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FABP5 encodes the fatty acid binding protein found in epidermal cells, and was first identified as being upregulated in psoriasis tissue. Zusätzlich bieten wir Ihnen FABP5 Proteine (8) und FABP5 Kits (6) und viele weitere Produktgruppen zu diesem Protein an.
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Findings show that FABP5 expression is up-regulated in hepatocellular carcinoma (HCC (zeige FAM126A Antikörper)), and provide evidence that that it could play a crucial role of tumor progression, invasion and metastasis in HCC (zeige FAM126A Antikörper) through EMT (zeige ITK Antikörper) induction.
Circulating levels of AFABP and EFABP are not decreased in Lipodystrophy despite adipose tissue loss in contrast to other adipokines including leptin and adiponectin.
A high expression ratio between FABP5 and CRABPII (zeige CRABP2 Antikörper) may be related to CP tumor recurrence and ATRA could be a potential therapeutic agent for CP chemotherapy.
Data suggest that antinociceptive agent SBFI-26 binds at a portal site as well as at the canonical site in the substrate pocket of FABP5 and FABP7 (zeige FABP7 Antikörper); only the S form of SBFI-26 binds to both FABP5 and FABP7 (zeige FABP7 Antikörper) in their co-crystal structures; SBFI-26 induces conformational changes in FABP5 and FABP7 (zeige FABP7 Antikörper).
secreted FABP4 and FABP5 from adipocytes as adipokines differentially affect transcriptional and metabolic regulation in ADSC near adipocytes
FABP5 plays an important role in the carcinogenesis and metastasis of cervical cancer, and FABP5 may be a novel predictor for prognostic assessment of cervical cancer patients.
FABP5 promoted VEGF expression and angiogenesis through PPARgamma which was activated by fatty acids transported by FABP5.
FABP5 is associated with increased subclinical atherosclerosis
the balance between FABP4 and FABP5 in endothelial cells may be important in regulation of angiogenic versus quiescent phenotypes in blood vessels.
Long chain fatty acids suppress the oncogenic properties of FABP5-expressing carcinoma cells in cultured cells.
Lack of PPARbeta (zeige PPARD Antikörper)/delta-expression, TUNEL reaction, RA receptor (RAR)beta (zeige RARB Antikörper), and cellular retinoic acid-binding protein (CRABP (zeige CRABP2 Antikörper))-II (zeige CRABP2 Antikörper) were induced in E-FABP-positive septoclasts under RA excess, suggesting the growth arrest/cell-death of septoclasts, whereas cartilage-derived retinoic acid-sensitive protein (CD-RAP (zeige MIA Antikörper)) inducing the cell growth arrest or morphological changes was induced in septoclasts under VA deficiency.
A 42.1 +/- 12.6% decrease in the BBB transport of (14) C-DHA in 8-month-old AD transgenic mice relative to wild-type mice was associated with a 34.5 +/- 6.7% reduction in FABP5 expression in isolated brain capillaries. Short-term spatial and recognition memory deficits were seen in AD mice on a 6-month n-3 fatty acid-depleted diet, but not those on control diet.
Using a yeast two-hybrid screen, immunoprecipitation, microscale thermophoresis analysis and cellular fractionation, we discovered that Fabp5 interacts with the calnexin (zeige CANX Antikörper) cytoplasmic C-tail domain at the endoplasmic reticulum. These observations identify Fabp5 as a previously unrecognized calnexin (zeige CANX Antikörper) binding partner.
Following infection with Listeria monocytogenes, we observed similar clonal expansion, contraction and formation of memory CD8 T cells in WT and E-FABP-/- mice. Analysis of Listeria-specific CD4 T cells revealed no defect in the expansion, contraction, and formation of memory CD4 T cells in E-FABP-/- mice. Our data demonstrate that E-FABP is dispensable for antigen-specific T cell response following bacterial infection.
Genetic deletion of fatty acid-binding protein 5 (FABP5) in mice reduces uptake of exogenous docosahexaenoic acid (DHA) into brain endothelial cells and brain capillaries and reduces brain parenchymal levels of endogenous DHA. Therefore, FABP5 in the brain endothelial cell is a crucial contributor to the brain levels of DHA. Critically, lowered brain DHA levels in FABP5(-/-) mice occurred in tandem with cognitive deficits
Mice lacking FABP5 and FABP7 (zeige FABP7 Antikörper), which exhibit highest affinities for endocannabinoids, possessed elevated levels of the endocannabinoid anandamide and the related N-acylethanolamines palmitoylethanolamide and oleoylethanolamide.
These studies show, for the first time, a correlation between FABP5 and EGFR (zeige EGFR Antikörper) in enhancing TNBC metastasis through a novel mechanism
loss of FABP5 promotes a more anti-inflammatory response.
Circulating levels of GIP were significantly decreased in FABP5-deficient mice.
FABP4 gene expression level in adipose tissue was higher than in muscle. In contrast, FABP5 was expressed at low levels in adipocytes and muscle tissues. Low and moderate correlations between FABP4 and FABP5 gene expression were observed in muscle and in backfat, respectively.
QTL and haplotype analysis revealed that both FABP4 (zeige FABP4 Antikörper) and FABP5 (clustered in mammals) are major candidate genes for the FAT1 (zeige FAT1 Antikörper) QTL; the most likely position for the FAT1 (zeige FAT1 Antikörper) QTL is between these two genes.
This gene encodes the fatty acid binding protein found in epidermal cells, and was first identified as being upregulated in psoriasis tissue. Fatty acid binding proteins are a family of small, highly conserved, cytoplasmic proteins that bind long-chain fatty acids and other hydrophobic ligands. FABPs may play roles in fatty acid uptake, transport, and metabolism. Polymorphisms in this gene are associated with type 2 diabetes. The human genome contains many pseudogenes similar to this locus.
epidermal-type fatty acid-binding protein
, fatty acid-binding protein, epidermal
, psoriasis-associated fatty acid-binding protein homolog
, fatty acid binding protein 5
, epithelial fatty acid-binding protein
, keratinocyte lipid-binding protein
, cutaneous fatty acid-binding protein
, fatty acid-binding protein 5
, epidermal fatty acid-binding protein
, differentiation-associated lipid-binding protein LP2