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Gene Review

Gyg1  -  glycogenin 1

Rattus norvegicus

Synonyms: GN-1, GN1, Glycogenin-1, Gyg
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High impact information on Gyg1

  • 2) When these astrocytes are fed with glucose, proglycogen is synthesized from the glycogenin primer by a glycogen-synthase-like UDPglucose transglucosylase activity (proglycogen synthase) distinct from the well-recognized glycogen synthase, and synthesis stops at this point [1].
  • Glycogen synthesis in the astrocyte: from glycogenin to proglycogen to glycogen [1].
  • A xylosyltransferase in rat kidney, tentatively identified as glycogenin (Meezan, E., Ananth, S., Manzella, S., Campbell, P., Siegal, S., Pillion, D. J., and Rodén, L. (1994) J. Biol. Chem. 269, 11503-11508), was purified by a procedure in which affinity chromatography on UDP-glucuronic acid-agarose was a particularly useful step [2].
  • In contrast to glycogenin, glycogen synthase did not catalyze transfer from UDP-xylose, and it is suggested that the incorporation of xylose into glycogen observed by other investigators was due to glycogenin-catalyzed xylosyl transfer and subsequent chain elongation by glycogen synthase [2].
  • In this study we found no evidence for hormonal control of the glucosylation state of glycogenin in hepatocytes [3].

Biological context of Gyg1

  • A 1624 bp fragment of rat glycogenin was cloned by RT-PCR that includes a 1002 bp open reading frame encoding a 333 amino acid protein [4].
  • Utilizing the differential display technique to analyze changes in gene expression during early postnatal cardiac development, we have isolated and cloned a 484 bp cDNA fragment that corresponds to the 3' end of rat glycogenin [4].
  • In addition, the nucleotide and amino acid sequences of rat glycogenin may be used to investigate the physiological and pathophysiological roles of glycogenin in rat tissues [4].

Anatomical context of Gyg1

  • No limiting role for glycogenin in determining maximal attainable glycogen levels in rat skeletal muscle [5].
  • The effect of increasing the glycogenin level on glycogen synthesis was studied in rat 1 fibroblasts stably overexpressing rabbit muscle glycogenin [6].

Associations of Gyg1 with chemical compounds

  • The following conclusions have been drawn: 1) In the ammonia-treated astrocytes starved of glucose, free glycogenin is present [1].
  • Analysis of [14C]glucose- or [35S]methionine-labeled extracts from glycogenin-expressing cells by continuous polyacrylamide gel electrophoresis and by two-dimensional gel electrophoresis revealed a continuum of glycogenin-containing species from low molecular mass to sizes significantly greater than 400 kDa [6].
  • In fasted rats, glycogenin was present predominantly as the free-form of the enzyme, i.e., not attached to an amylase-digestible glycan, presumably glycogen [7].

Analytical, diagnostic and therapeutic context of Gyg1


  1. Glycogen synthesis in the astrocyte: from glycogenin to proglycogen to glycogen. Lomako, J., Lomako, W.M., Whelan, W.J., Dombro, R.S., Neary, J.T., Norenberg, M.D. FASEB J. (1993) [Pubmed]
  2. Xylosyl transfer to an endogenous renal acceptor. Purification of the transferase and the acceptor and their identification as glycogenin. Rodén, L., Ananth, S., Campbell, P., Manzella, S., Meezan, E. J. Biol. Chem. (1994) [Pubmed]
  3. Phosphorylase regulates the association of glycogen synthase with a proteoglycogen substrate in hepatocytes. Tavridou, A., Agius, L. FEBS Lett. (2003) [Pubmed]
  4. Molecular cloning and developmental expression of rat glycogenin in cardiac tissue. Pak, B.J., Sangaralingham, S.J., Pang, S.C. Mol. Cell. Biochem. (1999) [Pubmed]
  5. No limiting role for glycogenin in determining maximal attainable glycogen levels in rat skeletal muscle. Hansen, B.F., Derave, W., Jensen, P., Richter, E.A. Am. J. Physiol. Endocrinol. Metab. (2000) [Pubmed]
  6. Glycogen biogenesis in rat 1 fibroblasts expressing rabbit muscle glycogenin. Skurat, A.V., Lim, S.S., Roach, P.J. Eur. J. Biochem. (1997) [Pubmed]
  7. Liver glycogenin activity in diabetic and adrenalectomized rats. Gannon, M.C., Nuttall, J.A., Nuttall, F.Q. Cell. Mol. Biol. (Noisy-le-grand) (1998) [Pubmed]
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