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Kindlins are a small family of proteins that mediate protein-protein interactions involved in integrin activation and thereby have a role in cell adhesion, migration, differentiation, and proliferation. Additionally we are shipping FERMT3 Antibodies (76) and FERMT3 Proteins (3) and many more products for this protein.
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Structure and lipid-binding properties of the kindlin-3 pleckstrin homology domain has been reported.
Mice expressing as little as 5% of kindlin-3 were viable and protected from spontaneous bleeding and infections. In vitro platelet functions, leukocyte adhesion, extravasation, and bacterial clearance were diminished. Bleeding time increased.
The accumulation of HSPCs in the circulation of leukocyte adhesion deficiency type III patients, who lack Kindlin-3, underlines the conserved functions of Kindlin-3 in man and the importance of our findings for human disease.
Optimal T cell activation and B cell antibody responses in vivo require the interaction between Integrin beta2 and kindlin-3.
Direct binding of kindlin-3 to integrin alphaIIbbeta3 is involved in supporting integrin alphaIIbbeta3 activation and integrin alphaIIbbeta3-dependent responses of platelets and consequently contributes significantly to arterial thrombus formation.
ADAP interacts with talin and kindlin-3 to promote platelet Integrin alphaIIbbeta3 activation and stable fibrinogen binding.
the requirement of Kindlin-3 for effector T cells to induce alpha4beta1 and alphaLbeta2 integrin ligand binding and stabilization of integrin-ligand bonds is critical when integrin ligand levels are low, but of less importance when integrin ligand levels are high.
This is the first in vivo demonstration that Kindlin-3-stabilized integrin adhesions, although essential for lymphocyte arrest on blood vessels and interstitial motility, are not obligatory for leukocyte diapedesis.
the beta-2-integrin-kindlin-3 interaction is particularly important in adhesion strengthening under shear flow, and for T-cell homing to lymph nodes, but dispensable for T cell activation which occurs in a shear-free environment
Kindlin-3 is central to conversion of mechanical force to intracellular signaling via calcium influx.
FERMT3 regulates glioma cell activity through integrin-mediated Wnt (show WNT2 ELISA Kits)/beta-catenin (show CTNNB1 ELISA Kits) signaling.
this case report describes a female Thai patient who was diagnosed with leukocyte adhesion deficiency type III with a novel mutation in FERMT3, presenting with a humoral immune defect
kindlin-3 plays an important role in maintaining a proper conformation of the resting alpha4beta1 to mediate both rolling and firm cell adhesion
Kindlin-3 regulates c-Myc (show MYC ELISA Kits) protein expression in the human chronic myeloid leukemia (show BCL11A ELISA Kits) cell line K562.
NMR studies demonstrated that the F1 loop of kindlin-3 is globally unfolded but stretches of residues assuming transient helical conformations could be detected in aqueous solution.
Suppression of the Kindlin-2 (show FERMT2 ELISA Kits)-integrin beta1-AKT (show AKT1 ELISA Kits) regulatory axis is an alternative mechanism underlying the tumor suppressor function of miR (show MLXIP ELISA Kits)-200b in esophageal squamous cell carcinoma.
Kindlin-3/FERMT3 is upregulated in atherosclerotic, mainly in cells of monocytic origin and of M2 type. Simultaneous upregulation of ITGB2 (show ITGB2 ELISA Kits) suggests a synergistic effect on leukocyte adherence and transmigration into the vessel wall.
A new C>T point mutation was found in exon 13 in the FERMT3 gene in an infant diagnosed with LAD (show DLD ELISA Kits)-III. KINDLIN-3 expression is required for platelet aggregation and leukocyte function, but also osteoclast-mediated bone resorption.
Mig-2 (show FERMT2 ELISA Kits) significantly attenuates the antitumor action of cisplatin.
Kindlins are a small family of proteins that mediate protein-protein interactions involved in integrin activation and thereby have a role in cell adhesion, migration, differentiation, and proliferation. The protein encoded by this gene has a key role in the regulation of hemostasis and thrombosis. This protein may also help maintain the membrane skeleton of erythrocytes. Mutations in this gene cause the autosomal recessive leukocyte adhesion deficiency syndrome-III (LAD-III). Alternative splicing results in multiple transcript variants encoding distinct isoforms.
fermitin family member 3
, fermitin family homolog 3
, unc-112-related protein 2
, MIG2-like protein
, UNC-112 related protein 2
, kindlin 3