The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

Gcs1  -  glucosidase 1

Rattus norvegicus

Synonyms: Glycoprotein-processing glucosidase I, Mannosyl-oligosaccharide glucosidase, Mogs
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of Gcs1

  • Contrary to our original expectations, the most influential gene was the one on chromosome (chr.) 15, Gastric cancer susceptibility gene 1 (Gcs1), which confers susceptibility to stomach carcinogenesis (LOD, 3.8) with a dominant BUF allele by promoting conversion from adenomas to carcinomas [1].
  • Glucosidase inhibition. A new approach to the treatment of diabetes, obesity, and hyperlipoproteinaemia [2].
  • Since these changes could be produced with an amount of glucosidase inhibitor which did not prevent normal rate of weight gain, the possibility arises that this approach may be useful in the treatment of various hypertriglyceridemic states in man [3].
  • Normal rat kidney (NRK) cells transformed by the v-sis oncogene of simian sarcoma virus (SSV) were treated with the glucosidase I inhibitor castanospermine [4].

High impact information on Gcs1


Chemical compound and disease context of Gcs1


Biological context of Gcs1


Anatomical context of Gcs1

  • Based on trypsin digestion pattern and the data on membrane topography, glucosidase I constitutes a single polypeptide chain of 85 kDa with two contiguous domains: a membrane-bound domain that anchors the protein to the endoplasmic reticulum and a luminal domain [9].
  • Role of sulfhydryl groups in the function of glucosidase I from mammary gland [13].
  • Intestinal brush border enzyme activities in the rats treated with urogastrone-epidermal growth factor were restored to those seen in the orally fed rats except for alpha glucosidase activity in the proximal gut [14].
  • Acarbose is a potent intestinal glucosidase inhibitor which could have an anti-obesity property by reducing postprandial plasma glucose and insulin levels, potentially responsible for high rates of lipid synthesis in adipose tissue [15].
  • Brush border gamma glutamyltransferase and alpha glucosidase activities were reduced by up to 50% throughout the small intestine of the animals fed intravenously [14].

Associations of Gcs1 with chemical compounds

  • We have analyzed the functional domain structure of rat mammary glucosidase I, an enzyme involved in N-linked glycoprotein processing, using biochemical and immunological approaches [9].
  • One of these glucosidases removes the distal glucose from Glc3Man9GlcNAc, and the other glucosidase sequentially removes glucose from Glc2Man9GlcNAc and Glc1Man9GlcNAc [16].
  • The fully core-glycosylated form of Mr = 41,000, which was detected after inhibition of glucosidase I with 1-deoxynojirimycin, was converted into a Mr = 39,000 intermediate, and upon further trimming, into a Mr = 36,000 endo-H-sensitive form [17].
  • Glucosidase I initiates the processing of asparagine-linked glycoproteins by excising the distal alpha 1,2-linked glucosyl residue from the Glc3Man9GlcNAc2 oligosaccharide, soon after its en bloc transfer from the lipid-linked donor to the nascent polypeptide [13].
  • The results on hormonal regulation of glucosidase I indicate that the synthesis of the enzyme is stimulated by a combination of insulin, hydrocortisone, and prolactin; additionally, epidermal growth factor may play a role in this regulation [18].

Regulatory relationships of Gcs1


Other interactions of Gcs1


Analytical, diagnostic and therapeutic context of Gcs1


  1. Chromosomal mapping of genes controlling development, histological grade, depth of invasion, and size of rat stomach carcinomas. Ushijima, T., Yamamoto, M., Suzui, M., Kuramoto, T., Yoshida, Y., Nomoto, T., Tatematsu, M., Sugimura, T., Nagao, M. Cancer Res. (2000) [Pubmed]
  2. Glucosidase inhibition. A new approach to the treatment of diabetes, obesity, and hyperlipoproteinaemia. Puls, W., Keup, U., Krause, H.P., Thomas, G., Hoffmeister, F. Naturwissenschaften (1977) [Pubmed]
  3. Inhibition of carbohydrate-induced hypertriglyceridemia by a disaccharidase inhibitor. Zavaroni, I., Reaven, G.M. Metab. Clin. Exp. (1981) [Pubmed]
  4. Inhibition of glycosylation processing alters the growth parameters of cells transformed by the oncogene of simian sarcoma virus. Hadwiger-Fangmeier, A., Niemann, H., Tamura, T. Arch. Virol. (1989) [Pubmed]
  5. Retention of membrane proteins by the endoplasmic reticulum. Brands, R., Snider, M.D., Hino, Y., Park, S.S., Gelboin, H.V., Rothman, J.E. J. Cell Biol. (1985) [Pubmed]
  6. Transformation by the v-fms oncogene product: role of glycosylational processing and cell surface expression. Nichols, E.J., Manger, R., Hakomori, S., Herscovics, A., Rohrschneider, L.R. Mol. Cell. Biol. (1985) [Pubmed]
  7. Golgi apparatus immunolocalization of endomannosidase suggests post-endoplasmic reticulum glucose trimming: implications for quality control. Zuber, C., Spiro, M.J., Guhl, B., Spiro, R.G., Roth, J. Mol. Biol. Cell (2000) [Pubmed]
  8. Effects of a glucosidase inhibitor (acarbose, BAY g 5421) on the development of obesity and food motivated behavior in Zucker (fafa) rats. Vasselli, J.R., Haraczkiewicz, E., Maggio, C.A., Greenwood, M.R. Pharmacol. Biochem. Behav. (1983) [Pubmed]
  9. Glucosidase I, a transmembrane endoplasmic reticular glycoprotein with a luminal catalytic domain. Shailubhai, K., Pukazhenthi, B.S., Saxena, E.S., Varma, G.M., Vijay, I.K. J. Biol. Chem. (1991) [Pubmed]
  10. Glucosidase II from rat liver microsomes. Kinetic model for binding and hydrolysis. Alonso, J.M., Santa-Cecilia, A., Calvo, P. Biochem. J. (1991) [Pubmed]
  11. Different effects of the glucosidase inhibitors 1-deoxynojirimycin, N-methyl-1-deoxynojirimycin and castanospermine on the glycosylation of rat alpha 1-proteinase inhibitor and alpha 1-acid glycoprotein. Gross, V., Tran-Thi, T.A., Schwarz, R.T., Elbein, A.D., Decker, K., Heinrich, P.C. Biochem. J. (1986) [Pubmed]
  12. The regulation of lipogenesis in vivo in the lactating mammary gland of the rat during the starved-refed transition. Studies wtih acarbose, a glucosidase inhibitor. Mercer, S.W., Williamson, D.H. Biochem. J. (1987) [Pubmed]
  13. Role of sulfhydryl groups in the function of glucosidase I from mammary gland. Pukazhenthi, B.S., Muniappa, N., Vijay, I.K. J. Biol. Chem. (1993) [Pubmed]
  14. Effects of urogastrone-epidermal growth factor on intestinal brush border enzymes and mitotic activity. Goodlad, R.A., Raja, K.B., Peters, T.J., Wright, N.A. Gut (1991) [Pubmed]
  15. Effect of acarbose on glucose homeostasis, lipogenesis and lipogenic enzyme gene expression in adipose tissue of weaned rats. Maury, J., Issad, T., Perdereau, D., Gouhot, B., Ferré, P., Girard, J. Diabetologia (1993) [Pubmed]
  16. Glycoprotein biosynthesis. Rat liver microsomal glucosidases which process oligosaccharides. Grinna, L.S., Robbins, P.W. J. Biol. Chem. (1979) [Pubmed]
  17. Cell surface glycoproteins involved in the stimulation of interleukin 1-dependent interleukin 2 production by a subline of EL4 thymoma cells. II. Structure, biosynthesis, and maturation. Lüscher, B., Rousseaux, M., Lees, R., MacDonald, H.R., Bron, C. J. Immunol. (1985) [Pubmed]
  18. Developmental regulation of glucosidase I, an enzyme involved in the processing of asparagine-linked glycoproteins in rat mammary gland. Shailubhai, K., Saxena, E.S., Balapure, A.K., Vijay, I.K. J. Biol. Chem. (1990) [Pubmed]
  19. Biosynthesis of inositol trisphosphate receptors: selective association with the molecular chaperone calnexin. Joseph, S.K., Boehning, D., Bokkala, S., Watkins, R., Widjaja, J. Biochem. J. (1999) [Pubmed]
  20. Secretion of rat hepatic lipase is blocked by inhibition of oligosaccharide processing at the stage of glucosidase I. Verhoeven, A.J., Jansen, H. J. Lipid Res. (1990) [Pubmed]
  21. In vitro reconstitution of calreticulin-substrate interactions. Peterson, J.R., Helenius, A. J. Cell. Sci. (1999) [Pubmed]
  22. Lipid composition and acid hydrolase content of lamellar granules of fetal rat epidermis. Freinkel, R.K., Traczyk, T.N. J. Invest. Dermatol. (1985) [Pubmed]
  23. alpha-Glucosidase inhibitors in diabetes: lessons from animal studies. Peterson, R.G. Eur. J. Clin. Invest. (1994) [Pubmed]
  24. The role of proteolytic enzymes in the deposition of amyloid proteins. Sato, A., Kawamura, M., Nishioka, M., Nakamura, S., Minaguchi, J. Adv. Enzyme Regul. (1996) [Pubmed]
  25. Microsomal glucosidases of rat liver. Partial purification and inhibition by disaccharides. Ugalde, R.A., Staneloni, R.J., Leloir, L.F. Eur. J. Biochem. (1980) [Pubmed]
  26. Changes in cecal microbial metabolism of rats induced by individual and a mixture of drinking water disinfection by-products. George, S.E., Wolf, D.C., Brooks, L.R., Bailey, K.C., Hooth, M.J., Nelson, G.M. Cancer Lett. (2004) [Pubmed]
  27. The degradation of glycogen in the lysosomes of newborn rat hepatocytes: glycogen-, maltose- and isomaltose-hydrolyzing acid alpha glucosidase activities in liver. Kalamidas, S.A., Kotoulas, O.B. Histol. Histopathol. (1999) [Pubmed]
WikiGenes - Universities