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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Gene Review: 

Chst10  -  carbohydrate sulfotransferase 10

Mus musculus

Synonyms: AI507003, AU041319, Carbohydrate sulfotransferase 10, HNK-1 sulfotransferase, HNK-1ST, ...
 
 
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Disease relevance of Chst10

  • We previously showed that murine polyomavirus mutants that lack both middle T (MT) and small T (ST) functions have a severe pleiotropic defect in early and late viral gene expression as well as genome amplification [1].
  • Isolated alterations such as extrasystolia, 1st degree atrioventricular block, arrhythmia and ST elevation were observed in normal as well as infected mice [2].
 

High impact information on Chst10

  • In this study, we found that GlcAT-S mRNA was expressed at higher levels in the kidney than in the brain, but that both GlcAT-P and HNK-1 sulfotransferase mRNAs, which were expressed at high levels in the brain, were not detected in the kidney [3].
  • The cDNAs encoding beta1,3-glucuronyltransferase (GlcAT-P) and HNK-1 sulfotransferase (HNK-1ST) have been recently cloned [4].
  • These findings reveal alterations in ST-/- mice that differ from EEG abnormalities of mice deficient in the HNK-1 carrier molecule tenascin-R [5].
  • Morphological analysis revealed a decreased density of parvalbumin-positive interneurons in the hippocampal CA3 subfield of ST-/- mice, which may contribute to the observed changes in networks oscillations [5].
  • ST-/- mice had amplitudes of auditory-evoked potentials similar to control mice, but the latencies of their hippocampal responses were shorter [5].
 

Biological context of Chst10

  • However, basal synaptic transmission in pyramidal cells in the CA1 region of the hippocampus was increased and long-term potentiation evoked by theta-burst stimulation was reduced in ST mutants [6].
  • Failure to observe a severe phenotype in the ST null mice prompted us to determine the compensatory molecular replacement of SGC by analyzing the carbohydrate of glycolipids and glycoproteins of the ST mutant nervous system [7].
  • This connection explains the pleiotropy of MT and ST effects on transcription and DNA replication [1].
  • What is common to ST and the individual MT signaling pathways is the ability to signal to the polyomavirus enhancer, in particular to the crucial AP-1 and PEA3/ets binding sites [1].
 

Other interactions of Chst10

References

  1. Independent contributions of polyomavirus middle T and small T to the regulation of early and late gene expression and DNA replication. Chen, L., Wang, X., Fluck, M.M. J. Virol. (2006) [Pubmed]
  2. Prevention of electrocardiographic and histopathologic alterations in the murine model of Chagas' disease by preinoculation of an attenuated Trypanosoma cruzi strain. Cuneo, C.A., Molina de Raspi, E., Basombrio, M.A. Rev. Inst. Med. Trop. Sao Paulo (1989) [Pubmed]
  3. A non-sulfated form of the HNK-1 carbohydrate is expressed in mouse kidney. Tagawa, H., Kizuka, Y., Ikeda, T., Itoh, S., Kawasaki, N., Kurihara, H., Onozato, M.L., Tojo, A., Sakai, T., Kawasaki, T., Oka, S. J. Biol. Chem. (2005) [Pubmed]
  4. Biosynthesis of HNK-1 glycans on O-linked oligosaccharides attached to the neural cell adhesion molecule (NCAM): the requirement for core 2 beta 1,6-N-acetylglucosaminyltransferase and the muscle-specific domain in NCAM. Ong, E., Suzuki, M., Belot, F., Yeh, J.C., Franceschini, I., Angata, K., Hindsgaul, O., Fukuda, M. J. Biol. Chem. (2002) [Pubmed]
  5. Increased hippocampal and cortical beta oscillations in mice deficient for the HNK-1 sulfotransferase. Gurevicius, K., Gureviciene, I., Sivukhina, E., Irintchev, A., Schachner, M., Tanila, H. Mol. Cell. Neurosci. (2007) [Pubmed]
  6. Mice deficient for the HNK-1 sulfotransferase show alterations in synaptic efficacy and spatial learning and memory. Senn, C., Kutsche, M., Saghatelyan, A., Bösl, M.R., Löhler, J., Bartsch, U., Morellini, F., Schachner, M. Mol. Cell. Neurosci. (2002) [Pubmed]
  7. HNK-1 sulfotransferase null mice express glucuronyl glycoconjugates and show normal cerebellar granule neuron migration in vivo and in vitro. Chou, D.K., Schachner, M., Jungalwala, F.B. J. Neurochem. (2002) [Pubmed]
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