Alkaline Ceramidase
Ceramidases
Acid Ceramidase
Neutral Ceramidase
Galactosylgalactosylglucosylceramidase
Ceramides
Sphingosine
Specific and sensitive assay for alkaline and neutral ceramidases involving C12-NBD-ceramide. (1/19)
A fluorescent analogue of ceramide, C12-NBD-ceramide, was found to be hydrolyzed much faster than 14C-labeled ceramide by alkaline ceramidase from Pseudomonas aeruginosa and neutral ceramidase from mouse liver, while this substrate was relatively resistant to acid ceramidase from plasma of the horseshoe crab. The radioactive substrate was used more preferentially by the acid ceramidase. It should be noted that C6-NBD-ceramide, which is usually used for ceramidase assays, was hardly hydrolyzed by any of the enzymes examined, compared to C12-NBD-ceramide. For the alkaline and neutral enzymes, the Vmax and k (Vmax/Km) with C12-NBD-ceramide were much higher than those with 14C-ceramide. In contrast, for the acid enzyme these parameters with C12-NBD-ceramide were less than half those with the radioisotope-labeled substrate. It is noteworthy that the labeling of ceramide with NBD did not itself reduce the Km of the alkaline enzyme, but did that of the neutral enzyme. It was also found that C12-NBD-ceramide was preferentially hydrolyzed by the alkaline and neutral enzymes, but not the acid one, in several mammalian cell lines. This study clearly shows that the attachment of NBD, but not dansyl, increases the susceptibility of ceramide to alkaline and neutral enzyme, and decreases that to acid enzymes. Thus the use of this substrate provides a specific and sensitive assay for alkaline and neutral ceramidases. (+info)Molecular cloning, sequencing, and expression of the gene encoding alkaline ceramidase from Pseudomonas aeruginosa. Cloning of a ceramidase homologue from Mycobacterium tuberculosis. (2/19)
We previously reported the purification and characterization of a novel type of alkaline ceramidase from Pseudomonas aeruginosa strain AN17 (Okino, N., Tani, M., Imayama, S., and Ito, M. (1998) J. Biol. Chem. 273, 14368-14373). Here, we report the molecular cloning, sequencing, and expression of the gene encoding the ceramidase of this strain. Specific oligonucleotide primers were synthesized using the peptide sequences of the purified ceramidase obtained by digestion with lysylendopeptidase and used for polymerase chain reaction. DNA fragments thus amplified were used as probes to clone the gene encoding the ceramidase from a genomic library of strain AN17. The open reading frame of 2,010 nucleotides encoded a polypeptide of 670 amino acids including a signal sequence of 24 residues, 64 residues of which matched the amino acid sequence determined for the purified enzyme. The molecular weight of the mature enzyme was estimated to be 70,767 from the deduced amino acid sequence. Expression of the ceramidase gene in Escherichia coli, resulted in production of a soluble enzyme with the identical N-terminal amino acid sequence. Recombinant ceramidase was purified to homogeneity from the lysate of E. coli cells and confirmed to be identical to the Pseudomonas enzyme in its specificity and other enzymatic properties. No significant sequence similarities were found in other known functional proteins including human acid ceramidase. However, we found a sequence homologous to the ceramidase in hypothetical proteins encoded in Mycobacterium tuberculosis, Dictyostelium discoideum, and Arabidopsis thaliana. The homologue of the ceramidase gene was thus cloned from an M. tuberculosis cosmid and expressed in E. coli, and the gene was demonstrated to encode an alkaline ceramidase. This is the first report for the cloning of an alkaline ceramidase. (+info)Purification and characterization of a neutral ceramidase from mouse liver. A single protein catalyzes the reversible reaction in which ceramide is both hydrolyzed and synthesized. (3/19)
We report here a novel ceramidase that was purified more than 150, 000-fold from the membrane fraction of mouse liver. The enzyme was a monomeric polypeptide having a molecular mass of 94 kDa and was highly glycosylated with N-glycans. The amino acid sequence of a fragment obtained from the purified enzyme was homologous to those deduced from the genes encoding an alkaline ceramidase of Pseudomonas aeruginosa and a hypotheical protein of the slime mold Dictyostelium discoideum. However, no significant sequence similarities were found in other known functional proteins including acid ceramidases of humans and mice. The enzyme hydrolyzed various N-acylsphingosines but not galactosylceramide, sulfatide, GM1a, or sphingomyelin. The enzyme exhibited the highest activity around pH 7.5 and was thus identified as a type of neutral ceramidase. The apparent K(m) and V(max) values for C12-4-nitrobenzo-2-oxa-1, 3-diazole-ceramide and C16-(14)C-ceramide were 22.3 microM and 29.1 micromol/min/mg and 72.4 microM and 3.6 micromol/min/mg, respectively. This study also clearly demonstrated that the purified 94-kDa ceramidase catalyzed the condensation of fatty acid to sphingosine to generate ceramide, but did not catalyze acyl-CoA-dependent acyl-transfer reaction. (+info)Cloning and characterization of a novel human alkaline ceramidase. A mammalian enzyme that hydrolyzes phytoceramide. (4/19)
Ceramidases are enzymes involved in regulating cellular levels of ceramides, sphingoid bases, and their phosphates. Based on sequence homology to the yeast alkaline ceramidases YPC1p (Mao, C., Xu, R., Bielawska, A., and Obeid, L. M. (2000) J. Biol. Chem. 275, 6876--6884) and YDC1p (Mao, C., Xu, R., Bielawska, A., Szulc, Z. M., and Obeid, L. M. (2000) J. Biol Chem. 275, 31369--31378), we report the identification and cloning of a cDNA encoding for a novel human alkaline ceramidase (aPHC) that hydrolyzes phytoceramide selectively. Northern blot analysis showed that aPHC was ubiquitously expressed, with the highest expression in placenta. Green fluorescent protein tagging showed that it was localized in both the Golgi apparatus and endoplasmic reticulum. Overexpression of aPHC in mammalian cells elevated in vitro ceramidase activity toward N-4-nitrobenz-2-oxa-1,3-diazole-C(12)-phytoceramide. Its expression in a yeast mutant strain devoid of any ceramidase activity restored the ceramidase activity and caused an increase in the hydrolysis of phytoceramide in yeast cells, thus leading to the decreased biosynthesis of sphingolipids. These data collectively suggest that, similar to the yeast phytoceramidase YPC1p, aPHC has phytoceramidase activity both in vitro and in cells; hence, it is a functional homolog of the yeast phytoceramidase YPC1p. However, in contrast to YPC1p, aPHC exhibited no reverse activity of ceramidase either in vitro or in cells. Biochemical characterization showed that aPHC had a pH optimum of 9.5, was activated by Ca(2+), but was inhibited by Zn(2+) and sphingosine. Substrate specificity showed that aPHC hydrolyzed phytoceramide preferentially. Together, these data demonstrate that aPHC is a novel human alkaline phytoceramidase, the first mammalian alkaline ceramidase to be identified as being specific for the hydrolysis of phytoceramide. (+info)Cloning and characterization of a mouse endoplasmic reticulum alkaline ceramidase: an enzyme that preferentially regulates metabolism of very long chain ceramides. (5/19)
Ceramidases deacylate ceramides, important intermediates in the metabolic pathway of sphingolipids. In this study, we report the cloning and characterization of a novel mouse alkaline ceramidase (maCER1) with a highly restricted substrate specificity. maCER1 consists of 287 amino acids, and it has a 28 and 32% identity to the Saccharomyces alkaline ceramidases (YPC1p and YDC1p) and the human alkaline phytoceramidase, respectively. Reverse transcriptase-PCR analysis demonstrated that maCER1 was predominantly expressed in skin. maCER1 was localized to the endoplasmic reticulum as revealed by immunocytochemistry. In vitro biochemical characterization determined that maCER1 hydrolyzed D-erythro-ceramide exclusively but not D-erythro-dihydroceramide or D-ribo-phytoceramide. Similar to other alkaline ceramidases, maCER1 had an alkaline pH optimum of 8.0, and it was activated by Ca2+ but inhibited by Zn2+,Cu2+, and Mn2+. maCER1 was also inhibited by sphingosine, one of its products. Metabolic labeling studies showed that overexpression of maCER1 caused a decrease in the incorporation of radiolabeled dihydrosphingosine into ceramide and complex sphingolipids but led to a concomitant increase in sphingosine-1-P (S1P) in HeLa cells. Mass measurement showed that overexpression of maCER1 selectively lowered the cellular levels of D-erythro-C24:1-ceramide, but not other ceramide species and caused an increase in the levels of S1P. Taken together, these data suggest that maCER1 is a novel alkaline ceramidase with a stringent substrate specificity and that maCER1 is selectively expressed in skin and may have a role in regulating the levels of bioactive lipids ceramide and S1P, as well as complex sphingolipids. (+info)Golgi alkaline ceramidase regulates cell proliferation and survival by controlling levels of sphingosine and S1P. (6/19)
Sphingosine-1-phosphate (S1P), a sphingolipid metabolite, promotes cell proliferation and survival whereas its precursor, sphingosine, has the opposite effects. However, much remains unknown about their regulation. Here we identify a novel human ceramidase (haCER2) that regulates the levels of both sphingosine and S1P by controlling the hydrolysis of ceramides. haCER2 is localized to the Golgi complex and is highly expressed in the placenta. High ectopic expression of haCER2 caused fragmentation of the Golgi complex and growth arrest in HeLa cells due to sphingosine accumulation. Low ectopic expression of haCER2 increased S1P without sphingosine accumulation, promoting cell proliferation in serum-free medium. This proliferative effect was suppressed by dimethylsphingosine, an inhibitor of the S1P formation, or by the RNA interference (RNAi) -mediated inhibition of S1P(1,) a G-protein-coupled receptor for S1P. The RNAi-mediated down-regulation of haCER2 enhanced the serum deprivation-induced growth arrest and apoptosis of HeLa cells, which was inhibited by addition of exogenous S1P. Serum deprivation up-regulated both haCER2 mRNA and activity in HeLa cells. haCER2 mRNA is also up-regulated in some tumors. Taken together, these results suggest that haCER2 is important for the generation of S1P and S1P-mediated cell proliferation and survival, but that its overexpression may cause cell growth arrest due to an accumulation of sphingosine. (+info)Upregulation of the human alkaline ceramidase 1 and acid ceramidase mediates calcium-induced differentiation of epidermal keratinocytes. (7/19)
Extracellular calcium (Ca2+(o)) potently induces the growth arrest and differentiation of human epidermal keratinocytes (HEKs). We report that Ca2+(o) markedly upregulates the human alkaline ceramidase 1 (haCER1) in HEKs; and its upregulation mediates the Ca2+(o)-induced growth arrest and differentiation of HEKs. haCER1 is the human ortholog of mouse alkaline ceramidase 1 that we previously identified. haCER1 catalyzed the hydrolysis of very long-chain ceramides to generate sphingosine (SPH). This in vitro activity required Ca2+. Ectopic expression of haCER1 in HEKs decreased the levels of D-e-C(24:1)-ceramide and D-e-C(24:0)-ceramide but elevated the levels of both SPH and its phosphate (S1P), whereas RNA interference-mediated knockdown of haCER1 caused the opposite effects on the levels of these sphingolipids in HEKs. Similar to haCER1 overexpression, Ca2+(o) increased the levels of SPH and S1P, and this was attenuated by haCER1 knockdown. haCER1 knockdown also inhibited the Ca2+(o)-induced growth arrest of HEKs and the Ca2+(o)-induced expression of keratin 1 and involucrin in HEKs. In addition, the acid ceramidase (AC) was also upregulated by Ca2+(o); and its knockdown attenuated the Ca2+(o)-induced expression of keratin 1 and involucrin in HEKs. These results strongly suggest that upregulation of haCER1 and AC mediates the Ca2+(o)-induced growth arrest and differentiation of HEKs by generating SPH and S1P. (+info)Ceramidases: regulators of cellular responses mediated by ceramide, sphingosine, and sphingosine-1-phosphate. (8/19)
(+info)KEGG BRITE: KEGG Orthology (KO) - Equus caballus (horse)
Alkaline ceramidase 1 is essential for mammalian skin homeostasis and regulating whole-body energy expenditure
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ACER3
Alkaline ceramidase 3 also known as ACER3 is a ceramidase enzyme which in humans is encoded by the ACER3 gene. GRCh38: Ensembl ... "Cloning and characterization of a novel human alkaline ceramidase. A mammalian enzyme that hydrolyzes phytoceramide". J. Biol. ... Mao C, Obeid LM (September 2008). "Ceramidases: regulators of cellular responses mediated by ceramide, sphingosine, and ...
ACER2
Alkaline ceramidase 2 also known as ACER2 is a ceramidase enzyme which in humans is encoded by the ACER2 gene. The ACER2/ ... Sun W, Hu W, Xu R, Jin J, Szulc ZM, Zhang G, Galadari SH, Obeid LM, Mao C (February 2009). "Alkaline ceramidase 2 regulates ... 2006). "Golgi alkaline ceramidase regulates cell proliferation and survival by controlling levels of sphingosine and S1P". ... Mao C, Obeid LM (September 2008). "Ceramidases: regulators of cellular responses mediated by ceramide, sphingosine, and ...
ENPP7
"Human meconium contains significant amounts of alkaline sphingomyelinase, neutral ceramidase, and sphingolipid metabolites". ... and named alkaline sphingomyelinase (alk-SMase), as the optimal pH of the enzyme was 9.0 and its main substrate is ... 2005). "Cloning of alkaline sphingomyelinase from rat intestinal mucosa and adjusting of the hypothetical protein XP_221184 in ... Andersson D, Kotarsky K, Wu J, Agace W, Duan RD (July 2009). "Expression of alkaline sphingomyelinase in yeast cells and anti- ...
ASAH2
2006). "Golgi alkaline ceramidase regulates cell proliferation and survival by controlling levels of sphingosine and S1P". ... A novel but highly conserved gene family of neutral/alkaline ceramidases". J. Biol. Chem. 275 (15): 11229-34. doi:10.1074/jbc. ... Neutral ceramidase is an enzyme that in humans is encoded by the ASAH2 gene. GRCh38: Ensembl release 89: ENSG00000188611 - ... 2004). "Neutral ceramidase gene: role in regulating ceramide-induced apoptosis". Gene. 315: 113-22. doi:10.1016/S0378-1119(03) ...
Lipid signaling
2006). "Golgi alkaline ceramidase regulates cell proliferation and survival by controlling levels of sphingosine and S1P". ... Sphingosine (Sph) is formed by the action of ceramidase (CDase) enzymes on ceramide in the lysosome. Sph can also be formed in ... The low levels of Sph and their increase in response to stimulation of cells, primarily by activation of ceramidase by growth- ... Ceramide can also be broken down by enzymes called ceramidases, leading to the formation of sphingosine, Moreover, a phosphate ...
ACER1
Alkaline ceramidase 1 also known as ACER1 is a ceramidase enzyme which in humans is encoded by the ACER1 gene. ACER1 mediates ... "Upregulation of the human alkaline ceramidase 1 and acid ceramidase mediates calcium-induced differentiation of epidermal ... "Cloning and characterization of a mouse endoplasmic reticulum alkaline ceramidase: an enzyme that preferentially regulates ... Ito M, Okino N, Tani M, Mitsutake S, Mori K (Mar 2002). "[Molecular evolution of neutral ceramidase: signalling molecule and ...
Ace1
Ace (disambiguation) Ace 2 (disambiguation) acel (disambiguation) acei (disambiguation) ACER1 (alkaline ceramidase 1) This ...
Ceramidase
... cell survival neutral ceramidase (ASAH2, ASAH2B, ASAH2C) - protective against inflammatory cytokines alkaline ceramidase 1 ( ... Presently, 7 human ceramidases encoded by 7 distinct genes have been cloned: acid ceramidase (ASAH1) - ... mediating cell differentiation by controlling the generation of SPH and S1P alkaline ceramidase 2 (ACER2) - important for cell ... Ceramidase at the US National Library of Medicine Medical Subject Headings (MeSH) EC 3.5.1.23 Portal: Biology v t e (EC 3.5.1, ...
List of EC numbers (EC 3)
... ceramidase EC 3.5.1.24: choloylglycine hydrolase EC 3.5.1.25: N-acetylglucosamine-6-phosphate deacetylase EC 3.5.1.26: N4-(β-N- ... alkaline phosphatase EC 3.1.3.2: acid phosphatase EC 3.1.3.3: phosphoserine phosphatase EC 3.1.3.4: phosphatidate phosphatase ... ceramidase EC 3.5.1.24: choloylglycine hydrolase EC 3.5.1.25: N-acetylglucosamine-6-phosphate deacetylase EC 3.5.1.26: N4-(β-N- ...
Alkaline ceramidase 2 regulates beta;1 integrin maturation and cell adhesion - Fingerprint - United Arab Emirates...
Discovery of highly potent acid ceramidase inhibitors with in vitro tumor chemosensitizing activity | Scientific Reports
The expression of acid ceramidase (AC) - a cysteine amidase that hydrolyses the proapoptotic lipid ceramide - is abnormally ... Description of a new alkaline ceramidase. Biochim. Biophys. Acta 398, 125-131 (1975). ... Recombinant acid ceramidase expression. Rat AC was cloned from a brain cDNA library using primers based on the sequence ... Acid ceramidase controls apoptosis and increases autophagy in human melanoma cells treated with doxorubicin *Michele Lai ...
MMRRC:041992-MU
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pEG302 22aa SunTag NtDRMcd SUP
DeCS
Alkaline Ceramidase - Preferred Concept UI. M0514738. Scope note. A ceramidase subtype that is active at alkaline pH. It is ... 2009; ALKALINE CERAMIDASE was indexed under AMIDOHYDROLASES 2007-2008. History Note:. 2009(2007); for ALKALINE CERAMIDASE use ... A ceramidase subtype that is active at alkaline pH. It is found at high levels within the SMALL INTESTINE.. ...
ABCA2 modulates the expression of the Alzheimer's disease gene, amyloid precursor protein (APP).
Pharmacological inhibition of ceramidase activity or activation PKC activity with 12-myristate 13-acetate (PMA) or ... ABCA2 overexpression increased in vitro alkaline and acid ceramidase activity. Sphingosine is a physiological inhibitor of ... ABCA2 overexpression increased in vitro alkaline and acid ceramidase activity. Sphingosine is a physiological inhibitor of ... Pharmacological inhibition of ceramidase activity or activation PKC activity with 12-myristate 13-acetate (PMA) or ...
abnormal epididymal fat pad morphology - Ontology Report - Rat Genome Database
ACER3 Antibody<...
Connexion
Mutagenetix > Incidental...
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YOR184W 2167.216480 INESSENTIAL SER1 phosphoserine transaminase,phosphoserine aminotransferase
3.442340 INESSENTIAL YPC1 alkaline ceramidase with reverse activity, sphingolipid metabolism, YOL111C 3.438519 INESSENTIAL ... 3.357342 INESSENTIAL PHO8 repressible alkaline phosphatase,alkaline phosphatase, YOR012W -3.360239 INESSENTIAL biological_ ... 3.667345 INESSENTIAL YDC1 alkaline dihydroceramidase with minor reverse activity., sphingolipid metabolism, YMR008C -3.675230 ...
Endogenous acid ceramidase protects epithelial cells from Porphyromonas gingivalis-induced inflammation in vitro. | Biochem...
Thus far, acid, neutral and alkaline ceramidase isozymes have been described. However, the expression patterns of ceramidase ... No significant fluctuation was detected for neutral or alkaline ceramidases in either gingival samples or cell cultures. Next, ... Ceramidases are a group of enzymes that degrade pro-inflammatory ceramide by cleaving a fatty acid to form anti-inflammatory ... In addition, acid-ceramidase expression in EpiGingival™ 3D culture and OBA-9â ¯cells was suppressed by stimulation with P. ...
DeCS 2009 - Novos termos
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Domain IPR003439:ABC transporter-like
Neutral/alkaline non-lysosomal ceramidase, N-terminal 3 Family IPR019291:Host attachment protein 3 Family IPR027565:Cupin fold ... Neutral/alkaline non-lysosomal ceramidase, C-terminal 2 Domain IPR027414:Glycosyl hydrolase family 95, N-terminal domain 2 ... Alkaline phosphatase, active site 8 Family IPR007390:Sporulation stage V, protein R 8 Family IPR014973:Protein of unknown ... Ceramidase 4 Domain IPR011682:Glycosyl hydrolase family 38, C-terminal 4 Domain IPR025423:Domain of unknown function DUF4149 4 ...
PathBank
Hydrolysis | Profiles RNS
DeCS 2009 - New terms
DeCS 2009 - New terms
DeCS 2009 - New terms
Ceramide5
- The expression of acid ceramidase (AC) - a cysteine amidase that hydrolyses the proapoptotic lipid ceramide - is abnormally high in several human tumors, which is suggestive of a role in chemoresistance. (nature.com)
- Ceramidases (EC 3.5.1.23), such as ASAH2, catalyze hydrolysis of the N-acyl linkage of ceramide, a second messenger in a variety of cellular events, to produce sphingosine. (utsouthwestern.edu)
- Ceramidases are a group of enzymes that degrade pro-inflammatory ceramide by cleaving a fatty acid to form anti-inflammatory sphingosine lipid . (bvsalud.org)
- Structural Basis for Ceramide Recognition and Hydrolysis by Human Neutral Ceramidase. (musc.edu)
- Saposin D facilitates acid ceramidase degradation of ceramide to sphingosine and fatty acids ( 14 ). (cdc.gov)
Acid8
- ABCA2 overexpression increased in vitro alkaline and acid ceramidase activity. (growkudos.com)
- Endogenous acid ceramidase protects epithelial cells from Porphyromonas gingivalis-induced inflammation in vitro. (bvsalud.org)
- Thus far, acid , neutral and alkaline ceramidase isozymes have been described. (bvsalud.org)
- A significantly lower level of acid ceramidase expression was detected in gingival tissues from periodontal patients compared to those from healthy subjects . (bvsalud.org)
- In addition, acid - ceramidase expression in EpiGingival™ 3D culture and OBA-9â ¯ cells was suppressed by stimulation with P. gingivalis in vitro. (bvsalud.org)
- Next, to elucidate the role of acid ceramidase in P. gingivalis-induced inflammation in vitro, OBA-9â ¯ cells were transduced with adenoviral vector expressing the human acid ceramidase (Ad-ASAH1) gene or control adenoviral vector (Ad-control). (bvsalud.org)
- Collectively, our data show the novel discovery of anti-inflammatory and anti-apoptotic effects of acid ceramidase in host cells exposed to periodontal bacteria , and the attenuation of the expression of host-protective acid ceramidase in periodontal lesions. (bvsalud.org)
- 4-Methylumbelliferyl oleate is a fluorogenic substrate for acid and alkaline lipases . (medchemexpress.com)
Neutral1
- No significant fluctuation was detected for neutral or alkaline ceramidases in either gingival samples or cell cultures . (bvsalud.org)
Antibodies1
- Diagnosis of PBC is based on sustained elevation of alkaline phosphatase (ALP), a serum marker of cholestasis, and the presence of either serum antimitochondrial antibodies or histological cholangiopathy.2, 3 Higher levels of ALP correlate with disease progression, and are associated with higher risk of liver transplantation or death.4 Elevated bilirubin levels, which occur later in advanced diseases, are a strong predictor of patient outcomes. (baxkyardgardener.com)
Activity1
- Pharmacological inhibition of ceramidase activity or activation PKC activity with 12-myristate 13-acetate (PMA) or diacylglycerol (DAG) decreased endogenous APP mRNA levels in ABCA2 overexpressing cells. (growkudos.com)
Human1
- Measured by its ability to inhibit BMP9 induced alkaline phosphatase production by MC3T3E1 mouse chondrogenic cells and the ED 50 is typically 5-15 ng/mL in the presence of 2 ng/mL of human BMP9. (medchemexpress.cn)
Cells1
- In this study, expression patterns of ceramidase isoforms were quantified by real-time PCR and immunohistochemistry in gingival samples of patients with periodontitis and healthy subjects , as well as in EpiGingivalTM-3D culture and OBA-9 gingival epithelial cells both of which were stimulated with or without the presence of live Porphyromonas gingivalis (ATCC 33277 strain ). (bvsalud.org)
Expression1
- However, the expression patterns of ceramidase isoforms as well as their role in periodontal disease pathogenesis remain unknown. (bvsalud.org)
1.231
- Ceramidases (EC 3.5.1.23), such as ASAH2, catalyze hydrolysis of the N-acyl linkage of ceramide, a second messenger in a variety of cellular events, to produce sphingosine. (utsouthwestern.edu)
Phosphatase3
- c The hBD3 proteins appearance degree of the transfected hPDLCs on times 1, 3, 5, and 7 at an MOI of 150 (*LPS (1?gmL?1) was put into cells to stimulate an inflammatory microenvironment.31 alkaline phosphatase (ALP) and alizarin crimson S (ARS) staining assays were conducted to detect any osteogenic differentiation adjustments. (secretion.org)
- [ 25 ] Other proteins are secreted by gallbladder cells (e.g., mucin glycoproteins, similar to those found in gastric juice and saliva) [ 24 ] or released by cells lining the whole biliary tract through the formation of microvesicules, which are made soluble by bile salts when their concentration in the canalicular lumen increases (e.g., alkaline phosphatase). (medscape.com)
- Currently, individuals with gallstones undergo ultrasonography exam and hepatobiliary biochemical serum analyses (bilirubin, alkaline phosphatase, etc.) as part of routine preoperative testing for CBD stones [8C16]. (immune-source.com)
Neutral3
- Ceramidases are classified as acidic, neutral or basic according to the optimal pH with which they function. (lookformedical.com)
- A ceramidase subtype that is active at neutral pH. (lookformedical.com)
- PREDICTED: neutral ceramidase [Beta vulgaris subsp. (nibb.ac.jp)
CDase1
- It has recently become evident that at least five ceramidase (CDase) isoforms are present in human epidermis, and that specifically acidic CDase (aCDase) and alkaline CDase (alkCDase) activities increase during keratinocyte differentiation, and thus might play a pivotal role(s) in permeability barrier function. (tno.nl)
Ceramides1
- It results from the accumulation of CERAMIDES in various tissues due to an inherited deficiency of ACID CERAMIDASE. (lookformedical.com)
250.3001
- HN - 2009 MH - Alkaline Ceramidase UI - D055574 MN - D8.811.277.87.250.300 MS - A ceramidase subtype that is active at alkaline pH. (nih.gov)