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Artificially applied c-kit(+) cells interact with the target organ endothelium following ischemia reperfusion injury. This interaction seems to depend on TLR-MyD88 (zeige MYD88 Proteine) signaling.
a critical role for PRL2 phosphatase in mediating Notch and c-Kit signals in early T cell progenitors, is reported.
These results suggest that CD44 (zeige CD44 Proteine)(+)CD117(+) T cells are stem cells and a specific T-cell phenotype that initially develops in the thymus, but they do not progress through DN3 and DN4 stages, lack a DP stage, and potently suppress T-cell proliferation and modulate the CTLA-4 (zeige CTLA4 Proteine) pathway.
we studied the efficacy of ACK2, an antibody that blocks KIT, followed by low-dose irradiation as a preconditioning regimen for hematopoietic cell transplantation using a murine model of Mucopolysaccharidosis type II.
C-kit-positive hematopoietic stem/progenitor cells expressed significantly higher of Nox1 (zeige NOX1 Proteine) and catalase (zeige CAT Proteine), but less of lactoperoxidase (zeige LPO Proteine) than in matured mononuclear cells.
c-KIT signaling regulates self-renewal capacity and prevents neurodifferentiation in culture.
These findings identify functional redundancy among Kit-dependent hematopoietic lineages and establish an unanticipated capacity of megakaryocytes to mediate IL-1 (zeige IL1A Proteine)-driven systemic inflammatory disease.
WNT (zeige WNT2 Proteine) signaling at an early stage (E12 (zeige ELSPBP1 Proteine)-E15) of submandibular salivary gland (SMG (zeige SNRPG Proteine)) development inhibits end bud morphogenesis and differentiation into proacini by suppressing Kit expression.
c-kit can reduce inflammation, positively modulate airway remodeling, and improve function in a mouse model of airway hyperresponsiveness
Kit inactivation within oocytes also led to premature ovarian failure, albeit via a contrasting phenotype. Despite normal initial complements of primordial follicles, oocytes remained dormant with arrested oocyte maturation. Foxo3 (zeige FOXO3 Proteine) protein localization in the nucleus versus cytoplasm explained both mutant phenotypes.
Results find that COA6 associates with COX2 and is crucial for its maturation and complex IV biogenesis. Also, COA6 interacts with the copper chaperone SCO1 which indicates that COA6 is intrinsically involved in the copper delivery process for COX2.
Sco1 is a metallochaperone that selectively transfers Cu(I) ions based on loop recognition, whereas Sco2 is a copper-dependent thiol reductase of the cysteine ligands in the oxidase.
COX20 cooperates with SCO1 and SCO2 (zeige SCO2 Proteine) to mature COX2 and promote the assembly of cytochrome c (zeige CYCS Proteine) oxidase.
COX19 (zeige COX19 Proteine) is necessary for the transduction of a SCO1-dependent mitochondrial redox signal that regulates ATP7A (zeige ATP7A Proteine)-mediated cellular copper efflux.
Results describe the tissue distribution of SCO1 and SCO2 in mouse and human tissues.
SCO1 facilitates the transfer of copper from SCO2 (zeige SCO2 Proteine) to the CuA site at an early stage of COX (zeige COX8A Proteine) assembly in mitochondria.
data suggest that both Cu(I) and Cu(II) binding are critical for normal Sco (zeige SNAI1 Proteine) function.
Cox17-mediated copper metallation of Sco1, as well as the subsequent failure of Cu(A) site maturation, is the basis for the inefficient assembly of the cytochrome c oxidase complex in SCO1 patients
Sco1 has evolved to bind a metal atom via the di-Cys (zeige DNAJC5 Proteine) motif to act as a copper chaperone, the oxidized form of the nickel-bound protein suggests that it may also maintain the thioredoxin (zeige TXN Proteine) function.
These results suggest a mitochondrial pathway for the regulation of cellular copper content that involves signaling through SCO1 and SCO2, perhaps by their thiol redox or metal-binding state.
Mammalian cytochrome c oxidase (COX) catalyzes the transfer of reducing equivalents from cytochrome c to molecular oxygen and pumps protons across the inner mitochondrial membrane. In yeast, 2 related COX assembly genes, SCO1 and SCO2 (synthesis of cytochrome c oxidase), enable subunits 1 and 2 to be incorporated into the holoprotein. This gene is the human homolog to the yeast SCO1 gene.
Dominant white spotting
, Steel Factor Receptor
, c-kit proto-oncogene protein
, dominant spotting
, mast/stem cell growth factor receptor Kit
, proto-oncogene c-Kit
, proto-oncogene tyrosine-protein kinase Kit
, spotted sterile male
, tyrosine-protein kinase Kit
, protein SCO1 homolog, mitochondrial
, SCO cytochrome oxidase deficient homolog 1