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Gene Review

GP2  -  glycoprotein 2 (zymogen granule membrane)

Homo sapiens

Synonyms: Pancreatic secretory granule membrane major glycoprotein GP2, Pancreatic zymogen granule membrane protein GP-2, ZAP75
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Disease relevance of GP2


High impact information on GP2


Chemical compound and disease context of GP2

  • Drug resistant variants were isolated, suggesting that these compounds act through inhibition of a viral protein, the viral glycoprotein (GP2), and not through cellular toxicity mechanisms [5].
  • In the present study we compared the sensitivity to adriamycin (ADR) and the capacity of ADR uptake in two human neuroblastoma cell lines differing in properties relevant to metastatic potential, the GP2 and MB, of low- and high-malignancy phenotype, respectively [6].

Biological context of GP2


Anatomical context of GP2

  • Expression of both forms of GP2 in the human pancreas was confirmed [12].
  • GP-2 released from zymogen granule membranes with phosphatidylinositol phospholipase C reacts with anti-cross-reactive determinant antibody (anti-CRD), confirming the GPI nature of the pancreatic homologue [13].
  • GP-2 homologues are observed in a wide variety of epithelial cells, several of which contain highly regulated secretory processes [13].
  • Sequence of the cDNA encoding human GP-2, the major membrane protein in the secretory granule of the exocrine pancreas [8].
  • This suggests that the cleavage of GP2 from the cell membrane may activate endocytosis through a tyrosine kinase-regulated pathway [9].

Associations of GP2 with chemical compounds

  • A family of homologous genes is shown to encode GP-2, the major glycosylphosphatidylinositol (GPI)-linked glycoprotein of pancreatic zymogen granule membranes, and Tamm-Horsfall protein (THP), a GPI-linked glycoprotein associated with apical vesicles in kidney thick ascending limb of Henle (TALH) cells [13].
  • Dot-blot assay showed that annexin IV interacts with GP-2 in the presence of calcium and that it recognizes the terminal sialic acid residues linked through alpha2-3 linkages to the carbohydrate of GP-2 [14].
  • Although 93% of the GP-2 in the resting secretions of anaesthetized rats could be pelleted, Triton X-114 phase extraction showed that 70% of this GP-2 had lost its hydrophobic properties [11].
  • It is therefore concluded that most of the GP-2 secreted by the pancreas of anaesthetized rats under resting conditions is released from the membrane by a phospholipase C which hydrolyses the phosphodiester bond linking GP-2 to its diradylglycerol anchor [11].
  • These studies show the presence of inositol 1,2-(cyclic)monophosphate on the secreted hydrophilic GP-2, confirming the involvement of an endogenous phospholipase C in the solubilization of GP-2 by the exocrine pancreas [11].

Other interactions of GP2

  • These results suggest that GP-2 is an endogenous ligand of annexin IV in the exocrine pancreas [14].
  • This suggests that in pancreatic acini, GP2 may exist in a complex with src kinases, caveolin, and an 85-kDa phosphorylated substrate to regulate endocytosis at the APM [9].
  • In experiments supporting the localization data, incubation of the AR42J transformants with the secretagogue cholecystokinin (CCK8) resulted in enhanced release of a shed form of GP-2 into the medium in parallel with amylase, suggesting that the two proteins were secreted from the same compartment [10].
  • Poor binding of a HER-2/neu epitope (GP2) to HLA-A2.1 is due to a lack of interactions with the center of the peptide [15].
  • All TCC displayed high specific proliferation, showed DR-restriction, and produced IFN-gamma upon stimulation with recombinant GP2 [16].

Analytical, diagnostic and therapeutic context of GP2


  1. GP2, the homologue to the renal cast protein uromodulin, is a major component of intraductal plugs in chronic pancreatitis. Freedman, S.D., Sakamoto, K., Venu, R.P. J. Clin. Invest. (1993) [Pubmed]
  2. Absence of the major zymogen granule membrane protein, GP2, does not affect pancreatic morphology or secretion. Yu, S., Michie, S.A., Lowe, A.W. J. Biol. Chem. (2004) [Pubmed]
  3. Use of a mammalian internal ribosomal entry site element for expression of a foreign protein by a transfectant influenza virus. García-Sastre, A., Muster, T., Barclay, W.S., Percy, N., Palese, P. J. Virol. (1994) [Pubmed]
  4. Properties of a basement membrane-related glycoprotein synthesized in culture by a mouse embryonal carcinoma-derived cell line. Chung, A.E., Jaffe, R., Freeman, I.L., Vergnes, J.P., Braginski, J.E., Carlin, B. Cell (1979) [Pubmed]
  5. Identification and characterization of potent small molecule inhibitor of hemorrhagic fever New World arenaviruses. Bolken, T.C., Laquerre, S., Zhang, Y., Bailey, T.R., Pevear, D.C., Kickner, S.S., Sperzel, L.E., Jones, K.F., Warren, T.K., Amanda Lund, S., Kirkwood-Watts, D.L., King, D.S., Shurtleff, A.C., Guttieri, M.C., Deng, Y., Bleam, M., Hruby, D.E. Antiviral Res. (2006) [Pubmed]
  6. Malignant phenotype correlating with drug resistance in two human neuroblastoma cell lines. Wollman, Y., Shahar, I., Goldstein, M., Leibovici, J. J. Neurooncol. (1994) [Pubmed]
  7. Assignment of pancreatic zymogen granule membrane protein GP2 (GP2) to human chromosome band 9q21.11 to q21.2 by in situ hybridization. Fukuoka, S.I., Suzuki, M., Okabayashi, K., Takahashi, E. Cytogenet. Cell Genet. (1997) [Pubmed]
  8. Sequence of the cDNA encoding human GP-2, the major membrane protein in the secretory granule of the exocrine pancreas. Wong, S.M., Lowe, A.W. Gene (1996) [Pubmed]
  9. GP2, a GPI-anchored protein in the apical plasma membrane of the pancreatic acinar cell, co-immunoprecipitates with src kinases and caveolin. Parker, E.M., Zaman, M.M., Freedman, S.D. Pancreas (2000) [Pubmed]
  10. Incorporation of the pancreatic membrane protein GP-2 into secretory granules in exocrine but not endocrine cells. Hoops, T.C., Ivanov, I., Cui, Z., Colomer-Gould, V., Rindler, M.J. J. Biol. Chem. (1993) [Pubmed]
  11. In resting conditions, the pancreatic granule membrane protein GP-2 is secreted by cleavage of its glycosylphosphatidylinositol anchor. Paul, E., Leblond, F.A., LeBel, D. Biochem. J. (1991) [Pubmed]
  12. Molecular cloning and sequences of cDNAs encoding alpha (large) and beta (small) isoforms of human pancreatic zymogen granule membrane-associated protein GP2. Fukuoka, S. Biochim. Biophys. Acta (2000) [Pubmed]
  13. GP-2/THP gene family encodes self-binding glycosylphosphatidylinositol-anchored proteins in apical secretory compartments of pancreas and kidney. Fukuoka, S., Freedman, S.D., Yu, H., Sukhatme, V.P., Scheele, G.A. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  14. A potential endogenous ligand of annexin IV in the exocrine pancreas. Carbohydrate structure of GP-2, a glycosylphosphatidylinositol-anchored glycoprotein of zymogen granule membranes. Tsujii-Hayashi, Y., Kitahara, M., Yamagaki, T., Kojima-Aikawa, K., Matsumoto, I. J. Biol. Chem. (2002) [Pubmed]
  15. Poor binding of a HER-2/neu epitope (GP2) to HLA-A2.1 is due to a lack of interactions with the center of the peptide. Kuhns, J.J., Batalia, M.A., Yan, S., Collins, E.J. J. Biol. Chem. (1999) [Pubmed]
  16. Old and New World arenaviruses share a highly conserved epitope in the fusion domain of the glycoprotein 2, which is recognized by Lassa virus-specific human CD4+ T-cell clones. Meulen, J., Badusche, M., Satoguina, J., Strecker, T., Lenz, O., Loeliger, C., Sakho, M., Koulemou, K., Koivogui, L., Hoerauf, A. Virology (2004) [Pubmed]
  17. The HER2/neu-derived peptide p654-662 is a tumor-associated antigen in human pancreatic cancer recognized by cytotoxic T lymphocytes. Peiper, M., Goedegebuure, P.S., Linehan, D.C., Ganguly, E., Douville, C.C., Eberlein, T.J. Eur. J. Immunol. (1997) [Pubmed]
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