The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Subcellular localization and membrane topology of serine palmitoyltransferase, 3-dehydrosphinganine reductase, and sphinganine N-acyltransferase in mouse liver.
Open accessAbstract
Serine palmitoyltransferase, 3-dehydrosphinganine reductase and sphinganine N-acyltransferase are responsible for the first steps in sphingolipid biosynthesis forming 3-oxosphinganine, sphinganine, and dihydroceramide, respectively. We confirmed the localization of these enzymes in the endoplasmic reticulum (ER) using highly purified mouse liver ER and Golgi preparations. Mild digestion of sealed "right-side out" mouse liver ER derived vesicles with different proteolytic enzymes under conditions where latency of mannose-6-phosphatase was 90% produced approximately 60-80% inactivation of serine palmitoyltransferase, 3-dehydrosphinganine reductase, and sphinganine N-acyltransferase activities. These sphingolipid biosynthetic activities (serine palmitoyltransferase, 3-dehydrosphinganine reductase, and sphinganine N-acyltransferase) are not latent, indicating that they face the cytosolic side of the ER, so that substrates have free access to their active sites. Moreover, the membrane-impermeable compound, 4,4'-diisothiocyanostilbene-2,2'-disulfonic acid, which binds to a large number of ER proteins, inhibits serine palmitoyltransferase and sphinganine N-acyltransferase activities by 30-70%.
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Cites
Bremer, E. G., Schlessinger, J., & Hakomori, S. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)35954-9 · Cited by 706
[16] Isolation of subcellular organelles
Storrie, B., & Amadden, E. (1990) · Methods in Enzymology · doi:10.1016/0076-6879(90)82018-w · Cited by 555
Briles, E. B., Li, E., & Kornfeld, S. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)75213-2 · Cited by 220
Cited by
Sphingolipid and Glycosphingolipid Metabolic Pathways in the Era of Sphingolipidomics
Merrill, A. H. (2011) · Chemical Reviews · doi:10.1021/cr2002917 · Cited by 785
Bioactive sphingolipids: metabolism and function
Bartke, N., & Hannun, Y. A. (2009) · Journal of Lipid Research · doi:10.1194/jlr.r800080-jlr200 · Cited by 683
Levy, M., & Futerman, A. H. (2010) · IUBMB Life · doi:10.1002/iub.319 · Cited by 632
“The subcellular location of the CerS proteins is the ER (8, 10, 11, 20, 23, 26, 27), although it should be emphasized that Table 1 Comparison of human CerS”
BackgroundThe sphingolipid salvage pathway in ceramide metabolism and signaling
Kitatani, K., Idkowiak-Baldys, J., & Hannun, Y. A. (2008) · Cellular Signalling · doi:10.1016/j.cellsig.2007.12.006 · Cited by 632
Serine palmitoyltransferase, a key enzyme of sphingolipid metabolism
Hanada, K. (2003) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/s1388-1981(03)00059-3 · Cited by 616
Metadata
- Authors
- Mandon, E. C., Ehses, I., Rother, J., van Echten, G., & Sandhoff, K.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1992-06
- Volume
- 267
- Issue
- 16
- Pages
- 11144-11148
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1536374844
- Cited by
- 346
- References
- 3
- FWCI
- 4.45
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Mandon, E. C., Ehses, I., Rother, J., van Echten, G., & Sandhoff, K. (1992). Subcellular localization and membrane topology of serine palmitoyltransferase, 3-dehydrosphinganine reductase, and sphinganine N-acyltransferase in mouse liver. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(19)49887-6
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