2 as a prognostic marker for oral squamous cell carcinoma. J Cancer Res Clin Oncol. Galectin-9 as a regulator of cellular adhesion in human oral squamous cell carcinoma cell lines.

Int J Mol Med. Kinesin family member 4A: Overexpression of cell cycle regulator CDCA3 promotes oral cancer progression by enhancing cell proliferation with prevention of G1 phase arrest.

Cavin-2 in oral cancer: A potential predictor for tumor progression. Loss of KAI1 expression in the progression of colorectal cancer. Aberrant expression of RAB1A in human tongue cancer.

A potential key component in human oral cancer progression through the RET receptor tyrosine kinase-mitogen-activated protein kinase signaling pathway.

Decreased expression of kallikrein-related peptidase Glutamate acid decarboxylase 1 promotes metastasis of human oral cancer by beta-catenin translocation and MMP7 activation.

Overexpression of stathmin in oral squamous-cell carcinoma: Control of vascular morphogenesis and homeostasis through the angiopoietin-Tie system.

Nat Rev Mol Cell Biol. Angiopoietin-1 overexpression modulates vascular endothelium to facilitate tumor cell dissemination and metastasis establishment.

Dominant-negative and targeted null mutations in the endothelial receptor tyrosine kinase, tek, reveal a critical role in vasculogenesis of the embryo.

Requisite role of angiopoietin-1, a ligand for the TIE2 receptor, during embryonic angiogenesis. Tie-1 and tie-2 define another class of putative receptor tyrosine kinase genes expressed in early embryonic vascular system.

Tie2 signaling regulates osteoclastogenesis and osteolytic bone invasion of breast cancer. Tie2 vascular endothelial receptor expression and function in hepatocellular carcinoma.

Jamora C, Fuchs E. Intercellular adhesion, signalling and the cytoskeleton. Lack of plakophilin 1 increases keratinocyte migration and reduces desmosome stability.

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