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CERS2 encodes a protein that has sequence similarity to yeast longevity assurance gene 1. Additionally we are shipping Ceramide Synthase 2 Antibodies (49) and Ceramide Synthase 2 Kits (1) and many more products for this protein.
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Data show that 1-acylglycerol-3-phosphate O-acyltransferase 9 (AGPAT9) inhibit cell growth by regulating expression of KLF4/LASS2/V-ATPase proteins in breast cancer.
these results indicate that miR (show MLXIP Proteins)-9 upregulation might be associated with malignant phenotype of bladder cancer. miR (show MLXIP Proteins)-9 promotes chemoresistance of bladder cancer cells by target LASS2.
Data show that CERS2 expression was markedly different between various breast cancer cells and inversely correlated with cell invasion.
silencing of TMSG1 increased V-ATPase (show ATP6V1H Proteins) activity, decreased extracellular pH and in turn the activation of secreted MMP-2 (show MMP2 Proteins), which ultimately promoted metastasis capacity of breast cancer cell.
Results confirmed that TMSG1 is a potential metastasis suppressor gene, and suggested that the mechanism involved the induction of apoptosis and inhibition of cell proliferation via a caspase (show CASP3 Proteins)-dependent mitochondrial pathway.
the vacuolar ATPase (V-ATPase) activity and extracellular hydrogen ion concentration were significantly decreased and the activity of secreted matrix metalloproteinase-2 (MMP-2 (show MMP2 Proteins)) was downregulated in MCF-7 cells overexpressing LASS2/TMSG1
the inhibitory effect of the LASS2 on growth, invasion and metastasis of prostate cancer cells
Co-expression of CerS2 with CerS4 (show CERS4 Proteins)/CerS6 (show CERS6 Proteins) reversed the inhibitory effect of long chain ceramides on cell proliferation and the induction of apoptosis. we detected no effect on cell proliferation.
expression and role of ceramide synthase-2 in the lung
results contribute to the conclusion that LASS2/TMSG1 could regulate V-ATPase (show ATP6V1H Proteins) activity and intracellular pH through the direct interaction of its homeodomain and the C subunit of V-ATPase (show ATP6V1H Proteins)
CerS1 (show CERS1 Proteins), -2, and -6 are hyperacetylated in the mitochondria of SIRT3 (show SIRT3 Proteins)-null mice.
Haploinsufficiency for this enzyme altered the pattern of ceramide acylation in the liver without affecting total ceramide levels, replacing very-long-chain ceramides with long-chain C16-ceramides.
Development of pheochromocytoma in ceramide synthase 2 null mice
our data strongly indicate that G-CSF (show CSF3 Proteins)-induced CXCR2 (show CXCR2 Proteins) expression is regulated in a CerS2-dependent manner and that CerS2 thereby promotes the migration of neutrophils, thus, contributing to inflammation and the development of EAE and MS.
Data indicate that the augmented rate of death of ceramide synthase 2 (CerS2) null mice is due to elevated levels of tumor necrosis factor alpha (TNFalpha (show TNF Proteins)) secretion as a result of enhanced activity of TNFalpha (show TNF Proteins)-converting enzyme (TACE (show ADAM17 Proteins)).
CerS2-deficient kidneys were completely depleted of phytosphingosine-containing cortical sulfatides without any compensatio
we first report that Lass2 deficiency caused the downregulation of miR (show MLXIP Proteins)-694 and the upregulation of its target gene Tnfaip3 (show TNFAIP3 Proteins) in vivo in mice, which may be related to a high risk of occurrence of hepatocellular carcinoma
The identification of specific cell types in which CerS2 protein is expressed is prerequisite to further mechanistic characterization of phenotypic abnormalities exhibited by CerS2-deficient mice.
Lass2 is a protective gene against diethylnitrosamine-induced liver tumorigenesis; and upregulation of the TGF-beta1 (show TGFB1 Proteins)-Smad4 (show SMAD4 Proteins)-PAI-1 (show SERPINE1 Proteins) axis may contribute to the vulnerability of Lass2-knockout mice to diethylnitrosamine.
Data indicate that oxidized phospholipids (OxPLs)-induced ceramide synthases (CerS1 (show CERS1 Proteins)-Cers6 (show CERS6 Proteins)) activity in macrophages is responsible for the accumulation of ceramide.
This gene encodes a protein that has sequence similarity to yeast longevity assurance gene 1. Mutation or overexpression of the related gene in yeast has been shown to alter yeast lifespan. The human protein may play a role in the regulation of cell growth. Alternatively spliced transcript variants encoding the same protein have been described.
LAG1 homolog, ceramide synthase 2
, LAG1 longevity assurance 2
, longevity assurance (LAG1, S. cerevisiae) homolog 2
, tumor metastasis-suppressor gene 1 protein
, LAG1 longevity assurance homolog 2
, TRAM homolog 3
, longevity assurance homolog 2
, translocating chain-associating membrane protein homolog 3