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Expression of a non-phosphorylatable mutant of the Tie1 juxtamembrane domain threonine site (T794A) significantly disrupted vascular development, resulting in fish with stunted and (show TEK Proteins)poorly branched intersomitic vessels.
Tie-1 and Tie-2 (show TEK Proteins) are not required for early heart development, yet they have redundant roles for the maintenance of endocardial-myocardial connection in later stages.
A natural antisense transcript was identified for tyrosine kinase containing immunoglobulin and epidermal growth factor (show EGF Proteins) homology domain-1 (tie-1), tie-1AS long noncoding RNA in zebrafish, mouse, and humans.
Tie1 directly interacts with Tie2 to promote ANG-induced vascular responses under noninflammatory conditions, whereas in inflammation, Tie1 cleavage contributes to loss of ANG2 agonist activity and vascular stability
Ang (show ANG Proteins),Tie1 and Tie2 (show TEK Proteins) play roles in vascular development and pathogenesis of vascular diseases.[review]
In vitro binding assays with purified components reveal that Tie-integrin recognition is direct, and further demonstrate that the receptor binding domain of the Tie2 ligand (show ANGPT2 Proteins) Ang-1 (show ANGPT1 Proteins), but not the receptor binding domain of Ang-2 (show ANGPT2 Proteins), can independently associate with a5b1 or aVb3. cooperative Tie/integrin interactions selectively stimulate ERK/MAPK (show MAPK1 Proteins) signaling in the presence of both Ang-1 (show ANGPT1 Proteins) and fibronectin (show FN1 Proteins)
The inhibition of Tie-2 (show TEK Proteins) exerted by Tie-1can be relieved by Tie-1 ectodomain cleavage mediated by tumor- and inflammatory-related factors, which causes destabilization of vessels and initiates vessel remodeling in cancer. (Review)
T794A-expressing human umbilical vein endothelial cells formed significantly shorter tubes with fewer branches in three-dimensional Matrigel cultures, but did not alter Tie1 or Tie2 (show TEK Proteins) tyrosine phosphorylation or downstream signaling.
The decreasing expression of Tie1 may play an important role in the pathogenesis of primary lower extremity varicose veins.
Data propose that EndMT associated with Tie1 downregulation participates in the pathological development of stroma observed in tumours.
the effects of factors activating ectodomain cleavage on both Tie1 and Tie2 (show TEK Proteins) within the same population of cells, and their impact on angiopoietin signalling
these results suggest that the expression level of Tie1 and its physical interaction with Tie2 defines whether Ang2 functions as a Tie2 agonist or antagonist, thereby determining the context-dependent differential endothelial sensitivity to Ang2.
The Tie-1 immunoreactivity was dominantly observed in the heamangiogenic cells and cells cords, whereas the matured villi showed immunoreactivity only in other components.
Data support an interactive model of Tie1 and Tie2 (show TEK Proteins) function, in which dynamically regulated Tie1 versus Tie2 (show TEK Proteins) expression determines the net positive or negative effect of Tie1 on Tie2 (show TEK Proteins) signaling.
Data indicate that receptor tyrosine kinase (show ERBB3 Proteins) Tie1 deletion resulted in lack of lymphatic valves and collecting vessel defects.
In contrast to the important role of Tie2 (show TEK Proteins) in the regulation of blood vascular development, Tie1 is crucial in the process of lymphatic remodeling and maturation, which is independent of Tie2 (show TEK Proteins).
Tie1 regulates tumor angiogenesis, postnatal sprouting angiogenesis, and endothelial cell survival, which are controlled by VEGF (show VEGFA Proteins), Angpt, and Notch (show NOTCH1 Proteins) signals
Shear stress conditions that modulate atherogenic events also regulate Tie1 expression. Therefore, Tie1 may play a novel proinflammatory role in atherosclerosis.
Developing lymphatic vasculature is particularly sensitive to alterations in Tie1 expression in mice.
Loss of Tie1 results in lymphatic vascular abnormalities that precede the blood vessel phenotype, suggesting that Tie1 is involved in lymphangiogenesis.
A natural antisense transcript was identified for tyrosine kinase (show TYRO3 Proteins) containing immunoglobulin and epidermal growth factor (show EGF Proteins) homology domain-1 (tie-1), tie-1AS long noncoding RNA in zebrafish, mouse, and humans.
In the lung, Tie1 expression increases prior to birth and rises in the newborn animal, a pattern not found in other organs.
Blood vessel homeostasis and endothelial cell survival depend on proper signalling through angiopoietin receptors such as the receptor tyrosine kinases Tie-1 and Tie-2 (show TEK Proteins). Tie-1 and Tie-2 (show TEK Proteins) localized to motile cilia of the oviduct.
This gene encodes a member of the tyrosine protein kinase family. The encoded protein plays a critical role in angiogenesis and blood vessel stability by inhibiting angiopoietin 1 signaling through the endothelial receptor tyrosine kinase Tie2. Ectodomain cleavage of the encoded protein relieves inhibition of Tie2 and is mediated by multiple factors including vascular endothelial growth factor. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene.
tyrosine-protein kinase receptor Tie-1
, tyrosine kinase with immunoglobulin and epidermal growth factor homology domains 1
, tyrosine kinase with immunoglobulin and epidermal growth factor homology domains
, tyrosine kinase receptor 1