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Human ILK Protein expressed in HEK-293 Cells - ABIN2723535
Radovanac, Morgner, Schulz, Blumbach, Patterson, Geiger, Mann, Krieg, Eckes, Fässler, Wickström: Stabilization of integrin-linked kinase by the Hsp90-CHIP axis impacts cellular force generation, migration and the fibrotic response. in The EMBO journal 2013
Targeted knockdown of the integrin focal adhesion complex components beta-integrin, PINCH, and integrin-linked kinase caused formation of multinucleate epidermal cells within the Drosophila larval epidermis.
PINCH and ILK have an independent capacity to localize at muscle attachment sites in vivo.
ILK functions as an essential hub in the assembly of its partner proteins at sites of integrin adhesion.
XeILK plays an essential role in morphogenetic movements during gastrulation
ILK is required for maintaining hepatic transcriptional and metabolic programs that sustain oxidative metabolism, which are required for hepatic maintenance of glucose homeostasis.
ILK has a critical role in renal-stromal and vascular development, as well as a noncell autonomous role of in ureteric bud branching morphogenesis.
Integrin-linked kinase regulates p38 MAPK-dependent cell cycle arrest in ureteric bud development.
Lipoxin A4 and its analog suppress hepatocarcinoma cell epithelial-mesenchymal transition, migration and metastasis via regulating integrin-linked kinase axis.
Depletion of integrin-linked kinase (ILK) in the pancreatic epithelial cells results in glucose intolerance due to a loss of the intra-islet vasculature. In turn, blood vessels accumulate at the islet periphery.
these data demonstrate the importance of integrin-mediated cell-matrix interactions and ILK signaling in osteoprogenitors in the control of osteoblast functioning during juvenile bone mass acquisition and adult bone remodeling and homeostasis.
We conclude that ILK is critical for maintaining the collecting duct epithelium and renal function and is a key intermediate for periostin activation of signaling pathways involved in cyst growth and fibrosis in PKD.
Ilk and ELMO2 modulate recycling endosomes in keratinocytes undergoing intercellular adhesion mediated through cell-cell contacts, including E-cadherin-based adherens junctions.
Ilk regulates cellular mechanics facilitating the motility in 3D extracellular matrices.
It was concluded that ILK depletion modifies the transcription of GLUT4, which results in reduced peripheral insulin sensitivity and glucose uptake, suggesting ILK as a molecular target and a prognostic biomarker of insulin resistance.
results demonstrate that TGF-beta1-induced autophagy links beta-catenin and Smad signaling to promote epithelial-mesenchymal transition in C1.1 cells through a novel pY654-beta-catenin/p-Smad2/ILK pathway.
ILK deletion impaired the developmental profile, proliferation, and differentiation of oligodendrocyte precursor cells.
Our results define ILK as a key mechanotransducer in modulating breast cancer stem-like cells development in response to tissue mechanics and oxygen tension.
iNOS-derived NO plays a crucial role during atherosclerosis by regulating the endocytic-lysosomal degradation of ILK in endothelial cells.
Hepatic ILK deletion has no effect on insulin action in lean mice but sensitizes the liver to insulin during the challenge of high fat feeding. This effect corresponds to changes in the expression and activation of key insulin signaling pathways as well as a greater capacity for hepatic mitochondrial glucose oxidation.
this study has identified a new role for Parvin and alphaPix downstream of the integrin-ILK signaling axis for mammary epithelial cell differentiation.
Work provides a new tool for studying mouse oligodendrocyte precursor cell migration and highlights the role of integrin-linked kinase in its regulation on extracellular matrix proteins relevant to multiple sclerosis.
We conclude that ILK negatively and independently of PI3K regulated MEF2C phosphorylation activity and MCK mRNA expression in C2C12 cells
high extracellular concentration of phosphate induced senescence in cultured smooth muscle through the activation of IGF-1 receptor and ILK overexpression
This study demonstrates a role for ILK in regulating laminin2-mediated adhesion and Ln-2-independent growth cone size/activity in oligodendrocyte
Using the ILK deficient zebrafish heart failure mutant main squeeze (msq), which shows reduced PKB phosphorylation and thereby impaired cardiac contractile force, we identified here, in an automated small compound screen, the protein phosphatase inhibitors calyculin A and okadaic acid significantly restoring myocardial contractile function by reconstituting PKB phosphorylation in msq ILK-deficient zebrafish embryos.
Heart failure in recessive embryonic lethal zebrafish mutant main squeeze (msq) mutants is due to a mutation in the integrin-linked kinase (ilk) gene.
The lost-contact mutant on chromosome 10 encodes a nonsense mutation (Y319X) associated with defective cardiomyocytes & endothelial cells that leads to severe myocardial dysfunction. There is epistatic regulation between laminin-alpha4, integrin, & Ilk.
Data show that integrin-linked kinase is an essential component downstream of laminin and integrin alpha7, providing strengthening of skeletal muscle fibre adhesion with the extracellular matrix.
Data indicate that ILK facilitates mechanosensitive VEGFR3 signaling and physiologic lymph vessel expansion by controlling beta1 integrin-mediated VEGFR3 activation.
The expression of ILK was significantly correlated with differentiation and metastasis of the laryngeal carcinomas. The inhibition of the ILK gene could downregulate the proliferation, migration and invasion of Hep-2 human laryngeal squamous cell carcinoma cells. Data suggested that ILK acts as an oncogene in laryngeal squamous cell carcinoma.
findings provide genetic and functional evidence that ILK is a cardiomyopathy disease gene and highlight its relevance for diagnosis and genetic counseling of inherited cardiomyopathies
Results found that ILK was highly expressed in EGFR-mutation positive non-small cell lung cancer and an independent poor prognostic factor for the progression-free survival of the patients.
Study found that both SDPR and ILK regulate the expression of ALDH1 in endometrioid carcinoma. Further results revealed that the localization of ILK at the cell cortex was disrupted by SDPR knockout, potentially interfering with ILK signaling.
high expression enhanced the migration and invasion abilities of endometrial stromal cells by facilitating the epithelial-mesenchymal transition; crucial role in the pathogenesis of endometriosis
epithelial mesenchymal transition significantly contributes to phyllodes tumor pathogenesis and implicates ILK and ZEB1 in phyllodes tumors malignant phenotype
By recruiting focal adhesions adaptors PINCH and Parvin into a heterotrimeric complex, integrin linked kinase (ILK) triggers F-actin filament bundling, generating a force/mechanical signal to promote cytoskeleton reassembly and dynamic cell adhesion. The process is sensitized to Mg-ATP bound to the pseudoactive site of ILK and its dysregulation severely impairs stress fibers formation, cell spreading, and migration.
Using molecular modeling and molecular dynamics simulations, we show that Asp344, Asp352, and Thr356 in kindlin-2 and Arg243 and Arg334 in ILK kinase domain (KD) are important in kindlin-2/ILK complex formation. Mutations that disrupt these interactions abrogate kindlin-2 and ILK colocalization in HeLa cells.
High ILK expression is associated with Neuroblastoma.
We further performed molecular dynamics simulation for 100ns to see the effect of urea on structural stability of kinase domain of ILK at atomic level. Structural changes with increasing concentrations of urea were analysed, and we observed a significant increase in the root mean square deviation, root mean square fluctuations, solvent accessible surface area and radius of gyration
ILK overexpression in human CRC associates with EMT and CSC traits, contributing to tumor progression and chemoresistance.
Dermal fibroblast-to-myofibroblast transition sustained by alphavss3 integrin-ILK-Snail1/Slug signaling is a common feature for hypermobile Ehlers-Danlos syndrome and hypermobility spectrum disorders.
These results indicated that ILK promoted cell proliferation and growth in breast cancer cells through activation of the PI3K/Akt pathway.
ILK-induced epithelial-mesenchymal transition is a novel mechanism in the pathogenesis of adenomyosis
Herein, we propose a new ILK-MMP9-MRTF axis that appears to be critical for endothelial-mesenchymal transition differentiation of endothelial to cancer-associated fibroblasts -like cells. Thus, it might be an attractive target for cancer treatment
The current data support MT1-MMP as an additional ILK substrate and show that modulation of ILK expression and activity inhibit MT1-MMP-related pro-metastatic behaviors of ovarian cancer cells.
Results show that ILK is overexpressed in metastasis of bladder cancer and the up-regulation of ILK could increase cell proliferation, change cell morphology and regulate cell cycle promoting epithelial-mesenchymal transition.
This study is the first to identify EMILIN-1 and ILK as prospective markers of islet regenerative function in human mesenchymal stem cells.
Integrin-linked kinase (ILK, MGC129022) is an important regulator of the endothelial phenotype and vascular network formation by directing the assembly and/or maturation of alpha5beta1-competent matrix-forming adhesions.
Rac1 only partially restores the spreading defects of integrin linked kinasse (ILK)-depleted cells, suggesting that an additional ILK-dependent signal is required for cell spreading.
Profilin-dependent dissociation of G-actin-Tbeta4 complexes simultaneously liberates actin for filament assembly and facilitates Tbeta4 binding to integrin-linked kinase (ILK) in the lamellipodia.
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.
, Integrin-linked kinase
, integrin linked kinase
, integrin-linked protein kinase
, integrin-linked kinase
, Integrin-linked protein kinase
, integrin binding protein kinase
, main squeeze
, beta-integrin-linked kinase
, 59 kDa serine/threonine-protein kinase
, integrin-linked kinase-2