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  1. Article ; Online: Plant sphingolipids: decoding the enigma of the Sphinx.

    Pata, Mickael O / Hannun, Yusuf A / Ng, Carl K-Y

    The New phytologist

    2009  Volume 185, Issue 3, Page(s) 611–630

    Abstract: Sphingolipids are a ubiquitous class of lipids present in a variety of organisms including eukaryotes and bacteria. In the last two decades, research has focused on characterizing the individual species of this complex family of lipids, which has led to ... ...

    Abstract Sphingolipids are a ubiquitous class of lipids present in a variety of organisms including eukaryotes and bacteria. In the last two decades, research has focused on characterizing the individual species of this complex family of lipids, which has led to a new field of research called 'sphingolipidomics'. There are at least 500 (and perhaps thousands of) different molecular species of sphingolipids in cells, and in Arabidopsis alone it has been reported that there are at least 168 different sphingolipids. Plant sphingolipids can be divided into four classes: glycosyl inositol phosphoceramides (GIPCs), glycosylceramides, ceramides, and free long-chain bases (LCBs). Numerous enzymes involved in plant sphingolipid metabolism have now been cloned and characterized, and, in general, there is broad conservation in the way in which sphingolipids are metabolized in animals, yeast and plants. Here, we review the diversity of sphingolipids reported in the literature, some of the recent advances in our understanding of sphingolipid metabolism in plants, and the physiological roles that sphingolipids and sphingolipid metabolites play in plant physiology.
    MeSH term(s) Animals ; Ceramides/chemistry ; Ceramides/metabolism ; Plants/metabolism ; Sphingolipids/chemistry ; Sphingolipids/classification ; Sphingolipids/metabolism
    Chemical Substances Ceramides ; Sphingolipids
    Language English
    Publishing date 2009-12-16
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 208885-x
    ISSN 1469-8137 ; 0028-646X
    ISSN (online) 1469-8137
    ISSN 0028-646X
    DOI 10.1111/j.1469-8137.2009.03123.x
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Bonn / Germany

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  2. Article: Plant sphingolipids: decoding the enigma of the Sphinx

    Pata, Mickael O / Hannun, Yusuf A / Ng, Carl K.Y

    New phytologist. 2010 Feb., v. 185, no. 3

    2010  

    Abstract: Sphingolipids are a ubiquitous class of lipids present in a variety of organisms including eukaryotes and bacteria. In the last two decades, research has focused on characterizing the individual species of this complex family of lipids, which has led to ... ...

    Abstract Sphingolipids are a ubiquitous class of lipids present in a variety of organisms including eukaryotes and bacteria. In the last two decades, research has focused on characterizing the individual species of this complex family of lipids, which has led to a new field of research called 'sphingolipidomics'. There are at least 500 (and perhaps thousands of) different molecular species of sphingolipids in cells, and in Arabidopsis alone it has been reported that there are at least 168 different sphingolipids. Plant sphingolipids can be divided into four classes: glycosyl inositol phosphoceramides (GIPCs), glycosylceramides, ceramides, and free long-chain bases (LCBs). Numerous enzymes involved in plant sphingolipid metabolism have now been cloned and characterized, and, in general, there is broad conservation in the way in which sphingolipids are metabolized in animals, yeast and plants. Here, we review the diversity of sphingolipids reported in the literature, some of the recent advances in our understanding of sphingolipid metabolism in plants, and the physiological roles that sphingolipids and sphingolipid metabolites play in plant physiology.
    Keywords sphingolipids
    Language English
    Dates of publication 2010-02
    Size p. 611-630.
    Publisher Blackwell Publishing Ltd
    Publishing place Oxford, UK
    Document type Article
    ZDB-ID 208885-x
    ISSN 1469-8137 ; 0028-646X
    ISSN (online) 1469-8137
    ISSN 0028-646X
    DOI 10.1111/j.1469-8137.2009.03123.x
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Bonn / Germany

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  3. Article: Molecular cloning and characterization of OsCDase, a ceramidase enzyme from rice

    Pata, Mickael O / Wu, Bill X / Bielawski, Jacek / Xiong, Tou Cheu / Hannun, Yusuf A / Ng, Carl K.-Y

    Plant journal. 2008 Sept., v. 55, no. 6

    2008  

    Abstract: Sphingolipids are a structurally diverse group of molecules based on long-chain sphingoid bases that are found in animal, fungal and plant cells. In contrast to the situation in animals and yeast, much less is known about the spectrum of sphingolipid ... ...

    Abstract Sphingolipids are a structurally diverse group of molecules based on long-chain sphingoid bases that are found in animal, fungal and plant cells. In contrast to the situation in animals and yeast, much less is known about the spectrum of sphingolipid species in plants and the roles they play in mediating cellular processes. Here, we report the cloning and characterization of a plant ceramidase from rice (Oryza sativa spp. Japonica cv. Nipponbare). Sequence analysis suggests that the rice ceramidase (OsCDase) is similar to mammalian neutral ceramidases. We demonstrate that OsCDase is a bona fide ceramidase by heterologous expression in the yeast double knockout mutant Δypc1Δydc1 that lacks the yeast ceramidases YPC1p and YDC1p. Biochemical characterization of OsCDase showed that it exhibited classical Michaelis-Menten kinetics, with optimum activity between pH 5.7 and 6.0. OsCDase activity was enhanced in the presence of Ca²⁺, Mg²⁺, Mn²⁺ and Zn²⁺, but inhibited in the presence of Fe²⁺. OsCDase appears to use ceramide instead of phytoceramide as a substrate. Subcellular localization showed that OsCDase is localized to the endoplasmic reticulum and Golgi, suggesting that these organelles are sites of ceramide metabolism in plants.
    Keywords rice
    Language English
    Dates of publication 2008-09
    Size p. 1000-1009.
    Publisher Blackwell Publishing Ltd
    Publishing place Oxford, UK
    Document type Article
    ZDB-ID 1088037-9
    ISSN 1365-313X ; 0960-7412
    ISSN (online) 1365-313X
    ISSN 0960-7412
    DOI 10.1111/j.1365-313X.2008.03569.x
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Bonn / Germany

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  4. Article ; Online: Molecular cloning and characterization of OsCDase, a ceramidase enzyme from rice.

    Pata, Mickael O / Wu, Bill X / Bielawski, Jacek / Xiong, Tou Cheu / Hannun, Yusuf A / Ng, Carl K-Y

    The Plant journal : for cell and molecular biology

    2008  Volume 55, Issue 6, Page(s) 1000–1009

    Abstract: Summary: Sphingolipids are a structurally diverse group of molecules based on long-chain sphingoid bases that are found in animal, fungal and plant cells. In contrast to the situation in animals and yeast, much less is known about the spectrum of ... ...

    Abstract Summary: Sphingolipids are a structurally diverse group of molecules based on long-chain sphingoid bases that are found in animal, fungal and plant cells. In contrast to the situation in animals and yeast, much less is known about the spectrum of sphingolipid species in plants and the roles they play in mediating cellular processes. Here, we report the cloning and characterization of a plant ceramidase from rice (Oryza sativa spp. Japonica cv. Nipponbare). Sequence analysis suggests that the rice ceramidase (OsCDase) is similar to mammalian neutral ceramidases. We demonstrate that OsCDase is a bona fide ceramidase by heterologous expression in the yeast double knockout mutant Deltaypc1Deltaydc1 that lacks the yeast ceramidases YPC1p and YDC1p. Biochemical characterization of OsCDase showed that it exhibited classical Michaelis-Menten kinetics, with optimum activity between pH 5.7 and 6.0. OsCDase activity was enhanced in the presence of Ca(2+), Mg(2+), Mn(2+) and Zn(2+), but inhibited in the presence of Fe(2+). OsCDase appears to use ceramide instead of phytoceramide as a substrate. Subcellular localization showed that OsCDase is localized to the endoplasmic reticulum and Golgi, suggesting that these organelles are sites of ceramide metabolism in plants.
    MeSH term(s) Amidohydrolases/genetics ; Amidohydrolases/metabolism ; Ceramidases ; Ceramides/metabolism ; Cloning, Molecular ; DNA, Complementary/genetics ; Endoplasmic Reticulum/metabolism ; Gene Expression ; Genes, Plant ; Golgi Apparatus/metabolism ; Oryza/enzymology ; Oryza/genetics ; Phylogeny ; Plant Proteins/genetics ; Plant Proteins/metabolism ; RNA, Plant/genetics ; Saccharomyces cerevisiae/enzymology ; Saccharomyces cerevisiae/genetics ; Sequence Alignment ; Sequence Analysis, DNA ; Sphingolipids/metabolism ; Substrate Specificity
    Chemical Substances Ceramides ; DNA, Complementary ; Plant Proteins ; RNA, Plant ; Sphingolipids ; Amidohydrolases (EC 3.5.-) ; Ceramidases (EC 3.5.1.23)
    Language English
    Publishing date 2008-06-10
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 1088037-9
    ISSN 1365-313X ; 0960-7412
    ISSN (online) 1365-313X
    ISSN 0960-7412
    DOI 10.1111/j.1365-313X.2008.03569.x
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

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    In stock of ZB MED Bonn / Germany

    Z 6071: Show issues

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

    Inter-library loan at ZB MED

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