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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. dans The EMBO journal 2013
Targeted knockdown of the integrin focal adhesion complex components beta-integrin, PINCH (Montrer LIMS1 Protéines), and integrin-linked kinase caused formation of multinucleate epidermal cells within the Drosophila larval epidermis.
PINCH (Montrer LIMS1 Protéines) 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.
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 (Montrer POSTN Protéines) activation of signaling pathways involved in cyst growth and fibrosis in PKD (Montrer PRKD1 Protéines).
Ilk and ELMO2 (Montrer ELMO2 Protéines) modulate recycling endosomes in keratinocytes undergoing intercellular adhesion mediated through cell-cell contacts, including E-cadherin (Montrer CDH1 Protéines)-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 (Montrer SLC2A4 Protéines), which results in reduced peripheral insulin (Montrer INS Protéines) sensitivity and glucose uptake, suggesting ILK as a molecular target and a prognostic biomarker of insulin (Montrer INS Protéines) resistance.
results demonstrate that TGF-beta1 (Montrer TGFB1 Protéines)-induced autophagy links beta-catenin (Montrer CTNNB1 Protéines) and Smad (Montrer SMAD1 Protéines) signaling to promote epithelial-mesenchymal transition in C1.1 cells through a novel pY654-beta-catenin (Montrer CTNNB1 Protéines)/p-Smad2 (Montrer SMAD2 Protéines)/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 (Montrer NOS2 Protéines)-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 (Montrer INS Protéines) action in lean mice but sensitizes the liver to insulin (Montrer INS Protéines) during the challenge of high fat feeding. This effect corresponds to changes in the expression and activation of key insulin (Montrer INS Protéines) signaling pathways as well as a greater capacity for hepatic mitochondrial glucose oxidation.
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.
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 (Montrer PIK3CA Protéines)/Akt (Montrer AKT1 Protéines) pathway.
ILK-induced epithelial-mesenchymal transition is a novel mechanism in the pathogenesis of adenomyosis
Herein, we propose a new ILK-MMP9 (Montrer MMP9 Protéines)-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 (Montrer MMP14 Protéines) as an additional ILK substrate and show that modulation of ILK expression and activity inhibit MT1-MMP (Montrer MMP14 Protéines)-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 (Montrer EMILIN1 Protéines) and ILK as prospective markers of islet regenerative function in human mesenchymal stem cells.
ILK aids trophoblast syncytialization via downregulation of CDH1 (Montrer CDH1 Protéines), perhaps through an ILK-PARP1 (Montrer PARP1 Protéines)-SNAI1 (Montrer SNAI1 Protéines) pathway
Emodin inhibits the migration and invasion abilities of human endometrial stromal cells by by facilitating the mesenchymal-epithelial transition through targeting integrin-linked kinase.
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 (Montrer PFN1 Protéines)-dependent dissociation of G-actin (Montrer ACTB Protéines)-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