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An aberrant LITAF-phosphoethanolamine interaction on the surface of intracellular membranes contributes to the molecular pathogenesis that underlies Charcot-Marie-Tooth disease type 1C.
Study conclude that LITAF is a monotopic membrane protein whose membrane integration is stabilised by a zinc finger. The related human protein, CDIP1 (cell death involved p53 target 1), displays identical membrane topology, suggesting that this mode of membrane integration is conserved in LITAF family proteins.
PIG7 promotes leukemia cell chemosensitivity via lysosomal membrane permeabilization.
Suggest LITAF as regulatory of pro-inflammatory and pro-fibrogenic pattern in non-alcoholic fatty liver disease.
LITAF may serve as a switch in the balance between classical and alternative activation in tumor-associated inflammation. (Review)
Results show that LITAF mutants in Charcot-Marie-Tooth 1C have an altered intracellular localization. They localize either completely or partially in the mitochondria depending on the mutation site. This can explain the different severity of the disease.
Study shows that the I92V LITAF sequence variant would be a good candidate for a biomarker in the case of the CMT1A/HNPP (show PMP22 Proteins) disorders.
The results of this study findings confirm that the genetic analysis of LITAF/SIMPLE should be considered for the diagnostic flow-chart of CMT1 patient, especially when nerve conduction studies show the presence of conduction blocks.
Early-onset hereditary neuropathy with liability to pressure palsy (HNPP (show PMP22 Proteins)) was associated frequently with isoleucine92valine LITAF polymorphism.
It is concluded that PA can induce insulin (show INS Proteins) resistance in liver cells and knockdown of LITAF expression can reduce insulin (show INS Proteins) resistance in liver cells.
Data suggest that atypical inflammatory signaling kinetics may account for the gain of function elicited by the Litaf protein SIMPLE mutation in Charcot-Marie-Tooth Type 1C (CMT1C) patients.
Mutation of SIMPLE (Litaf) in Charcot-Marie-Tooth 1C alters production of exosomes.
This study demonistrated that loss of Litaf function is unlikely to be a major contributor to Charcot-Marie-Tooth disease, but modulating effects of macrophages need to be considered in the etiology of the disease.
In LITAF-deficient mice, mLITAF-mediated CCL2 (show CCL2 Proteins) production in macrophages was significantly reduced compared to the wild-type control animals
Study provides evidence that LITAF contributes to the regulation of TNF-alpha (show TNF Proteins) in LPM harvested following acute inflammation.
Whole-body deletion of LPS-induced TNF-alpha factor (LITAF) markedly improves experimental endotoxic shock and inflammatory arthritis.
the regulation of LITAF/TNF-alpha by p53 (show TP53 Proteins) and its short peptide 162-motif
PTP4A3 (show PTP4A3 Proteins) was identified as a novel negative regulator of LPS (show TLR4 Proteins)-induced LITAF/TNF-alpha production.
LITAF is an important mediator of the LPS (show TLR4 Proteins)-induced inflammatory response.
Lipopolysaccharide is a potent stimulator of monocytes and macrophages, causing secretion of tumor necrosis factor-alpha (TNF-alpha) and other inflammatory mediators. This gene encodes lipopolysaccharide-induced TNF-alpha factor, which is a DNA-binding protein and can mediate the TNF-alpha expression by direct binding to the promoter region of the TNF-alpha gene. The transcription of this gene is induced by tumor suppresor p53 and has been implicated in the p53-induced apoptotic pathway. Mutations in this gene cause Charcot-Marie-Tooth disease type 1C (CMT1C) and may be involved in the carcinogenesis of extramammary Paget's disease (EMPD). Multiple alternatively spliced transcript variants have been found for this gene.
LPS-induced TNF-alpha factor
, lipopolysaccharide-induced TNF-alpha factor
, lipopolysaccharide-induced tumor necrosis factor-alpha factor
, p53-induced gene 7 protein
, small integral membrane protein of lysosome/late endosome
, tumor protein p53 inducible protein 7
, LPS-induced TN factor
, LPS-induced TNF-alpha factor homolog
, estrogen-enhanced transcript protein 1
, estrogen-responsive uterine transcript
, lipopolysaccharide-induced tumor necrosis factor-alpha factor homolog
, TNF-alpha factor
, lipid-induced TNF-alpha factor
, tissue necrosis factor-alpha
, LITAF-like protein
, Nedd4 WW domain-binding protein 3
, estrogen-enhanced transcript protein