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Validated All-in-One™ qPCR Primer for ILK(NM_004517.3) Search again
Product ID:
HQP053997
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
HEL-S-28, ILK-1, ILK-2, P59, p59ILK
Gene Description:
integrin linked kinase
Target Gene Accession:
NM_004517.3(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Summary
Transduction of extracellular matrix signals through integrins influences intracellular and extracellular functions, and appears to require interaction of integrin cytoplasmic domains with cellular proteins. Integrin-linked kinase (ILK), interacts with the cytoplasmic domain of beta-1 integrin. This gene encodes a serine/threonine protein kinase with 4 ankyrin-like repeats, which associates with the cytoplasmic domain of beta integrins and acts as a proximal receptor kinase regulating integrin-mediated signal transduction. Multiple alternatively spliced transcript variants encoding the same protein have been found for this gene. [provided by RefSeq].
Gene References into function
- Role of integrin-linked kinase in leukocyte recruitment
- Integrin-linked kinase phosphorylates the myosin phosphatase target subunit at the inhibitory site in platelet cytoskeleton.
- Ionizing radiation strongly induced the expression of functional beta1-integrin and ILK in the two lung cancer cell lines, A549 and SKMES1.
- Integrin-linked kinase transiently associates with and phosphorylates beta3 in a PI3-kinase dependent manner
- Ganglioside loss promotes survival primarily by activating integrin-linked kinase/Akt without phosphoinositide 3-OH kinase signaling.
- the ILK-affixin complex has a role in integrin-cytoskeleton linkage during platelet aggregation
- Assembly of the PINCH-ILK-CH-ILKBP complex precedes and is essential for localization of each component to cell-matrix adhesion sites
- role in alpha(v)integrin in regulating cell proliferation in ovarian cancer cells
- Cells that are depleted of this enzyme undergo extensive apoptosis.
- role in protein kinase B/Akt activation.
- Overexpression of integrin-linked kinase is associated with sporadic human colon cancer
- Cell adhesion to the extracellular matrix protein fibronectin modulates radiation-dependent G2 phase arrest and involve this enzyme in vitro.
- ILK has a role in oncogenic transformation and progression to invasive and metastatic phenotypes [review]
- ILK is a critical mediator for tubular EMT and likely plays a crucial role in the pathogenesis of chronic renal fibrosis
- ILK kinase activity, or expression, results in the inhibition of cell attachment, cell migration, F-actin organization
- PINCH1 and ILK are essential for prompt cell spreading and motility; PINCH1 and ILK, like alpha-parvin, are crucial for cell survival; PINCH1 and ILK are required for optimal activating phosphorylation of PKB/Akt of the survival pathway
- Increased expression of integrin-linked kinase is correlated with melanoma progression
- integrin-lined kinase plays an important role in vascular morphogenesis
- essential role of ILK in two key aspects of tumor angiogenesis: VEGF expression by tumor cells and VEGF-stimulated blood vessel formation
- Taken together, these data suggest that PI3K-ILK-Akt pathway that is independent of the TGFbeta-induced Smad pathway is required for TGFbeta-mediated epithelial to mesenchymal transition.
- 59 kDa immunoreactive integrin-linked kinase is upreguated in the blood and peritoneal fluid of ovarian cancer patients before, but not after chemotherapy
- ILK regulates alpha 2 beta 1 in HEL cells, is activated in platelets and associates with beta 1-integrins
- Data provide evidence that ILK signaling modulates the cellular radiation response involving diverse signaling pathways and through changes in f-actin-based processes such as focal adhesion formation, cell adhesion, and spreading.
- loss of ParvB expression is a novel mechanism for upregulating ILK activity in tumors
- ILK overexpression protects vascular endothelium cells and progenitor cells from anchorage- or nutrient-deprived stress and enhances neovascularization
- Finding suggests that therapies directed against ILK and its downstream signaling targets may have the potential to enhance the efficacy of gemcitabine-based chemotherapy.
- Dissociation of ILK from Hsp90 shortened its half-life by promoting proteasome-dependent degradation
- matrix-derived mechanical forces sensed by beta1 integrin are capable of modulating ILK activity which regulates fibroblast viability via an Akt-dependent mechanism
- Strong expression of ILK in cancerous tissues is involved with aggressive capability in pancreatic cancer.
- ILK is a critical effector in a signaling pathway necessary for granule cell proliferation and cerebellar development.
- ILK may act as a pro-survival factor and play a role in protecting mesangial cells from hyperglycaemic osmotic stress
- functions as a downstream mediator of the ET-1/ET(A)R axis to potentiate aggressive cellular behavior in ovarian cancer cells.
- ILK activity can modulate acute Wnt3a mediated beta-catenin phosphorylation, stabilization and nuclear activation in a PI3K-independent manner.
- Endogenous ILK is a novel and physiological upstream responder of numerous intracellular molecules involved in hypoxic stress in endothelial cellss and may control the recruitment of peogenitor cells to ischemic tissue.
- Review highlights the role of integrin-linked kinase (ILK) as a novel component of the cardiac mechanical stretch sensor.
- R-Ras and ILK have roles upstream of GSK-3beta in the regulation of neuronal polarity
- Identification of ILK as a player in hypoxia survival signaling employed by cancer cells further validates ILK as a unique target for cancer therapy.
- This study suggests that ILK serves as a key mediator in TGFbeta1 regulation of uPA/PAI-1 system critical for the invasiveness of human ovarian cancer cells. And ILK is a potential target for cancer therapy.
- Downregulation of either FAK or ILK expression inhibited SPARC-mediated AKT phosphorylation, and targeting both FAK and ILK attenuated AKT activation more potently than targeting either FAK or ILK alone
- findings show integrin-linked kinase activity is indispensable for streptococcal M1-induced paxillin recruitment and phosphorylation
- ILK transfection can support cell survival in the absence of matrix interactions and enable fundamental studies of three-dimensional cell function in response to extrinsic signals, independently of matrix-ligand interactions.
- ILK is a substrate for p21-activated kinase 1 (PAK1); mutation of PAK1 phosphorylation sites on ILK to alanine reduces cell motility and cell proliferation.
- PI3K/ILK/Akt/NF-kappaB axis is a promising target for therapeutic intervention in renal cell carcinoma.
- Connective tissue growth factor (CTFG) induces the expression of integrin-linked kinase (ILK) protein in HK-2 cells
- ILK may provide a linkage between kAE1 and the underlying actin cytoskeleton to stabilize kAE1 at the basolateral membrane, resulting in higher levels of cell surface expression
- Occurrence of ILK expression with lens epithelial cells differentiation is consistent with positive regulatory function of ILK, revealed in a model of epithelial-mesenchymal transition in vitro.
- ILK knockdown decreased the invasion ability of melanoma cells and the formation of anchorage-independent colonies in soft agar
- A mutation (785C>T [Ala262Val]) is associated with loss of endothelial cells & cardiac dysfunction. It negatively affects cardiac mechanosensation. ILK maintains embryonic cardiomyocyte shape and ventricle morphology.
- PINCH-1, through its interaction with integrin-linked kinase, plays important role in regulating TGF-beta1-mediated epithelial-to-mesenchymal transition and could be potential future therapeutic target to prevent progression of renal disease.
- ILK mediated the effect of epithelial to mesenchymal transition in proximal tubular epithelial cells stimulated by CTGF
- tPA induces LRP-1 tyrosine phosphorylation, which in turn facilitates the LRP-1-mediated recruitment of beta1 integrin and downstream ILK signaling, thereby leading to myofibroblast activation.
- Regulation of cell-matrix contacts and beta-catenin signaling in vascular smooth muscle by integrin-linked kinase: implications for intimal thickening.
- ILK expression does not appear to have a role in predicting outcome in patients with resected Hepatocellular cancer
- a new signaling connection from ILK to cofilin for dynamic actin polymerization during cell adhesion, depending on the activity of ILK-associated c-Src.
- These data demonstrate a critical and unexpected function for ILK in the organization of centrosomal protein complexes during mitotic spindle assembly and DNA segregation
- 25 ILK-interacting proteins were identified in immunoprecipitates, and when ILK is complexed with tubulin and RuvB-like 1, alpha-parvin and PINCH are not present, suggesting that ILK has the ability to form distinct protein complexes throughout the cell.
- Both integrins, v3 and v5, are involved in the glioma cell radioresistance through the integrin-linked kinase (ILK) and the small GTPase RhoB, at least by regulating the radiation-induced mitotic cell death.
- Elevated levels of ILK are associated with cellular differentiation in high turnover tissues but not generally with a malignant phenotype. ILK is not a general molecular target for cancer therapy but rather an indicator of differentiation.
- These studies demonstrate the importance for keratinocyte proliferation of ILK regulation through changes in its subcellular localization, and establish ILKAP and CRM1 as pivotal modulators of ILK subcellular distribution and activity in these cells.
- ILK silencing inhibited binding of PARP-1 to SIRE
- ILK expression may be implicated in human laryngeal carcinoma and its localization in the nucleus possibly proposes novel nuclear functions of this molecule
- These data extend current knowledge about the role of ILK in endothelial progenitor cells biology and implicate ILK as a therapeutic target in coronary artery disease.
- ILK overexpression during liver oncogenesis and cirrhosis correlates with activation of Akt but not with other conventional ILK targets
- zincs are coordinated by PINCH1 LIM1, and suggests that conformational flexibility and twisting between the 2 zinc fingers within the LIM1 domain may be important for ILK binding.
- EphA1 regulates cell morphology and motility through the ILK-RhoA-ROCK pathway.
- pneumococci exploit the vitronectin-alphavbeta3-integrin complex as a cellular receptor for invasion and this integrin-mediated internalization requires the cooperation between the host signalling molecules ILK, PI3K and Akt.
- Fish oil inhibits ILK expression thereby inhibiting non-small cell lung carcinoma growth in a cell line.