Degradation of glycosphingolipids in oyster: ceramide glycanase and ceramidase in the hepatopancreas of oyster, Crassostrea virginica

Degradation of glycosphingolipids in oyster: ceramide glycanase and ceramidase in the... The hepatopancreas of oyster, Crassostrea virginica, was found to contain two unique glycosphingolipid (GSL) cleaving enzymes, ceramide glycanase (CGase) and ceramidase. These two enzymes were found to be tightly associated together through the consecutive purification steps including gel filtration, hydrophobic interaction and cation-exchange chromatographies. They were separated only by preparatory SDS-PAGE. The purified CGase was found to have a molecular mass of 52 kDa and pH optimum of 3.2–3.3. This enzyme prefers to hydrolyze the acidic GSLs, II3SO3LacCer and gangliosides over the neutral GSLs. Oyster ceramidase was found to have a molecular mass of 88 kDa and pH optimum of 4–4.5. Since oyster ceramidase greatly prefers ceramides with C6 to C8 fatty acids, C6-ceramide (N-hexanoyl-D-sphingosine) was used as the substrate for its purification and characterization. The oyster acid ceramidase also catalyzed the synthesis of ceramide from a sphingosine and a fatty acid. For the synthesis, C16 and C18 fatty acids were the best precursors. The amino acid sequences of the two cyanogenbromide peptides derived from the purified ceramidase were found to have similarities to those of several neutral and alkaline ceramidases reported. The tight association of CGase and ceramidase may indicate that CGase in oyster hepatopancreas acts as a vehicle to release ceramide from GSLs for subsequent generation of sphingosines and fatty acids by ceramidase to serve as signaling factors and energy source. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Glycoconjugate Journal Springer Journals

Degradation of glycosphingolipids in oyster: ceramide glycanase and ceramidase in the hepatopancreas of oyster, Crassostrea virginica

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Publisher
Springer US
Copyright
Copyright © 2017 by Springer Science+Business Media, LLC
Subject
Life Sciences; Biochemistry, general; Pathology
ISSN
0282-0080
eISSN
1573-4986
D.O.I.
10.1007/s10719-017-9802-7
Publisher site
See Article on Publisher Site

Abstract

The hepatopancreas of oyster, Crassostrea virginica, was found to contain two unique glycosphingolipid (GSL) cleaving enzymes, ceramide glycanase (CGase) and ceramidase. These two enzymes were found to be tightly associated together through the consecutive purification steps including gel filtration, hydrophobic interaction and cation-exchange chromatographies. They were separated only by preparatory SDS-PAGE. The purified CGase was found to have a molecular mass of 52 kDa and pH optimum of 3.2–3.3. This enzyme prefers to hydrolyze the acidic GSLs, II3SO3LacCer and gangliosides over the neutral GSLs. Oyster ceramidase was found to have a molecular mass of 88 kDa and pH optimum of 4–4.5. Since oyster ceramidase greatly prefers ceramides with C6 to C8 fatty acids, C6-ceramide (N-hexanoyl-D-sphingosine) was used as the substrate for its purification and characterization. The oyster acid ceramidase also catalyzed the synthesis of ceramide from a sphingosine and a fatty acid. For the synthesis, C16 and C18 fatty acids were the best precursors. The amino acid sequences of the two cyanogenbromide peptides derived from the purified ceramidase were found to have similarities to those of several neutral and alkaline ceramidases reported. The tight association of CGase and ceramidase may indicate that CGase in oyster hepatopancreas acts as a vehicle to release ceramide from GSLs for subsequent generation of sphingosines and fatty acids by ceramidase to serve as signaling factors and energy source.

Journal

Glycoconjugate Journal – Springer Journals

Published: Oct 16, 2017

References

  • Enzymatic hydrolysis of glycosphingolipids
    Li, YT; Li, SC
  • A unique glycolipid-splitting enzyme (ceramide glycanase) from leech cleaving the linkage between the oligosaccharide and the ceramide
    Li, SC; DeGasperi, R; Muldrey, JE; Li, YT
  • Ceramide glycanase from earthworm, Lumbricus terrestris
    Carter, BZ; Li, SC; Li, YT
  • Analysis of glycosphingolipids by fluorophore-assisted carbohydrate electrophoresis using ceramide glycanase from Mercenaria mercenaria
    Basu, SS; Dastgheib-Hosseini, S; Hoover, G; Li, Z; Basu, S
  • Purification, characterization and cDNA cloning of a novel acidic endoglycoceramidase from the jellyfish, Cyanea nozakii
    Horibata, Y; Okino, N; Ichinose, S; Omori, A; Ito, M
  • Unique catabolic pathway of glycosphingolipids in a hydrozoan, Hydra magnipapillata, involving endoglycoceramidase
    Horibata, Y; Sakaguchi, K; Okino, N; Iida, H; Inagaki, M; Fujisawa, T; Hama, Y; Ito, M
  • A novel glycolipid-degrading enzyme cleaves the linkage between the oligosaccharide and ceramide of neutral and acidic glycosphingolipids
    Ito, M; Yamagata, T
  • On the presence of ceramide glycanase activity in mammalian tissues
    Li, YT; Li, SC
  • Ceramidases, roles in sphingolipid metabolism and in health and disease
    Coant, N; Sakamoto, W; Mao, C; Hannun, YA
  • Enzymatic hydrolysis and synthesis of ceramides
    Gatt, S
  • Molecular cloning and characterization of a full-length complementary DNA encoding human acid ceramidase
    Koch, J; Gaertner, S; Li, CM; Quintern, LE; Bernardo, K; Levran, O; Schnabel, D; Desnick, RJ; Schuchman, EH; Sandhoff, K
  • Cloning and characterization of the full-length cDNA and genomic sequencing encoding murine acid ceramidase
    Li, CM; Hong, SB; Kopal, G; He, X; Linke, T; Hou, WS; Koch, J; Gatt, S; Sandhoff, K; Schuchman, EH
  • Ceramide deficiency in Farber’s disease (Lipogranulomatosis)
    Sugita, M; Dulaney, JT; Moser, HW
  • Purification and biochemical characterization of membrane bound epidermal ceramidases from guinea pig skin
    Yada, Y; Higuchi, K; Imokawa, G
  • Purification and characterization of a membrane-bound nonlysosomal ceramidase from rat brain
    Bawab, SE; Bielawska, A; Hannun, YA
  • Molecular cloning and characterization of a human mitochondrial ceramidase
    Bawab, SE; Roddy, P; Qian, T; Bielawska, A; Lemasters, JJ; Hannun, YA
  • Purification and characterization of a neutral ceramidase from mouse liver
    Tani, M; Okino, N; Mitsutake, S; Tanigawa, T; Izu, H; Ito, M
  • Molecular cloning of the full-length cDNA encoding mouse neutral ceramidase
    Tani, M; Okino, N; Mori, K; Tanigawa, T; Izu, H; Ito, M
  • Enzymatic hydrolysis of sphingolipids. VIII. Further purification and properties of rat brain ceramidase
    Yavin, E; Gatt, S
  • Purification and characterization of a novel ceramidase from Pseudomonas aeruginosa
    Okino, N; Tani, M; Imayama, S; Ito, M
  • Molecular cloning, sequencing, and expression of the gene encoding alkaline ceramidase from Pseudomonas aeruginosa: cloning of a ceramidase homoloque from Mycobacterium tubercurosis
    Okino, N; Ichinose, S; Omori, A; Imayama, S; Nakamura, T; Ito, M
  • Cloning and characterization of a Saccharomyces cerevisiae alkaline ceramidase with specificity for dihydroceramide
    Mao, C; Xu, R; Bielawska, A; Szulc, ZM; Obeid, L
  • Biomodal regulation of ceramidase by interleukin-1β
    Nikolova-Karakashian, M; Morgan, ET; Alexander, C; Lotta, DC; Merrill, AH
  • Different regulation of sphingomyelinase and ceramidase activities by growth factors and cytokines: imprecation for cellular proliferation and differentiation
    Coroneos, E; Martinez, M; McKenna, S; Kesler, M
  • Comparison of two copper reagents for detection of saturated and unsaturated neutral lipids by charring densitometry
    Baron, CB; Coburn, RF
  • Diphenylamine-aniline-phosphoric acid reagent, a versatile spray reagent for revealing glycoconjugates on thin-layer chromatography plates
    Anderson, K; Li, SC; Li, YT
  • Simplified fluorometric assay for sphingosine bases
    Higgins, TJ
  • A discontinuous and highly porous sodium dodecyl sulfate-polyacrylamide slab gel system of high resolution
    Doucet, JP; Trifaro, JM
  • 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN)- and N-acetylneuraminic acid-cleaving sialidase (KDN-sialidase) and KDN-cleaving hydrolase (KDNase) from the hepatopancreas of oyster, Crassostrea virginica
    Pavlova, NV; Yuziuk, JA; Nakagawa, H; Kiso, M; Li, SC; Li, YT
  • Limited N-terminal sequence analysis
    Matsudaira, P
  • Specific and sensitive assay for alkaline and neutral ceramidase involving C12-NBD-ceramide
    Tani, M; Okino, N; Mitsutake, S; Ito, M
  • A fluorescence-based high-performance liquid chromatograhpic assay to determine acid ceramidase activity
    He, X; Li, CM; Park, JH; Dagan, A; Gatt, S; Schuchman, H
  • Novel enzyme that cleaves N-acyl linkage of ceramidase in various glycosphingo-lipids as well as sphingomyelin to produce their lyso forms
    Ito, M; Kurita, T; Kita, K
  • Reverse hydrolysis reaction of a recombinant alkaline ceramidase of Pseudomonas aeruginosa
    Kita, K; Okino, N; Ito, M
  • Clustal W algorithm: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    Thompson, JD; Higgins, DG; Gibson, TJ

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