Role and Function of Sphingomyelin Biosynthesis in the Development of Cancer

被引:52
作者
D'Angelo, Giovanni [1 ]
Moorthi, Sitapriya [2 ]
Luberto, Chiara [2 ]
机构
[1] Natl Res Council Italy, Inst Prot Biochem, Naples, Italy
[2] SUNY Stony Brook, Dept Physiol & Biophys, Stony Brook, NY 11794 USA
来源
SPHINGOLIPIDS IN CANCER | 2018年 / 140卷
关键词
CERAMIDE TRANSPORT PROTEIN; SYNTHASE; ACTIVITY; PORE-FORMING TOXIN; LIPID RAFTS; ENDOPLASMIC-RETICULUM; CELL-PROLIFERATION; DIFFERENTIAL LOCALIZATION; NONVESICULAR TRAFFICKING; SPHINGOLIPID METABOLISM; MEMBRANE SPHINGOMYELIN;
D O I
10.1016/bs.acr.2018.04.009
中图分类号
R73 [肿瘤学];
学科分类号
100214 ;
摘要
Sphingomyelin (SM) biosynthesis represents a complex, finely regulated process, mostly occurring in vertebrates. It is intimately linked to lipid transport and it is ultimately carried out by two enzymes, SM synthase 1 and 2, selectively localized in the Golgi and plasma membrane. In the course of the SM biosynthetic reaction, various lipids are metabolized. Because these lipids have both structural and signaling functions, the SM biosynthetic process has the potential to affect diverse important cellular processes (such as cell proliferation, cell survival, and migration). Thus defects in SM biosynthesis might directly or indirectly impact the normal physiology of the cell and eventually of the organism. In this chapter, we will focus on evidence supporting a role for SM biosynthesis in specific cellular functions and how its dysregulation can affect neoplastic transformation.
引用
收藏
页码:61 / 96
页数:36
相关论文
共 153 条
[1]   A Role for Sphingomyelin-Rich Lipid Domains in the Accumulation of Phosphatidylinositol-4,5-Bisphosphate to the Cleavage Furrow during Cytokinesis [J].
Abe, Mitsuhiro ;
Makino, Asami ;
Hullin-Matsuda, Francoise ;
Kamijo, Keiju ;
Ohno-Iwashita, Yoshiko ;
Hanada, Kentaro ;
Mizuno, Hideaki ;
Miyawaki, Atsushi ;
Kobayashi, Toshihide .
MOLECULAR AND CELLULAR BIOLOGY, 2012, 32 (08) :1396-1407
[2]   Protection by D609 Through Cell-Cycle Regulation After Stroke [J].
Adibhatla, Rao Muralikrishna ;
Hatcher, James F. .
MOLECULAR NEUROBIOLOGY, 2010, 41 (2-3) :206-217
[3]   Nuclear sphingomyelin-synthase and protein kinase Cδ in melanoma cells [J].
Albi, E ;
La Porta, CAM ;
Cataldi, S ;
Magni, MV .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 2005, 438 (02) :156-161
[4]   RESYNTHESIS OF SPHINGOMYELIN FROM PLASMA-MEMBRANE PHOSPHATIDYLCHOLINE IN BHK CELLS TREATED WITH STAPHYLOCOCCUS-AUREUS SPHINGOMYELINASE [J].
ALLAN, D ;
QUINN, P .
BIOCHEMICAL JOURNAL, 1988, 254 (03) :765-771
[5]   Shaping up the membrane: diacylglycerol coordinates spatial orientation of signaling [J].
Almena, Maria ;
Merida, Isabel .
TRENDS IN BIOCHEMICAL SCIENCES, 2011, 36 (11) :593-603
[6]   Regulation of Cell Migration by Sphingomyelin Synthases: Sphingomyelin in Lipid Rafts Decreases Responsiveness to Signaling by the CXCL12/CXCR4 Pathway [J].
Asano, Satoshi ;
Kitatani, Kazuyuki ;
Taniguchi, Makoto ;
Hashimoto, Mayumi ;
Zama, Kota ;
Mitsutake, Susumu ;
Igarashi, Yasuyuki ;
Takeya, Hiroyuki ;
Kigawa, Junzo ;
Hayashi, Akira ;
Umehara, Hisanori ;
Okazaki, Toshiro .
MOLECULAR AND CELLULAR BIOLOGY, 2012, 32 (16) :3242-3252
[7]   Fluorescent annexin A1 reveals dynamics of ceramide platforms in living cells [J].
Babiychuk, Eduard B. ;
Monastyrskaya, Katia ;
Draeger, Annette .
TRAFFIC, 2008, 9 (10) :1757-1775
[8]   A Toxin-based Probe Reveals Cytoplasmic Exposure of Golgi Sphingomyelin [J].
Bakrac, Biserka ;
Kladnik, Ales ;
Macek, Peter ;
McHaffie, Gavin ;
Werner, Andreas ;
Lakey, Jeremy H. ;
Anderluh, Gregor .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2010, 285 (29) :22186-22195
[9]   Sphingomyelin and sphingomyelin synthase (SMS) in the malignant transformation of glioma cells and in 2-hydroxyoleic acid therapy [J].
Barcelo-Coblijn, Gwendolyn ;
Laura Martin, Maria ;
de Almeida, Rodrigo F. M. ;
Antonia Noguera-Salva, Maria ;
Marcilla-Etxenike, Amaia ;
Guardiola-Serrano, Francisca ;
Lueth, Anja ;
Kleuser, Burhard ;
Halver, John E. ;
Escriba, Pablo V. .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2011, 108 (49) :19569-19574
[10]   Lipid phase coexistence favors membrane insertion of equinatoxin-II, a pore-forming toxin from Actinia equina [J].
Barlic, A ;
Gutiérrez-Aguirre, I ;
Caaveiro, JMM ;
Cruz, A ;
Ruiz-Argüello, MB ;
Pérez-Gil, J ;
González-Mañas, JM .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (33) :34209-34216