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Gene Review

SPTLC2  -  serine palmitoyltransferase, long chain...

Homo sapiens

Synonyms: HSN1C, KIAA0526, LCB 2, LCB2, LCB2A, ...
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Disease relevance of SPTLC2


High impact information on SPTLC2

  • Although in HSN1 lymphoblasts, the C133Y and C133W mutations do not alter the steady-state levels of LCB1 and LCB2 subunits, they result in reduced SPT activity and sphingolipid synthesis [3].
  • These results indicated that the LCB1 subunit is most likely an integral protein having a single transmembrane domain with a lumenal orientation of its N terminus in the endoplasmic reticulum and that the LCB1 subunit is indispensable for the maintenance of the LCB2 subunit in mammalian cells [4].
  • The first four exons and the last exon are common to the LCB2 and LCB3 isoforms [2].
  • SPT2 was localized in both nuclei and cytoplasm of the adrenomedullary chromaffin cells, whereas SPT1 was primarily cytoplasmic [5].
  • In addition, we observed SPT1 and SPT2 immunoreactivity in reactive stromal fibroblasts surrounding the carcinoma cells of some of the tumors [6].

Biological context of SPTLC2

  • Recent work has also revealed that diverse agonists and stresses (cytokines, UV light, glucocorticoids, heat shock and toxic compounds) modulate SPT activity by induction of SPTLC2 gene transcription and/or post-translational modification [7].
  • Interestingly, there was far less LCB2 in LY-B cells than in wild-type cells, and the amount of LCB2 in LY-B cells was restored to the wild-type level by transfection with LCB1 cDNA [4].

Anatomical context of SPTLC2


Associations of SPTLC2 with chemical compounds


Physical interactions of SPTLC2

  • The endogenous LCB2 protein was co-purified with the tagged LCB1 protein in purification of SPT [9].

Other interactions of SPTLC2

  • Here we report the identification of a novel, third, SPT subunit (SPTLC3) that shows 68% homology to the SPTLC2 subunit [10].

Analytical, diagnostic and therapeutic context of SPTLC2

  • Likewise, Lcb2 protein levels (by Western blot analysis), as well as SPT activity, increase in parallel with the increased LCB2 mRNA [11].
  • In CHK, transcripts for both LCB1 (3.0 kb) and LCB2 (2.3 kb) are evident by Northern blot analysis, and UVB exposure (23 mJ/cm2) induces a delayed 1.8 to 3.3-fold increase in LCB2 mRNA levels (P < 0.01) 48 h after treatment versus non-irradiated control cells [11].
  • Primary rat neuronal cell cultures express predominantly the brain specific LCB2 isoform, whereas primary rat cultures of glia express only the LCB3 isoform, suggesting that expression of the brain-specific LCB2 form is limited to neurons [2].
  • Preliminary cytologic diagnoses at endoscopy included 1 SPTP 2 low-grade neoplasms, and 3 pancreatic endocrine tumors [12].


  1. Exclusion of serine palmitoyltransferase long chain base subunit 2 (SPTLC2) as a common cause for hereditary sensory neuropathy. Dawkins, J.L., Brahmbhatt, S., Auer-Grumbach, M., Wagner, K., Hartung, H.P., Verhoeven, K., Timmerman, V., De Jonghe, P., Kennerson, M., LeGuern, E., Nicholson, G.A. Neuromuscul. Disord. (2002) [Pubmed]
  2. Clathrin light chain B: gene structure and neuron-specific splicing. Stamm, S., Casper, D., Dinsmore, J., Kaufmann, C.A., Brosius, J., Helfman, D.M. Nucleic Acids Res. (1992) [Pubmed]
  3. Hereditary sensory neuropathy type 1 mutations confer dominant negative effects on serine palmitoyltransferase, critical for sphingolipid synthesis. Bejaoui, K., Uchida, Y., Yasuda, S., Ho, M., Nishijima, M., Brown, R.H., Holleran, W.M., Hanada, K. J. Clin. Invest. (2002) [Pubmed]
  4. Localization, topology, and function of the LCB1 subunit of serine palmitoyltransferase in mammalian cells. Yasuda, S., Nishijima, M., Hanada, K. J. Biol. Chem. (2003) [Pubmed]
  5. Characterization of serine palmitoyltransferase in normal human tissues. Batheja, A.D., Uhlinger, D.J., Carton, J.M., Ho, G., D'Andrea, M.R. J. Histochem. Cytochem. (2003) [Pubmed]
  6. Enhanced serine palmitoyltransferase expression in proliferating fibroblasts, transformed cell lines, and human tumors. Carton, J.M., Uhlinger, D.J., Batheja, A.D., Derian, C., Ho, G., Argenteri, D., D'Andrea, M.R. J. Histochem. Cytochem. (2003) [Pubmed]
  7. Regulation of de novo sphingolipid biosynthesis and the toxic consequences of its disruption. Linn, S.C., Kim, H.S., Keane, E.M., Andras, L.M., Wang, E., Merrill, A.H. Biochem. Soc. Trans. (2001) [Pubmed]
  8. Nicotinamide increases biosynthesis of ceramides as well as other stratum corneum lipids to improve the epidermal permeability barrier. Tanno, O., Ota, Y., Kitamura, N., Katsube, T., Inoue, S. Br. J. Dermatol. (2000) [Pubmed]
  9. Purification of the serine palmitoyltransferase complex responsible for sphingoid base synthesis by using affinity peptide chromatography techniques. Hanada, K., Hara, T., Nishijima, M. J. Biol. Chem. (2000) [Pubmed]
  10. Cloning and Initial Characterization of a New Subunit for Mammalian Serine-palmitoyltransferase. Hornemann, T., Richard, S., R??tti, M.F., Wei, Y., von Eckardstein, A. J. Biol. Chem. (2006) [Pubmed]
  11. UVB irradiation up-regulates serine palmitoyltransferase in cultured human keratinocytes. Farrell, A.M., Uchida, Y., Nagiec, M.M., Harris, I.R., Dickson, R.C., Elias, P.M., Holleran, W.M. J. Lipid Res. (1998) [Pubmed]
  12. Endoscopic ultrasound-guided fine-needle aspiration cytology diagnosis of solid-pseudopapillary tumor of the pancreas: a rare neoplasm of elusive origin but characteristic cytomorphologic features. Bardales, R.H., Centeno, B., Mallery, J.S., Lai, R., Pochapin, M., Guiter, G., Stanley, M.W. Am. J. Clin. Pathol. (2004) [Pubmed]
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