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Neutral sphingomyelinase: Localization in rat liver nuclei and involvement in regeneration/proliferation

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Abstract

We have studied the localization of neutral sphingomyelinase (N-SMase) in rat liver nuclei. The levels of neutral sphingomyelinase in regenerating liver nuclei were also assessed.

We found that rat liver nuclei contain a sphingomyelinase having a pH optima of 7.2 and a kDa of 92. In intact nuclei, neutral sphingomyelinase was associated predominantly with the nuclear envelope. In regenerating/proliferating rat liver (during DNA synthesis), neutral sphingomyelinase was translocated from the nuclear envelope to the nuclear matrix. The levels of sphingomyelin in whole nuclei decreased in reverse proportion to an increase in the levels of neutral sphingomyelinase. By contrast, there was a corresponding increase in the levels of ceramide and sphingosine during cell regeneration/proliferation. Thus, endogenous nuclear neutral sphingomyelinase may play a role in the regulation of sphingomyelin levels and in relevant signal transduction reactions involving cell regeneration/proliferation. The potential significance of ceramide generation may be aimed at programmed cell death to allow the regeneration of liver mediated via target proteins such as, ceramide activated protein kinases/phospholipases or other unknown mechanisms.

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Abbreviations

N-SMase:

neutral sphingomyelinase

A-SMase:

acid sphingomyelinase

References

  1. Chatterjee S: Neutral Sphingomyelinase. Adv Lipid Res 26: 25–48, 1993

    PubMed  Google Scholar 

  2. Spence MW, Callahan JW: The Niemann-Pick group of diseases. In: C.R. Scriver, A.L. Beaudet, W.S. Sly and D. Valle (eds). The Metabolic Basis of Inherited Disease. McGraw-Hill, New York, 1989, pp 1655–1676

    Google Scholar 

  3. Ghosh P, Chatterjee S: The Effects of Gentamicin on Sphingomyelinase Activity in Cultured Human Renal Proximal Tubular Cell. J Biol Chem 262: 12550–12556, 1987

    PubMed  Google Scholar 

  4. Filippova GN, Borovkova OV, Alessenko AV: Comparison of Lipid Metabolism in Rat Liver Nuclei and Cells Under Conditions of Cycloheximide-Induced Superexpression of Nuclear Oncogenes. Biochemia (Russia) English translation 56(5): 611–619, 1991

    Google Scholar 

  5. Alessenko AV, Burlanova EB, Pantaz EA: Effect of Sphingomyelin on the RNA Polymerase Activity in Cell Nuclei of Normal and Regenerating Rat Liver. Biokhimiya 49(4): 621–628, 1984

    Google Scholar 

  6. Hannun YA: The Sphingomyelin Cycle and the Second Messenger Function of Ceramide. J Biol Chem 269: 3125–3128, 1994

    PubMed  Google Scholar 

  7. Higgins GM, Anderson RM: Experimental Pathology of the Liver. Arch Pathol 12: 186–202, 1931

    Google Scholar 

  8. Blobel G, Potter VR: Nuclei from Rat Liver: Isolation Method that Combines Purity with High yield. Science 154(757): 1662–1665, 1966

    PubMed  Google Scholar 

  9. Hostetler KX, Yazaki PI: The subcellular localization of N-SMase in Rat Liver. J Lipid Res 20(4): 456–463, 1979

    PubMed  Google Scholar 

  10. Chatterjee S, Ghosh N: Neutral Sphingomyelinase from Human Urine. J Biol Chem 264: 12554–12561, 1989

    PubMed  Google Scholar 

  11. Bligh EG, Dyer WJ: A Rapid Method of Total Lipid Extraction and Purification. Can J Biochem Physiol 37: 911–917, 1959

    PubMed  Google Scholar 

  12. Kim MY, Linardic C, Obeid L, Hannun YA: Identification of sphingomyelin turnover as an effect of mechanism for the action of tumor necrosis factor-α and gamma interferon. J Biol Chem 266: 484–489, 1991

    PubMed  Google Scholar 

  13. Mathias S, Dressler KA, Kolesnick RN: Characterization of a ceramide-activated protein kinase. Proc Natl Acad Sci USA 88: 10009–10013, 1992

    Google Scholar 

  14. Shutze S, Potthoff K, Machleidt T, Berkovic D, Woegmann K, Kronke M: TNF Activates NF-kappa B by Phosphatidylcholine-Specific Phospholipase C-Induced ‘Acidic’ Sphingomyelin breakdown. Cell 7(5): 765–776, 1992

    Google Scholar 

  15. Chatterjee S: Neutral Sphingomyelinase Action Stimulates Signal Transduction of Tumor Necrosis Factor-α in the Synthesis of Cholesteryl Esters in Human Fibroblasts. J Biol Chem 269: 879–882, 1994

    PubMed  Google Scholar 

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Author notes

  1. Alice Alessenko

    Present address: Institute of Chemical Physics, Russian Academy of Sciences, 117977, Moscow, Russia

Authors and Affiliations

  1. Department of Pediatrics, Johns Hopkins University, 600 N. Woolfe Street, 21287-3654, Baltimore, MD, USA

    Alice Alessenko & Subroto Chatterjee

Authors
  1. Alice Alessenko
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  2. Subroto Chatterjee
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Alessenko, A., Chatterjee, S. Neutral sphingomyelinase: Localization in rat liver nuclei and involvement in regeneration/proliferation. Mol Cell Biochem 143, 169–174 (1995). https://doi.org/10.1007/BF01816950

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  • DOI: https://doi.org/10.1007/BF01816950

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