A ceramidase subtype that is active at alkaline pH. It is found at high levels within the SMALL INTESTINE.
Amidohydrolases that are specific for the cleavage of the N-acyl linkage of CERAMIDES. Ceramidases are classified as acidic, neutral or basic according to the optimal pH with which they function.
A ceramidase subtype that is active at acid pH. It plays an important role in sphingolipid degradation by catalyzing the lysosomal hydrolysis of ceramide to sphingosine and free fatty acid. Inherited deficiency of acid ceramidase activity results in FARBER LIPOGRANULOMATOSIS.
A ceramidase subtype that is active at neutral pH. It is found at high levels within the SMALL INTESTINE and in the BRAIN.
An enzyme that catalyzes the hydrolysis of a ceramidetrihexoside to a ceramidedihexoside plus galactose.
Amidohydrolases are enzymes that catalyze the hydrolysis of amides and related compounds, playing a crucial role in various biological processes including the breakdown and synthesis of bioactive molecules.
Members of the class of neutral glycosphingolipids. They are the basic units of SPHINGOLIPIDS. They are sphingoids attached via their amino groups to a long chain fatty acyl group. They abnormally accumulate in FABRY DISEASE.
An amino alcohol with a long unsaturated hydrocarbon chain. Sphingosine and its derivative sphinganine are the major bases of the sphingolipids in mammals. (Dorland, 28th ed)
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.

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)

Alkaline ceramidase is a type of enzyme that belongs to the family of hydrolases, specifically those acting on ester bonds. This enzyme's function is to catalyze the hydrolysis of ceramides into sphingosine and free fatty acids. Ceramides are important lipid molecules found in cell membranes, and their metabolism plays a crucial role in various biological processes such as cell differentiation, proliferation, and apoptosis.

Alkaline ceramidase is localized in the endoplasmic reticulum and Golgi apparatus of cells and has an optimum pH range between 8.5 to 9.5. It is involved in several physiological processes, including skin barrier formation, inflammation, and cancer development. Mutations in the gene that encodes for alkaline ceramidase have been associated with various diseases such as Farber's lipogranulomatosis, a rare genetic disorder characterized by accumulation of ceramides in tissues leading to joint pain, hoarseness, and progressive intellectual disability.

Ceramidases are a group of enzymes that catalyze the hydrolysis of ceramide into sphingosine and free fatty acids. Ceramides are important components of cell membranes, and their metabolism is tightly regulated in cells. The hydrolysis of ceramide by ceramidases produces sphingosine, which can be further phosphorylated to form sphingosine-1-phosphate (S1P), a signaling molecule involved in various cellular processes such as proliferation, differentiation, and survival.

There are several types of ceramidases that have been identified, including acid ceramidase, neutral ceramidase, and alkaline ceramidase. These enzymes differ in their subcellular localization, substrate specificity, and physiological functions. Dysregulation of ceramidase activity has been implicated in various diseases, including cancer, neurodegenerative disorders, and inflammatory conditions. Therefore, ceramidases are considered as potential therapeutic targets for the treatment of these diseases.

Acid ceramidase is an enzyme that plays a role in the metabolism of ceramides, which are lipid molecules found in cell membranes. Specifically, acid ceramidase helps to break down ceramides into sphingosine and free fatty acids. This enzyme is active at an acidic pH and is located in the lysosomes, which are organelles within cells that help to break down and recycle various materials.

Defects in the gene that provides instructions for making acid ceramidase can lead to a condition called Farber disease, which is characterized by the accumulation of ceramides in various tissues and organs. This can cause a range of symptoms, including joint pain, muscle weakness, and developmental delays.

Neutral ceramidase is an enzyme that plays a role in the metabolism of sphingolipids, which are a type of lipid found in cell membranes. Specifically, neutral ceramidase catalyzes the conversion of ceramide to sphingosine and free fatty acid. This reaction takes place at a neutral pH, hence the name "neutral" ceramidase.

Ceramide is a key component of the lipid bilayer in cell membranes and is also involved in various signaling pathways related to cell growth, differentiation, and apoptosis (programmed cell death). The conversion of ceramide to sphingosine by neutral ceramidase helps to regulate these processes.

Abnormal levels or activity of neutral ceramidase have been implicated in various diseases, including cancer, inflammation, and neurodegenerative disorders. For example, increased activity of this enzyme has been observed in some types of cancer, which may contribute to tumor growth and progression. On the other hand, decreased activity of neutral ceramidase has been linked to inflammatory conditions and neurodegenerative diseases such as Alzheimer's disease.

Galactosylgalactosylglucosylceramidase is a type of enzyme that is involved in the breakdown and recycling of complex lipids called glycosphingolipids in the body. More specifically, it helps to break down a particular type of glycosphingolipid known as globotriaosylceramide (Gb3 or CD77) into simpler components.

This enzyme is critical for maintaining the health and function of various tissues in the body, including the nervous system. Deficiencies in galactosylgalactosylglucosylceramidase have been linked to a number of serious genetic disorders, such as Tay-Sachs disease and Sandhoff disease, which are characterized by the accumulation of Gb3 and other glycosphingolipids in various tissues, leading to progressive neurological deterioration and other symptoms.

Amidohydrolases are a class of enzymes that catalyze the hydrolysis of amides and related compounds, resulting in the formation of an acid and an alcohol. This reaction is also known as amide hydrolysis or amide bond cleavage. Amidohydrolases play important roles in various biological processes, including the metabolism of xenobiotics (foreign substances) and endogenous compounds (those naturally produced within an organism).

The term "amidohydrolase" is a broad one that encompasses several specific types of enzymes, such as proteases, esterases, lipases, and nitrilases. These enzymes have different substrate specificities and catalytic mechanisms but share the common ability to hydrolyze amide bonds.

Proteases, for example, are a major group of amidohydrolases that specifically cleave peptide bonds in proteins. They are involved in various physiological processes, such as protein degradation, digestion, and regulation of biological pathways. Esterases and lipases hydrolyze ester bonds in various substrates, including lipids and other organic compounds. Nitrilases convert nitriles into carboxylic acids and ammonia by cleaving the nitrile bond (C≡N) through hydrolysis.

Amidohydrolases are found in various organisms, from bacteria to humans, and have diverse applications in industry, agriculture, and medicine. For instance, they can be used for the production of pharmaceuticals, biofuels, detergents, and other chemicals. Additionally, inhibitors of amidohydrolases can serve as therapeutic agents for treating various diseases, such as cancer, viral infections, and neurodegenerative disorders.

Ceramides are a type of lipid molecule that are found naturally in the outer layer of the skin (the stratum corneum). They play a crucial role in maintaining the barrier function and hydration of the skin. Ceramides help to seal in moisture, support the structure of the skin, and protect against environmental stressors such as pollution and bacteria.

In addition to their role in the skin, ceramides have also been studied for their potential therapeutic benefits in various medical conditions. For example, abnormal levels of ceramides have been implicated in several diseases, including diabetes, cardiovascular disease, and cancer. As a result, ceramide-based therapies are being investigated as potential treatments for these conditions.

Medically, ceramides may be mentioned in the context of skin disorders or diseases where there is a disruption in the skin's barrier function, such as eczema, psoriasis, and ichthyosis. In these cases, ceramide-based therapies may be used to help restore the skin's natural barrier and improve its overall health and appearance.

Sphingosine is not a medical term per se, but rather a biological compound with importance in the field of medicine. It is a type of sphingolipid, a class of lipids that are crucial components of cell membranes. Sphingosine itself is a secondary alcohol with an amino group and two long-chain hydrocarbons.

Medically, sphingosine is significant due to its role as a precursor in the synthesis of other sphingolipids, such as ceramides, sphingomyelins, and gangliosides, which are involved in various cellular processes like signal transduction, cell growth, differentiation, and apoptosis (programmed cell death).

Moreover, sphingosine-1-phosphate (S1P), a derivative of sphingosine, is an important bioactive lipid mediator that regulates various physiological functions, including immune response, vascular maturation, and neuronal development. Dysregulation of S1P signaling has been implicated in several diseases, such as cancer, inflammation, and cardiovascular disorders.

In summary, sphingosine is a crucial biological compound with medical relevance due to its role as a precursor for various sphingolipids involved in cellular processes and as a precursor for the bioactive lipid mediator S1P.

Substrate specificity in the context of medical biochemistry and enzymology refers to the ability of an enzyme to selectively bind and catalyze a chemical reaction with a particular substrate (or a group of similar substrates) while discriminating against other molecules that are not substrates. This specificity arises from the three-dimensional structure of the enzyme, which has evolved to match the shape, charge distribution, and functional groups of its physiological substrate(s).

Substrate specificity is a fundamental property of enzymes that enables them to carry out highly selective chemical transformations in the complex cellular environment. The active site of an enzyme, where the catalysis takes place, has a unique conformation that complements the shape and charge distribution of its substrate(s). This ensures efficient recognition, binding, and conversion of the substrate into the desired product while minimizing unwanted side reactions with other molecules.

Substrate specificity can be categorized as:

1. Absolute specificity: An enzyme that can only act on a single substrate or a very narrow group of structurally related substrates, showing no activity towards any other molecule.
2. Group specificity: An enzyme that prefers to act on a particular functional group or class of compounds but can still accommodate minor structural variations within the substrate.
3. Broad or promiscuous specificity: An enzyme that can act on a wide range of structurally diverse substrates, albeit with varying catalytic efficiencies.

Understanding substrate specificity is crucial for elucidating enzymatic mechanisms, designing drugs that target specific enzymes or pathways, and developing biotechnological applications that rely on the controlled manipulation of enzyme activities.

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 ...
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 ...
"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- ...
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) ...
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 ...
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 ...
Ace (disambiguation) Ace 2 (disambiguation) acel (disambiguation) acei (disambiguation) ACER1 (alkaline ceramidase 1) This ...
... 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 U.S. National Library of Medicine Medical Subject Headings (MeSH) EC 3.5.1.23 Portal: Biology v t e (EC 3.5.1 ...
... 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 ...
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 ...
For the second most abundant putative partial, [Pfam:PF04734] (neutral/alkaline non-lysomal ceramidase), about 10% of the ...
Neutral/alkaline non-lysosomal ceramidase, N-terminal [Interproscan].","protein_coding" "SymbC1.scaffold1.804","1.804"," ...
Ceramidases convert Cers into LCBs. Human ceramidases can be divided into acidic, neutral, and alkaline ceramidases according ... 2019). It will be interesting to know whether NCER2 and other ceramidases exhibit both ceramidase and reverse ceramidase ... Loss of alkaline ceramidase inhibits autophagy in Arabidopsis and plays an important role during environmental stress response ... 2015b). In addition to ACER, the alkaline ceramidase TURGOR REGULATION DEFECT 1 (TOD1) has been identified in Arabidopsis and ...
TIM interacted with specificity protein 1 (Sp1) which contributes to upregulate the expression of alkaline ceramidase 2 (ACER2 ... Ceramidase Alcalina/fisiologia , Animais , Biópsia , Linhagem Celular Tumoral , Proliferação de Células/efeitos dos fármacos , ...
Alkaline Ceramidase. Ceramidase Alcalina. Ceramidasa Alcalina. Bone Morphogenetic Protein 1. Proteína Morfogenética do Osso 1. ... Neutral Ceramidase. Ceramidase Neutra. Ceramidasa Neutra. Pancreatic alpha-Amylases. alfa-Amilases Pancreáticas. alfa-Amilasas ...
Alkaline Ceramidase. Ceramidase Alcalina. Ceramidasa Alcalina. Bone Morphogenetic Protein 1. Proteína Morfogenética do Osso 1. ... Neutral Ceramidase. Ceramidase Neutra. Ceramidasa Neutra. Pancreatic alpha-Amylases. alfa-Amilases Pancreáticas. alfa-Amilasas ...
Alkaline Ceramidase. Ceramidasa Alcalina. Ceramidase Neutra. Neutral Ceramidase. Ceramidasa Neutra. Ceramidases. Ceramidases. ... Ceramidase Ácida. Acid Ceramidase. Ceramidasa Ácida. Ceramidase Alcalina. ...
Acid ceramidase deficiency.. *Farber disease o Lipogranulomatosis type 2 and 3 . Ceramide deficiency. Acid ceramidase ... Hypophosphatasia (HPP). Deficiency of alkaline phosphatase. Phosphoethanolaminuria. I (Back to top). *Iminoglycinuria. ... Acid ceramidase deficiency.. *Farber disease o Lipogranulomatosis type 5 (late infantil neurological form). Ceramide deficiency ...
... are plasma membrane proteins often considered to act as adiponectin receptors with a ceramidase activity. Additionally, the ... In particular, IZH2 shows sequence homology with ceramidases, signals via sphingoid bases (a product of the ceramidase reaction ... lipid extracts were first evaporated and exposed to alkaline hydrolysis (0.1 M KOH in methanol for 60 min) in order to remove ... Acid ceramidase overexpression prevents the inhibitory effects of saturated fatty acids on insulin signaling. J Biol Chem. 2005 ...
... ceramidase_C 1 XM0123051271 IPR012588 DOMAIN:Exosome-assoc_fac_Rrp6_N 1 XM0045212902 IPR027401 HOMOLOGOUS_SUPERFAMILY:Myosin_IQ ... Alkaline_phosphatase_AS 4 XM0045337142;XM0045203512;XM0045243132;XM0123001931 IPR002933 FAMILY:Peptidase_M20 5 XM0045296012; ... Ceramidase_alk 1 XM0123051271 IPR001544 FAMILY:Aminotrans_IV 1 XM0045258502 IPR024132 FAMILY:Akirin 1 XM0123022451 IPR026571 ... ceramidase_N 1 XM0123051271 IPR005141 DOMAIN:eRF1_2 2 XM0123018931;XM0045219952 IPR000990 FAMILY:Innexin 6 XM0045300372; ...
Unexpectedly, serum levels of alanine transaminase, aspartate transaminase, alkaline phosphatase, gamma-glutamyl transpeptidase ... Ceramidases *Ceramide-Specific Glycosyltransferase *CFTR *CGRP Receptors *Channel Modulators, Other *Checkpoint Control Kinases ...
P-Bromotetramisole Oxalate is a potent nonspecific alkaline phosphatase inhibitor.. * GC38444 (-)-SHIN1 (-)-SHIN1 ((-)-RZ-2994 ... Ceramidases(4). *CERK(1). *Collagen proline hydroxylase(3). *COT/TpI2(2). *COMT(13) ...
... in this case alkaline phosphatase and gamma-glutamyltransferase. In asymptomatic individuals the diagnosis is determined after ... Ceramidases *Ceramide-Specific Glycosyltransferase *CFTR *CGRP Receptors *Channel Modulators, Other *Checkpoint Control Kinases ...
Alkaline ceramidase activity on NBD-C12-PHC in the brains of young (6W) versus middle-aged mice (8M). Note that the alkaline ... Reduction of alkaline ceramidase activity on NBD-C12-PHC in Acer3-/- mice. Note that Acer3-/- mice at either 6W or 8M of age ... Alkaline ceramidase 2 is essential for the homeostasis of plasma sphingoid bases and their phosphates. Li F, Xu R, Low BE, Lin ... Reduction of alkaline ceramidase activity on C18:1-ceramide in the whole brains of Acer3 knockout mice. Note that the brain ...
Purchase Recombinant Alkaline ceramidase (W02F12.2). It is produced in in vitro E.coli expression system. High purity. Good ... Recombinant Alkaline ceramidase (W02F12.2), partial ( Yeast-CSB-YP524292CXY1 E.coli-CSB-EP524292CXY1 Baculovirus-CSB- ...
Abbreviations: ACER2, alkaline ceramidase 2; FUT4, fucosyltransferase 4; GCNT1, glucosaminyl (N-acetyl) transferase 1, core 2; ...
Alkaline ceramidase 2 regulates beta1 integrin maturation and cell adhesion.. Sun WHu WXu RJin JSzulc ZMZhang GGaladari SHObeid ... Correction: Alkaline Ceramidase 3 Deficiency Results in Purkinje Cell Degeneration and Cerebellar Ataxia Due to Dyshomeostasis ... Alkaline Ceramidase 3 Deficiency Results in Purkinje Cell Degeneration and Cerebellar Ataxia Due to Dyshomeostasis of ...
... acid ceramidase (AC), neutral ceramidase (NC), alkaline ceramidase 1 (ACER1), alkaline ceramidase 2 (ACER2), and alkaline ... Alkaline ceramidase family: The first two decades. Xu R, Antwi Boasiako P, Mao C. Xu R, et al. Cell Signal. 2021 Feb;78:109860 ... Role of alkaline ceramidases in the generation of sphingosine and its phosphate in erythrocytes. Xu R, Sun W, Jin J, Obeid LM, ... Alkaline ceramidase 2 is essential for the homeostasis of plasma sphingoid bases and their phosphates. Li F, Xu R, Low BE, Lin ...
4. Role of alkaline ceramidases in the generation of sphingosine and its phosphate in erythrocytes.. Xu R; Sun W; Jin J; Obeid ... Alkaline ceramidase 2 is essential for the homeostasis of plasma sphingoid bases and their phosphates.. Li F; Xu R; Low BE; Lin ... Deficiency of the alkaline ceramidase ACER3 manifests in early childhood by progressive leukodystrophy.. Edvardson S; Yi JK; ... Role of Ceramidases in Sphingolipid Metabolism and Human Diseases.. Parveen F; Bender D; Law SH; Mishra VK; Chen CC; Ke LY. ...
2009; ALKALINE CERAMIDASE was indexed under AMIDOHYDROLASES 2007-2008. History Note. 2009(2007); for ALKALINE CERAMIDASE use ... Alkaline Ceramidase Preferred Concept UI. M0514738. Registry Number. EC 3.5.1.23. Scope Note. A ceramidase subtype that is ... Alkaline Ceramidase Preferred Term Term UI T714789. Date02/21/2008. LexicalTag NON. ThesaurusID NLM (2009). ... A ceramidase subtype that is active at alkaline pH. It is found at high levels within the SMALL INTESTINE.. Registry Number. EC ...
2009; ALKALINE CERAMIDASE was indexed under AMIDOHYDROLASES 2007-2008. History Note. 2009(2007); for ALKALINE CERAMIDASE use ... Alkaline Ceramidase Preferred Concept UI. M0514738. Registry Number. EC 3.5.1.23. Scope Note. A ceramidase subtype that is ... Alkaline Ceramidase Preferred Term Term UI T714789. Date02/21/2008. LexicalTag NON. ThesaurusID NLM (2009). ... A ceramidase subtype that is active at alkaline pH. It is found at high levels within the SMALL INTESTINE.. Registry Number. EC ...
Acid ceramidase C. *Neutral ceramidases C. *Alkaline ceramidases C. *Ceramide kinase C ...
alkaline ceramidase 2 Q8VD53. Aqp2. aquaporin-2. P56402. Aqp3. aquaporin-3. Q8R2N1. ...
C103892 Q8TDN7 Alkaline Ceramidase 1 C103895 Q5QJU3 Alkaline Ceramidase 2 C103898 Q9NUN7 Alkaline Ceramidase 3 C191782 P10696 ... Alkaline Phosphatase, Germ Cell Type C107554 P05187 Alkaline Phosphatase, Placental Type C104232 P05186 Alkaline Phosphatase, ... C103901 Q13510 Acid Ceramidase C26201 O43427 Acidic Fibroblast Growth Factor Intracellular-Binding Protein C125587 P39687 ... C103904 Q9NR71 Neutral Ceramidase C41046 P22894 Neutrophil Collagenase C179388 P14598 Neutrophil Cytosol Factor 1 C104565 ...
Alkaline Ceramidase. Ceramidasa Alcalina. Ceramidase Neutra. Neutral Ceramidase. Ceramidasa Neutra. Ceramidases. Ceramidases. ... Ceramidase Ácida. Acid Ceramidase. Ceramidasa Ácida. Ceramidase Alcalina. ...
HN - 2009 MH - Alkaline Ceramidase UI - D055574 MN - D8.811.277.87.250.300 MS - A ceramidase subtype that is active at alkaline ... HN - 2009(2007); for ALKALINE CERAMIDASE use CERAMIDASES 2007-2008 MH - Allomyces UI - D055134 MN - B5.230.74 MS - A genus of ... HN - 2009 MH - Neutral Ceramidase UI - D055576 MN - D8.811.277.87.250.650 MS - A ceramidase subtype that is active at neutral ... HN - 2009(2007); for NEUTRAL CERAMIDASE use CERAMIDASES 2007-2008 MH - Nevus, Halo UI - D055882 MN - C4.557.665.560.580 MS - A ...
Alkaline Ceramidase 1 Protects Mice from Premature Hair Loss by Maintaining the Homeostasis of Hair Follicle Stem Cells Stem ...
Furthermore, the enzyme responsible for CER hydrolysis, alkaline ceramidase, was not altered, suggesting that it was not ... Ceramidase Alcalina/metabolismo , Antioxidantes , Ceramidas/metabolismo , Cloridrato de Fingolimode , Humanos , ...
Alkaline Ceramidase. Ceramidasa Alcalina. Ceramidase Neutra. Neutral Ceramidase. Ceramidasa Neutra. Ceramidases. Ceramidases. ... Ceramidase Ácida. Acid Ceramidase. Ceramidasa Ácida. Ceramidase Alcalina. ...
Alkaline Ceramidase Alkaline Phosphatase Alkaloids Alkalosis Alkalosis, Respiratory Alkanes Alkanesulfonates Alkanesulfonic ... Acid Ceramidase Acid Etching, Dental Acid Phosphatase Acid Rain Acid Sensing Ion Channel Blockers Acid Sensing Ion Channels ... Ceramidases Ceramides Ceratitis capitata Ceratopogonidae Cercaria Cerclage, Cervical Cercocebus Cercocebus atys Cercopithecidae ...
For instance, recent researches showed that acid ceramidase, known as an important enzyme, which can regulate the levels of ... on the number of colonies obtained that were positive for the early pluripotency reprogramming and stem cell marker alkaline ...
... alkaline phosphatase).[3] Finally, some hepatic enzymes (e.g., lysosomal enzymes, alcohol dehydrogenase and lactate ... Acid ceramidase. [13] AT1B1_HUMAN. Sodium/potassium-transporting ATPase subunit-β1 [13] ...
In isolated mitochondria acidic pH increased and alkaline pH decreased release of free HK-1 and HK-2 from the mitochondrial ... Hence SL 0101-1 alkaline and acidic cellular pH tends to drive energy metabolism toward glycolysis and oxidative ... Furthermore experiments using purified proteins showed that alkaline pH promoted co-immunoprecipitation of HK with VDAC protein ... Confocal microscopy showed increased co-localization of HK-1 and HK-2 with VDAC1 by alkaline treatment. ...
Bach1 is a transcription factor of the capncollar type alkaline region leucine zipper factor family (CNC-bZip) that regulates ...
  • 15. Role of Ceramidases in Sphingolipid Metabolism and Human Diseases. (nih.gov)
  • [ 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)
  • Furthermore experiments using purified proteins showed that alkaline pH promoted co-immunoprecipitation of HK with VDAC protein. (cell-signaling-pathways.com)
  • 12. Deficiency of the alkaline ceramidase ACER3 manifests in early childhood by progressive leukodystrophy. (nih.gov)
  • Inherited deficiency of acid ceramidase activity results in FARBER LIPOGRANULOMATOSIS. (nih.gov)
  • 4. Role of alkaline ceramidases in the generation of sphingosine and its phosphate in erythrocytes. (nih.gov)
  • AN - coordinate with organ or disease /surg HN - 2009 MH - Acid Ceramidase UI - D055573 MN - D8.811.277.87.250.100 MS - A ceramidase subtype that is active at acid pH. (nih.gov)
  • 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)
  • In isolated mitochondria acidic pH increased and alkaline pH decreased release of free HK-1 and HK-2 from the mitochondrial pellet into SL 0101-1 the supernatant. (cell-signaling-pathways.com)