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ALG10  -  ALG10, alpha-1,2-glucosyltransferase

Homo sapiens

Synonyms: ALG10A, Alpha-1,2-glucosyltransferase ALG10-A, Alpha-2-glucosyltransferase ALG10-A, Asparagine-linked glycosylation protein 10 homolog A, DIE2, ...
 
 
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High impact information on ALG10

  • This clinical result is supported by in vitro studies of HERG dofetilide sensitivity by using coexpression of HERG with wild-type and I447V KCR1 cDNAs [1].
  • Examination of the human KCR1 sequence in patients with drug-induced cardiac repolarization defects revealed a sequence variation (the substitution of isoleucine 447 by valine, I447V) that occurs at a reduced frequency (1.1%) relative to a matched control population (7.0%), suggesting that I447V may be an allele for reduced aLQTS susceptibility [1].
  • KCR1 also accelerates the activation of rat EAG K+ channels expressed in Xenopus oocytes or in COS-7 cells [2].
  • Cerebellar granule neurons possess a non-inactivating K+ current, which controls resting membrane potentials and modulates the firing rate by means of muscarinic agonists. kcr1 was cloned from the cerebellar cDNA library by suppression cloning [2].
  • The IKr drug response is modulated by KCR1 in transfected cardiac and noncardiac cell lines [3].
 

Anatomical context of ALG10

  • KCR1 is a novel protein with 12 putative transmembrane domains and enhances the functional expression of the cerebellar non-inactivating K+ current in Xenopus oocytes [2].
 

Associations of ALG10 with chemical compounds

 

Analytical, diagnostic and therapeutic context of ALG10

References

  1. In vivo identification of genes that modify ether-a-go-go-related gene activity in Caenorhabditis elegans may also affect human cardiac arrhythmia. Petersen, C.I., McFarland, T.R., Stepanovic, S.Z., Yang, P., Reiner, D.J., Hayashi, K., George, A.L., Roden, D.M., Thomas, J.H., Balser, J.R. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  2. KCR1, a membrane protein that facilitates functional expression of non-inactivating K+ currents associates with rat EAG voltage-dependent K+ channels. Hoshi, N., Takahashi, H., Shahidullah, M., Yokoyama, S., Higashida, H. J. Biol. Chem. (1998) [Pubmed]
  3. The IKr drug response is modulated by KCR1 in transfected cardiac and noncardiac cell lines. Kupershmidt, S., Yang, I.C., Hayashi, K., Wei, J., Chanthaphaychith, S., Petersen, C.I., Johns, D.C., George, A.L., Roden, D.M., Balser, J.R. FASEB J. (2003) [Pubmed]
 
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