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physiological function
CerS5 activity is inhibited in a dominant-negative fashion by co-expression with catalytically inactive CerS5, and isoform CerS2 activity is enhanced by co-expression with a catalytically active form of CerS5 or CerS6. In a constitutive heterodimer comprising CerS5 and CerS2, the activity of CerS2 depends on the catalytic activity of CerS5. CerS dimers are formed upon rapid stimulation of ceramide synthesis by curcumin
physiological function
CerS5 is essential to maintain cellular C16:0 sphingolipid pools in lung, spleen, muscle, liver, and white adipose tissue. In CerS5-deficient mice, glycerophospholipid levels are not altered, while in skeletal muscle, liver, and spleen, C16:0-ceramide levels aere altered independent of feeding conditions. The loss of CerS5 is associated with reduced weight gain and improved systemic health, including maintenance of glucose homeostasis and reduced white adipose tissue inflammation after high fat diet challenge
physiological function
exogenously expressed LASS5 in lung epithelia triggers increased ceramide synthesis, knockdown studies using fumonisin B1 or LASS5 siRNA reduce ceramide synthase activity by 78% or 45%, respectively. Overexpression of LASS5 also reduces phosphatidylcholine synthesis. Maximal inhibition is achieved when LASS5 is coexpressed with a plasmid encoding a neutral sphingomyelinase involved in sphingomyelin hydrolysis
physiological function
inhibition of isoform Cers5 by fuminisin B1 or siRNA suppresses myristate-induced C14-ceramide generation and X-box binding protein XBP1 splicing. Increased XBP1 splicing induces the downstream expression of IL-6 in a isoforms CerS5/6-dependent manner. A myristate-enriched milk fat-based diet, but not a lard-based diet, increases C14-ceramide, XBP1 splicing, and IL-6 expression in vivo
physiological function
ionizing radiation induces de novo synthesis of ceramide to influence HeLa cell apoptosis by specifically activating CerS isoforms 2, 5, and 6 that generate opposing anti- and pro-apoptotic ceramides in mitochondrial membranes. Isoforms CerS5 and CerS6 each confer about 50% of the C16:0 CerS baseline synthetic activity, both are required for ionizing radiation-induced activity. Isoforms CerS2, 5, and 6 might exist as heterocomplexes in HeLa cells
physiological function
Lass5 interacts with succinate dehydrogenase subunit B. The C-terminal fragment of succinate dehydrogenase subunit B is required for the interaction. Lass5 and succinate dehydrogenase subunit B co-localize in COS-7 cells. Lass5 and succinate dehydrogenase subunit B expressions are up-regulated in neuroglioma tissue, and Lass5 or succinate dehydrogenase subunit B expression represses p53 or p21 reporter activity, respectively
physiological function
overexpression of isoform Cers5 leads to accumulation of C16:0 ceramides. Presence of insulin has no effect on sphingomyelins, while palmitate treatment causes a significant decrease in several species, including the predominant C16:0 species. CerS5 knockdown reduces glycogen synthesis in the absence or presence of palmitate. Isoform CerS1 overexpression results in minor upregulation of endogenous CerS5
physiological function
overexpression of LASS elevates the synthesis of (dihydro)ceramides selectively enriched in palmitic acid
physiological function
skeletal muscle from mice deficient of either CerS1 or CerS5 shows reduced caliber sizes of both slow (type 1) and fast (type 2) muscle fibers, fiber grouping, and fiber switch to type 1 fibers. CerS1- and CerS5-deficient mice exhibit reduced twitch and tetanus forces of musculus extensor digitorum longus
physiological function
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exogenously expressed LASS5 in lung epithelia triggers increased ceramide synthesis, knockdown studies using fumonisin B1 or LASS5 siRNA reduce ceramide synthase activity by 78% or 45%, respectively. Overexpression of LASS5 also reduces phosphatidylcholine synthesis. Maximal inhibition is achieved when LASS5 is coexpressed with a plasmid encoding a neutral sphingomyelinase involved in sphingomyelin hydrolysis
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medicine
both isoforms CerS4 and CerS5 are up-regulated in endometrial and colon cancer cells. Apoptosis induction by anastrozole or 5-FU results in down-regulation of CerS4 and CerS5 in endometrial and colon cancer cells
medicine
CerS1 and CerS5 mRNA expression is reduced in muscle biopsies from patients in advanced stage of chronic heart failure suffering from muscle wasting and frailty
medicine
CerS5-dependent ceramide synthesis has a strong impact in white adipose tissue after high fat diet feeding
medicine
in human breast cancer tissue, a significant increase in CerS4 and CerS6 mRNA is observed in estrogen receptor positive cancer tissue. The activities of CerS4 and CerS5 promoter constructs increase after estradiol treatment in MCF-7 cells. Estradiol and GPER1 mediate their effects on CerS4 and Cers5 promoter by activating AP-1, most likely through dimerization of c-Jun and c-Fos
medicine
in human breast cancer tissue, a significant increase in CerS4 and CerS6 mRNA isobserved in estrogen receptor positive cancer tissue. The activities of CerS4 and CerS5 promoter constructs increase after estradiol treatment in MCF-7 cells. Estradiol and GPER1 mediate their effects on CerS4 and Cers5 promoter by activating AP-1, most likely through dimerization of c-Jun and c-Fos
medicine
in human wild-type p53 HCT-116 colon cancer cells, treatment with oxaliplatin or 5-fluorouracil leads to a strong increase in ceramide synthase CerS5 expression and C16:0-ceramide levels, which is not seen in HCT-116 cells lacking p53 expression. The increase in CerS5 expression occurs by stabilizing CerS5 mRNA at the 3'-UTR
medicine
long-chain ceramides are upregulated whereas very long-chain ceramides are downregulated in cell lines, mouse animal model, and patients with cystic fibrosis, compared with their controls. Treatment with fenretinide decreases the levels of long-chain ceramides and increases the levels of very long-chain ceramides
medicine
long-chain ceramides are upregulated whereas very long-chain ceramides are downregulated in cell lines, mouse animal model, and patients with cystic fibrosis, compared with their controls. Treatment with fenretinide decreases the levels of long-chain ceramides and increases the levels of very long-chain ceramides
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A tissue-specific screen of ceramide expression in aged mice identifies ceramide synthase-1 and ceramide synthase-5 as potential regulators of fiber size and strength in skeletal muscle
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Homo sapiens (Q8N5B7), Mus musculus (Q9D6K9)
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Homo sapiens (Q8N5B7)
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Homo sapiens (Q8N5B7), Homo sapiens (Q9HA82)
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