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Article ; Online: An update on sphingosine-1-phosphate and other sphingolipid mediators.

Fyrst, Henrik / Saba, Julie D

2010 Volume 6, Issue 7, Page(s) 489–497

Abstract: Sphingolipids comprise a complex family of naturally occurring molecules that are enriched in lipid rafts and contribute to their unique biochemical properties. Membrane sphingolipids also serve as a reservoir for bioactive metabolites including ... ...

Abstract	Sphingolipids comprise a complex family of naturally occurring molecules that are enriched in lipid rafts and contribute to their unique biochemical properties. Membrane sphingolipids also serve as a reservoir for bioactive metabolites including sphingosine, ceramide, sphingosine-1-phosphate and ceramide-1-phosphate. Among these, sphingosine-1-phosphate has emerged as a central regulator of mammalian biology. Sphingosine-1-phosphate is essential for mammalian brain and cardiac development and for maturation of the systemic circulatory system and lymphatics. In addition, sphingosine-1-phosphate contributes to trafficking and effector functions of lymphocytes and other hematopoietic cells and protects against various forms of tissue injury. However, sphingosine-1-phosphate is also an oncogenic lipid that promotes tumor growth and progression. Recent preclinical and clinical investigations using pharmacological agents that target sphingosine-1-phosphate, its receptors and the enzymes required for its biosynthesis and degradation demonstrate the promise and potential risks of modulating sphingosine-1-phosphate signaling in treatment strategies for autoimmunity, cancer, cardiovascular disease and other pathological conditions.
MeSH term(s)	Animals ; Gene Expression Regulation/drug effects ; Gene Expression Regulation/physiology ; Humans ; Lysophospholipids/genetics ; Lysophospholipids/metabolism ; Sphingolipids/genetics ; Sphingolipids/metabolism ; Sphingosine/analogs & derivatives ; Sphingosine/genetics ; Sphingosine/metabolism
Chemical Substances	Lysophospholipids ; Sphingolipids ; sphingosine 1-phosphate (26993-30-6) ; Sphingosine (NGZ37HRE42)
Language	English
Publishing date	2010-06-17
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	2202962-X
ISSN	1552-4469 ; 1552-4450
ISSN (online)	1552-4469
ISSN	1552-4450
DOI	10.1038/nchembio.392
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Article: Sphingosine-1-phosphate lyase in development and disease: sphingolipid metabolism takes flight.

Fyrst, Henrik / Saba, Julie D

Biochimica et biophysica acta

2008 Volume 1781, Issue 9, Page(s) 448–458

Abstract: Sphingosine-1-phosphate lyase (SPL) is a highly conserved enzyme that catalyses the final step of sphingolipid degradation, namely the irreversible cleavage of the carbon chain at positions 2-3 of a long-chain base phosphate (LCBP), thereby yielding a ... ...

Abstract	Sphingosine-1-phosphate lyase (SPL) is a highly conserved enzyme that catalyses the final step of sphingolipid degradation, namely the irreversible cleavage of the carbon chain at positions 2-3 of a long-chain base phosphate (LCBP), thereby yielding a long-chain aldehyde and phosphoethanolamine. LCBPs are potent signaling molecules involved in cell proliferation, survival, migration, cell-cell interactions and cell stress responses. Therefore, tight regulation of LCBP signaling is required for proper cell function, and perturbations of this system can lead to alterations in biological processes including development, reproduction and physiology. SPL is a key enzyme in regulating the intracellular and circulating levels of LCBPs and is, therefore, gaining attention as a putative target for pharmacological intervention. This review provides an overview of our current understanding of SPL structure and function, mechanisms involved in SPL regulation and the role of SPL in development and disease.
MeSH term(s)	Aldehyde-Lyases/chemistry ; Aldehyde-Lyases/genetics ; Aldehyde-Lyases/metabolism ; Animals ; Apoptosis ; Disease ; Gene Expression Regulation, Developmental ; Humans ; Sphingosine/chemistry ; Sphingosine/metabolism
Chemical Substances	Aldehyde-Lyases (EC 4.1.2.-) ; sphingosine 1-phosphate lyase (aldolase) (EC 4.1.2.27) ; Sphingosine (NGZ37HRE42)
Language	English
Publishing date	2008-06-17
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbalip.2008.05.005
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Article ; Online: Mammalian acyl-CoA:lysophosphatidylcholine acyltransferase enzymes.

Soupene, Eric / Fyrst, Henrik / Kuypers, Frans A

Proceedings of the National Academy of Sciences of the United States of America

2008 Volume 105, Issue 1, Page(s) 88–93

Abstract: The mammalian RBC lacks de novo lipid synthesis but maintains its membrane composition by rapid turnover of acyl moieties at the sn-2 position of phospholipids. Plasma-derived fatty acids are esterified to acyl-CoA by acyl-CoA synthetases and transferred ...

Abstract	The mammalian RBC lacks de novo lipid synthesis but maintains its membrane composition by rapid turnover of acyl moieties at the sn-2 position of phospholipids. Plasma-derived fatty acids are esterified to acyl-CoA by acyl-CoA synthetases and transferred to lysophospholipids by acyl-CoA:lysophospholipid acyltransferases. We report the characterization of three lysophosphatidylcholine (lysoPC) acyltransferases (LPCATs), products of the AYTL1, -2, and -3 genes. These proteins are three members of a LPCAT family, of which all three genes are expressed in an erythroleukemic cell line. Aytl2 mRNA was detected in mouse reticulocytes, and the presence of the product of the human ortholog was confirmed in adult human RBCs. The three murine Aytl proteins generated phosphatidylcholine from long-chain acyl-CoA and lysoPC when expressed in Escherichia coli membranes. Spliced variants of Aytl1, affecting a conserved catalytic motif, were identified. Calcium and magnesium modulated LPCAT activity of both Aytl1 and -2 proteins that exhibit EF-hand motifs at the C terminus. Characterization of the product of the Aytl2 gene as the phosphatidylcholine reacylating enzyme in RBCs represents the identification of a plasma membrane lysophospholipid acyltransferase and establishes the function of a LPCAT protein.
MeSH term(s)	1-Acylglycerophosphocholine O-Acyltransferase/genetics ; 1-Acylglycerophosphocholine O-Acyltransferase/physiology ; Amino Acid Sequence ; Animals ; Catalytic Domain ; Cell Line, Tumor ; Cell Membrane/metabolism ; Cloning, Molecular ; Erythrocytes/metabolism ; Escherichia coli/metabolism ; Fatty Acids/metabolism ; Humans ; Mice ; Molecular Sequence Data ; Phosphatidylcholines/chemistry ; Reticulocytes/metabolism ; Sequence Homology, Amino Acid
Chemical Substances	Fatty Acids ; Phosphatidylcholines ; 1-Acylglycerophosphocholine O-Acyltransferase (EC 2.3.1.23) ; Lpcat1 protein, human (EC 2.3.1.23) ; Lpcat1 protein, mouse (EC 2.3.1.23)
Language	English
Publishing date	2008-01-08
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.0709737104
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Article: A rapid fluorescence assay for sphingosine-1-phosphate lyase enzyme activity.

Bandhuvula, Padmavathi / Fyrst, Henrik / Saba, Julie D

Journal of lipid research

2007 Volume 48, Issue 12, Page(s) 2769–2778

Abstract: Sphingosine-1-phosphate (S1P) lyase (SPL) catalyzes the conversion of S1P to ethanolamine phosphate and hexadecenal. This enzyme plays diverse roles in physiology and disease and, thus, may be useful as a disease marker and/or drug target. Unfortunately, ...

Abstract	Sphingosine-1-phosphate (S1P) lyase (SPL) catalyzes the conversion of S1P to ethanolamine phosphate and hexadecenal. This enzyme plays diverse roles in physiology and disease and, thus, may be useful as a disease marker and/or drug target. Unfortunately, the radioisotope-based assay currently used to quantify SPL activity is suboptimal. We have devised an assay using a commercially available omega(7-nitro-2-1,3-benzoxadiazol-4-yl)-d-erythro (NBD)-labeled fluorescent substrate. Alternatively, we provide a method for synthesis of the substrate from NBD-sphingosine. Enzyme activity is determined by following the formation of NBD-aldehyde product, which is isolated from unreacted substrate by lipid extraction and quantified after separation by HPLC using a C18 column. A fluorescent NBD-C18-sphingosine internal standard is used to control for extraction efficiency. The reaction is linear over 20 min and total protein concentrations of 20-200 mg/l. The sensitivity of the fluorescence assay is comparable to or better than that of the radioactive assay, and SPL levels as low as 8 pmol/mg/min were readily detected. Semicarbazide, a nonspecific SPL inhibitor, reduced SPL activity in vitro by approximately 70% using both standard and fluorescence methods. Product inhibition was not observed using ethanolamine phosphate and a commercially available source of hexadecenal. This method is suitable for quantifying SPL activity in a variety of cell and tissue sources.
MeSH term(s)	3T3-L1 Cells ; Aldehyde-Lyases/analysis ; Aldehyde-Lyases/chemistry ; Aldehyde-Lyases/metabolism ; Animals ; Catechols/chemistry ; Cell Line, Tumor ; Cells, Cultured ; Chromatography, High Pressure Liquid ; Enzyme Activation ; Enzyme Inhibitors/pharmacology ; Humans ; Mice ; Organometallic Compounds/chemistry ; Spectrometry, Fluorescence/methods
Chemical Substances	Catechols ; Enzyme Inhibitors ; Organometallic Compounds ; neodymium pyrocatechin disulfonate (15338-78-0) ; Aldehyde-Lyases (EC 4.1.2.-) ; sphingosine 1-phosphate lyase (aldolase) (EC 4.1.2.27)
Language	English
Publishing date	2007-09-13
Publishing country	United States
Document type	Evaluation Study ; Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	80154-9
ISSN	1539-7262 ; 0022-2275
ISSN (online)	1539-7262
ISSN	0022-2275
DOI	10.1194/jlr.D700010-JLR200
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Article ; Online: Chemopreventive sphingadienes downregulate Wnt signaling via a PP2A/Akt/GSK3β pathway in colon cancer.

Kumar, Ashok / Pandurangan, Ashok K / Lu, Fang / Fyrst, Henrik / Zhang, Meng / Byun, Hoe-Sup / Bittman, Robert / Saba, Julie D

Carcinogenesis

2012 Volume 33, Issue 9, Page(s) 1726–1735

Abstract: Sphingadienes (SDs) derived from soy and other natural sphingolipids are cytotoxic to colon cancer cells via an Akt-dependent mechanism and reduce adenoma formation in Apc(Min/+) mice. Wnt signaling is fundamental to colon carcinogenesis and is the basis ...

Abstract	Sphingadienes (SDs) derived from soy and other natural sphingolipids are cytotoxic to colon cancer cells via an Akt-dependent mechanism and reduce adenoma formation in Apc(Min/+) mice. Wnt signaling is fundamental to colon carcinogenesis and is the basis for spontaneous tumorigenesis in Apc(Min/+) mice and patients with familial adenomatous polyposis. In the present study, we investigated the impact of SDs on Wnt signaling. Oral SD administration reduced levels of active β-catenin and Wnt targets c-Myc and cyclin D1 in Apc(Min/+) mouse intestinal tissues. Colon cancer cells treated with SDs exhibited reduced Wnt transcriptional activity, as well as reduced nuclear β-catenin localization and subsequent reduction in active-β-catenin levels. Further, we observed a decrease in phosphorylated (inactive) GSK3β in SD-treated mice and colon cancer cells. Expression of constitutively active myristoylated-Akt or inactivation of GSK3β using LiCl attenuated SD-mediated inhibition of Wnt transcriptional activity and active-β-catenin levels. SDs exhibited additive effects with inhibitors of the phosphatidylinositol-3-kinase/Akt/mTOR pathway to induce cytotoxicity. Further, a combination regime of SDs and low-dose rapamycin decreased visible polyps in Apc(Min/+) mice and reduced the levels of Wnt target gene expression and mTOR target activation. SD-mediated inhibition of Akt and Wnt pathways and cytotoxicity in colon cancer cells was dependent upon the activity of protein phosphatase 2A, as shown by reversal of these effects by pretreatment with okadaic acid or calyculin A. Our cumulative findings indicate that SDs inhibit Wnt signaling through a protein phosphatase 2A/Akt/GSK3β-dependent mechanism that may contribute to their chemopreventive effects in intestinal tumorigenesis.
MeSH term(s)	AMP-Activated Protein Kinases/physiology ; Anticarcinogenic Agents/pharmacology ; Cell Line, Tumor ; Colonic Neoplasms/metabolism ; Colonic Neoplasms/prevention & control ; Cytochrome P-450 Enzyme System/genetics ; Down-Regulation ; Glycogen Synthase Kinase 3/physiology ; Glycogen Synthase Kinase 3 beta ; Humans ; Protein Phosphatase 2/physiology ; Proto-Oncogene Proteins c-akt/physiology ; Response Elements ; Signal Transduction ; Sphingolipids/pharmacology ; Tumor Suppressor Protein p53/physiology ; Wnt Signaling Pathway/drug effects ; Wnt Signaling Pathway/physiology
Chemical Substances	Anticarcinogenic Agents ; Sphingolipids ; Tumor Suppressor Protein p53 ; Cytochrome P-450 Enzyme System (9035-51-2) ; GSK3B protein, human (EC 2.7.11.1) ; Glycogen Synthase Kinase 3 beta (EC 2.7.11.1) ; Gsk3b protein, mouse (EC 2.7.11.1) ; Proto-Oncogene Proteins c-akt (EC 2.7.11.1) ; Glycogen Synthase Kinase 3 (EC 2.7.11.26) ; AMP-Activated Protein Kinases (EC 2.7.11.31) ; Protein Phosphatase 2 (EC 3.1.3.16)
Language	English
Publishing date	2012-05-11
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	603134-1
ISSN	1460-2180 ; 0143-3334
ISSN (online)	1460-2180
ISSN	0143-3334
DOI	10.1093/carcin/bgs174
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Article: Mammalian acyl-CoA:lysophosphatidylcholine acyltransferase enzymes

Soupene, Eric / Fyrst, Henrik / Kuypers, Frans A

Proceedings of the National Academy of Sciences of the United States of America. 2008 Jan. 8, v. 105, no. 1

2008

Abstract	The mammalian RBC lacks de novo lipid synthesis but maintains its membrane composition by rapid turnover of acyl moieties at the sn-2 position of phospholipids. Plasma-derived fatty acids are esterified to acyl-CoA by acyl-CoA synthetases and transferred to lysophospholipids by acyl-CoA:lysophospholipid acyltransferases. We report the characterization of three lysophosphatidylcholine (lysoPC) acyltransferases (LPCATs), products of the AYTL1, -2, and -3 genes. These proteins are three members of a LPCAT family, of which all three genes are expressed in an erythroleukemic cell line. Aytl2 mRNA was detected in mouse reticulocytes, and the presence of the product of the human ortholog was confirmed in adult human RBCs. The three murine Aytl proteins generated phosphatidylcholine from long-chain acyl-CoA and lysoPC when expressed in Escherichia coli membranes. Spliced variants of Aytl1, affecting a conserved catalytic motif, were identified. Calcium and magnesium modulated LPCAT activity of both Aytl1 and -2 proteins that exhibit EF-hand motifs at the C terminus. Characterization of the product of the Aytl2 gene as the phosphatidylcholine reacylating enzyme in RBCs represents the identification of a plasma membrane lysophospholipid acyltransferase and establishes the function of a LPCAT protein.
Language	English
Dates of publication	2008-0108
Size	p. 88-93.
Publishing place	National Academy of Sciences
Document type	Article
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
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Article ; Online: A suppressor/enhancer screen in Drosophila reveals a role for wnt-mediated lipid metabolism in primordial germ cell migration.

McElwain, Mark A / Ko, Dennis C / Gordon, Michael D / Fyrst, Henrik / Saba, Julie D / Nusse, Roel

PloS one

2011 Volume 6, Issue 11, Page(s) e26993

Abstract: Wnt proteins comprise a large family of secreted ligands implicated in a wide variety of biological roles. WntD has previously been shown to inhibit the nuclear accumulation of Dorsal/NF-κB protein during embryonic dorsal/ventral patterning and the adult ...

Abstract	Wnt proteins comprise a large family of secreted ligands implicated in a wide variety of biological roles. WntD has previously been shown to inhibit the nuclear accumulation of Dorsal/NF-κB protein during embryonic dorsal/ventral patterning and the adult innate immune response, independent of the well-studied Armadillo/β-catenin pathway. In this paper, we present a novel phenotype for WntD mutant embryos, suggesting that this gene is involved in migration of primordial germ cells (PGC) to the embryonic gonad. Additionally, we describe a genetic suppressor/enhancer screen aimed at identifying genes required for WntD signal transduction, based on the previous observation that maternal overexpression of WntD results in lethally dorsalized embryos. Using an algorithm to narrow down our hits from the screen, we found two novel WntD signaling components: Fz4, a member of the Frizzled family, and the Drosophila Ceramide Kinase homolog, Dcerk. We show here that Dcerk and Dmulk (Drosophila Multi-substrate lipid kinase) redundantly mediate PGC migration. Our data are consistent with a model in which the activity of lipid phosphate phosphatases shapes a concentration gradient of ceramide-1-phosphate (C1P), the product of Dcerk, allowing proper PGC migration.
MeSH term(s)	Animals ; Animals, Genetically Modified ; Blotting, Southern ; Blotting, Western ; Carrier Proteins/genetics ; Carrier Proteins/metabolism ; Cell Movement ; Ceramides/metabolism ; Drosophila/genetics ; Drosophila/growth & development ; Drosophila/metabolism ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism ; Embryo, Nonmammalian/cytology ; Embryo, Nonmammalian/metabolism ; Enhancer Elements, Genetic ; Female ; Genetic Testing ; Germ Cells/physiology ; Immunoprecipitation ; Intracellular Signaling Peptides and Proteins/genetics ; Intracellular Signaling Peptides and Proteins/metabolism ; Lipid Metabolism ; Male ; Phylogeny ; RNA, Messenger/genetics ; Real-Time Polymerase Chain Reaction ; Receptors, G-Protein-Coupled/genetics ; Receptors, G-Protein-Coupled/metabolism ; Reverse Transcriptase Polymerase Chain Reaction ; Signal Transduction ; Suppression, Genetic ; beta Catenin/metabolism
Chemical Substances	CERT protein, Drosophila ; Carrier Proteins ; Ceramides ; Drosophila Proteins ; Intracellular Signaling Peptides and Proteins ; RNA, Messenger ; Receptors, G-Protein-Coupled ; WntD protein, Drosophila ; beta Catenin ; frizzled protein 4, Drosophila
Language	English
Publishing date	2011-11-01
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0026993
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Article: A rapid fluorescence assay for sphingosine-1-phosphate lyase enzyme activity

Bandhuvula, Padmavathi / Fyrst, Henrik / Saba, Julie D

Journal of lipid research JLR. 2007 Dec., v. 48, no. 12

2007

Abstract	Sphingosine-1-phosphate (S1P) lyase (SPL) catalyzes the conversion of S1P to ethanolamine phosphate and hexadecenal. This enzyme plays diverse roles in physiology and disease and, thus, may be useful as a disease marker and/or drug target. Unfortunately, the radioisotope-based assay currently used to quantify SPL activity is suboptimal. We have devised an assay using a commercially available ω(7-nitro-2-1,3-benzoxadiazol-4-yl)-D-erythro (NBD)-labeled fluorescent substrate. Alternatively, we provide a method for synthesis of the substrate from NBD-sphingosine. Enzyme activity is determined by following the formation of NBD-aldehyde product, which is isolated from unreacted substrate by lipid extraction and quantified after separation by HPLC using a C18 column. A fluorescent NBD-C18-sphingosine internal standard is used to control for extraction efficiency. The reaction is linear over 20 min and total protein concentrations of 20-200 mg/l. The sensitivity of the fluorescence assay is comparable to or better than that of the radioactive assay, and SPL levels as low as 8 pmol/mg/min were readily detected. Semicarbazide, a nonspecific SPL inhibitor, reduced SPL activity in vitro by ~70% using both standard and fluorescence methods. Product inhibition was not observed using ethanolamine phosphate and a commercially available source of hexadecenal. This method is suitable for quantifying SPL activity in a variety of cell and tissue sources.
Language	English
Dates of publication	2007-12
Size	p. 2769-2778.
Publishing place	American Society for Biochemistry and Molecular Biology
Document type	Article
ZDB-ID	80154-9
ISSN	1539-7262 ; 0022-2275
ISSN (online)	1539-7262
ISSN	0022-2275
Database	NAL-Catalogue (AGRICOLA)

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Article: Disruption of sphingolipid metabolism elicits apoptosis-associated reproductive defects in Drosophila.

Phan, Van H / Herr, Deron R / Panton, Dionne / Fyrst, Henrik / Saba, Julie D / Harris, Greg L

Developmental biology

2007 Volume 309, Issue 2, Page(s) 329–341

Abstract: Sphingolipid signaling is thought to regulate apoptosis via mechanisms that are dependent on the concentration of ceramide relative to that of sphingosine-1-phosphate (S1P). This study reports defects in reproductive structures and function that are ... ...

Abstract	Sphingolipid signaling is thought to regulate apoptosis via mechanisms that are dependent on the concentration of ceramide relative to that of sphingosine-1-phosphate (S1P). This study reports defects in reproductive structures and function that are associated with enhanced apoptosis in Drosophila Sply05091 mutants that lack functional S1P lyase and thereby accumulate sphingolipid long chain base metabolites. Analyses of reproductive structures in these adult mutants unmasked multiple abnormalities, including supernumerary spermathecae, degenerative ovaries, and severely reduced testes. TUNEL assessment revealed increased cell death in mutant egg chambers at most oogenic stages and in affected mutant testes. These reproductive abnormalities and elevated gonadal apoptosis were also observed, to varying degrees, in other mutants affecting sphingolipid metabolism. Importantly, the reproductive defects seen in the Sply05091 mutants were ameliorated both by a second site mutation in the lace gene that restores long chain base levels towards normal and by genetic disruption of the proapoptotic genes reaper, hid and grim. These data thus provide the first evidence in Drosophila that accumulated sphingolipids trigger elevated levels of apoptosis via the modulation of known signaling pathways.
MeSH term(s)	Aldehyde-Lyases/genetics ; Aldehyde-Lyases/metabolism ; Animals ; Apoptosis ; Drosophila/enzymology ; Drosophila/genetics ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism ; Female ; Genitalia/abnormalities ; Genitalia/enzymology ; Larva ; Lysophospholipids/metabolism ; Male ; Mutation ; Sphingolipids/metabolism ; Sphingosine/analogs & derivatives ; Sphingosine/metabolism
Chemical Substances	Drosophila Proteins ; Lysophospholipids ; Sphingolipids ; sphingosine 1-phosphate (26993-30-6) ; Aldehyde-Lyases (EC 4.1.2.-) ; sphingosine 1-phosphate lyase (aldolase) (EC 4.1.2.27) ; Sphingosine (NGZ37HRE42)
Language	English
Publishing date	2007-09-15
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1114-9
ISSN	1095-564X ; 0012-1606
ISSN (online)	1095-564X
ISSN	0012-1606
DOI	10.1016/j.ydbio.2007.07.021
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Article: Sphingosine phosphate lyase expression is essential for normal development in Caenorhabditis elegans.

Mendel, Jane / Heinecke, Karie / Fyrst, Henrik / Saba, Julie D

The Journal of biological chemistry

2003 Volume 278, Issue 25, Page(s) 22341–22349

Abstract: Sphingolipids are ubiquitous membrane constituents whose metabolites function as signaling molecules in eukaryotic cells. Sphingosine 1-phosphate, a key sphingolipid second messenger, regulates proliferation, motility, invasiveness, and programmed cell ... ...

Abstract	Sphingolipids are ubiquitous membrane constituents whose metabolites function as signaling molecules in eukaryotic cells. Sphingosine 1-phosphate, a key sphingolipid second messenger, regulates proliferation, motility, invasiveness, and programmed cell death. These effects of sphingosine 1-phosphate and similar phosphorylated sphingoid bases have been observed in organisms as diverse as yeast and humans. Intracellular levels of sphingosine 1-phosphate are tightly regulated by the actions of sphingosine kinase, which is responsible for its synthesis and sphingosine-1-phosphate phosphatase and sphingosine phosphate lyase, the two enzymes responsible for its catabolism. In this study, we describe the cloning of the Caenorhabditis elegans sphingosine phosphate lyase gene along with its functional expression in Saccharomyces cerevisiae. Promoter analysis indicates tissue-specific and developmental regulation of sphingosine phosphate lyase gene expression. Inhibition of C. elegans sphingosine phosphate lyase expression by RNA interference causes accumulation of phosphorylated and unphosphorylated long-chain bases and leads to poor feeding, delayed growth, reproductive abnormalities, and intestinal damage similar to the effects seen with exposure to Bacillus thuringiensis toxin. Our results show that sphingosine phosphate lyase is an essential gene in C. elegans and suggest that the sphingolipid degradative pathway plays a conserved role in regulating animal development.
MeSH term(s)	Amino Acid Sequence ; Animals ; Base Sequence ; Caenorhabditis elegans/enzymology ; Caenorhabditis elegans/genetics ; Caenorhabditis elegans/growth & development ; Cloning, Molecular ; DNA Primers ; Gene Expression Regulation, Developmental/genetics ; Gene Expression Regulation, Enzymologic/genetics ; Humans ; Lysophospholipids ; Mice ; Molecular Sequence Data ; Recombinant Proteins/chemistry ; Recombinant Proteins/metabolism ; Saccharomyces cerevisiae/genetics ; Sequence Alignment ; Sequence Homology, Amino Acid ; Sphingosine/analogs & derivatives ; Sphingosine/chemistry ; Sphingosine/genetics
Chemical Substances	DNA Primers ; Lysophospholipids ; Recombinant Proteins ; sphingosine 1-phosphate (26993-30-6) ; Sphingosine (NGZ37HRE42)
Language	English
Publishing date	2003-04-07
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M302857200
Database	MEDical Literature Analysis and Retrieval System OnLINE

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