Congenital disorders of glycosylation in hepatology: The example of polycystic liver disease

Journal of Hepatology

Volumn 52, Issue 3, 2010, Pages 432-440

  Janssen, Manoe J ^a   Waanders, Esmé ^a   Woudenberg, Jannes ^a   Lefeber, Dirk J ^a   Drenth, Joost P H ^a  

^a RADBOUD UNIVERSITY MEDICAL CENTER   (Netherlands)

Author keywords

Congenital disorders of glycosylation; Glucosidase II; Polycystic liver disease; PRKCSH; Protein folding; Protein quality control; SEC63

Indexed keywords

ANGIOPEPTIN; CALNEXIN; CALRETICULIN; GENE PRODUCT; GLUCOSIDASE; GLYCAN; HEPATOCYSTIN; LIVER PROTEIN; PLACEBO; TRANSLOCON; UNCLASSIFIED DRUG;

BETA CHAIN; CLINICAL TRIAL; CONGENITAL DISORDER OF GLYCOSYLATION; CYTOPLASM; ENDOPLASMIC RETICULUM; GENE; GENE FUNCTION; GENETIC DISORDER; HUMAN; LIVER POLYCYSTIC DISEASE; PRIORITY JOURNAL; PRKCSH GENE; PROTEIN BINDING; PROTEIN FOLDING; REGULATORY MECHANISM; REVIEW; SCLEROTHERAPY; SEC63 GENE;

CYSTS; GLUCOSIDASES; GLYCOSYLATION; HUMANS; INTRACELLULAR SIGNALING PEPTIDES AND PROTEINS; LIVER DISEASES; MEMBRANE PROTEINS;

EID: 77249128360     PISSN: 01688278     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jhep.2009.12.011     Document Type: Review

References (83)

1. Blomme B., Van S.C., Callewaert N., and Van V.H. Alteration of protein glycosylation in liver diseases. J Hepatol 50 (2009) 592-603
2. Everson G.T., Taylor M.R., and Doctor R.B. Polycystic disease of the liver. Hepatology 40 (2004) 774-782
3. Masyuk T., and LaRusso N. Polycystic liver disease: new insights into disease pathogenesis. Hepatology 43 (2006) 906-908
4. Kida T., Nakanuma Y., and Terada T. Cystic dilatation of peribiliary glands in livers with adult polycystic disease and livers with solitary nonparasitic cysts: an autopsy study. Hepatology 16 (1992) 334-340
5. Qian Q., Li A., King B.F., Kamath P.S., Lager D.J., Huston III J., et al. Clinical profile of autosomal dominant polycystic liver disease. Hepatology 37 (2003) 164-171
6. Lazaridis K.N., Strazzabosco M., and Larusso N.F. The cholangiopathies: disorders of biliary epithelia. Gastroenterology 127 (2004) 1565-1577
7. Drenth J.P., Martina J.A., van de K.R., Bonifacino J.S., and Jansen J.B. Polycystic liver disease is a disorder of cotranslational protein processing. Trends Mol Med 11 (2005) 37-42
8. Hoevenaren I.A., Wester R., Schrier R.W., McFann K., Doctor R.B., Drenth J.P., et al. Polycystic liver: clinical characteristics of patients with isolated polycystic liver disease compared with patients with polycystic liver and autosomal dominant polycystic kidney disease. Liver Int 28 (2008) 264-270
9. Van Keimpema L., de Koning D.B., Strijk S.P., and Drenth J.P. Aspiration-sclerotherapy results in effective control of liver volume in patients with liver cysts. Dig Dis Sci 53 (2008) 2251-2257
10. Van Keimpema L., Ruurda J.P., Ernst M.F., van Geffen H.J., and Drenth J.P. Laparoscopic fenestration of liver cysts in polycystic liver disease results in a median volume reduction of 12.5%. J Gastrointest Surg 12 (2008) 477-482
11. Van Keimpema L., and Hockerstedt K. Treatment of polycystic livers. Br J Surg 96 (2009) 1379-1380
12. Van Keimpema L., Nevens F., Adam R., Porte R., Kirkegaard P., Metselaar H., et al. Liver transplantation in isolated polycystic liver disease. Transpl Int 22 (2009) 3
13. Van Keimpema L., Nevens F., Vanslembrouck R., Van Oijen M.G.H., Hoffmann A.L., Dekker H.M., et al. Lanreotide reduces the volume of polycystic liver: a randomized, double-blind, placebo-controlled trial. Gastroenterology 137 (2009) 1661-1668
14. Drenth J.P., te Morsche R.H., Smink R., Bonifacino J.S., and Jansen J.B. Germline mutations in PRKCSH are associated with autosomal dominant polycystic liver disease. Nat Genet 33 (2003) 345-347
15. Li A., Davila S., Furu L., Qian Q., Tian X., Kamath P.S., et al. Mutations in PRKCSH cause isolated autosomal dominant polycystic liver disease. Am J Hum Genet 72 (2003) 691-703
16. Davila S., Furu L., Gharavi A.G., Tian X., Onoe T., Qian Q., et al. Mutations in SEC63 cause autosomal dominant polycystic liver disease. Nat Genet 36 (2004) 575-577
17. Brodsky J.L., Goeckeler J., and Schekman R. BiP and Sec63p are required for both co- and posttranslational protein translocation into the yeast endoplasmic reticulum. Proc Natl Acad Sci USA 92 (1995) 9643-9646
18. Rapoport T.A. Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes. Nature 450 (2007) 663-669
19. Young B.P., Craven R.A., Reid P.J., Willer M., and Stirling C.J. Sec63p and Kar2p are required for the translocation of SRP-dependent precursors into the yeast endoplasmic reticulum in vivo. EMBO J 20 (2001) 262-271
20. Wang X., and Johnsson N. Protein kinase CK2 phosphorylates Sec63p to stimulate the assembly of the endoplasmic reticulum protein translocation apparatus. J Cell Sci 118 (2005) 723-732
21. Jermy A.J., Willer M., Davis E., Wilkinson B.M., and Stirling C.J. The Brl domain in Sec63p is required for assembly of functional endoplasmic reticulum translocons. J Biol Chem 281 (2006) 7899-7906
22. Willer M., Jermy A.J., Young B.P., and Stirling C.J. Identification of novel protein-protein interactions at the cytosolic surface of the Sec63 complex in the yeast ER membrane. Yeast 20 (2003) 133-148
23. Lyman S.K., and Schekman R. Binding of secretory precursor polypeptides to a translocon subcomplex is regulated by BiP. Cell 88 (1997) 85-96
24. Matlack K.E., Misselwitz B., Plath K., and Rapoport T.A. BiP acts as a molecular ratchet during posttranslational transport of prepro-alpha factor across the ER membrane. Cell 97 (1999) 553-564
25. Brodsky J.L., and Schekman R. A Sec63p-BiP complex from yeast is required for protein translocation in a reconstituted proteoliposome. J Cell Biol 123 (1993) 1355-1363
26. Corsi A.K., and Schekman R. The lumenal domain of Sec63p stimulates the ATPase activity of BiP and mediates BiP recruitment to the translocon in Saccharomyces cerevisiae. J Cell Biol 137 (1997) 1483-1493
27. Willer M., Jermy A.J., Steel G.J., Garside H.J., Carter S., and Stirling C.J. An in vitro assay using overexpressed yeast SRP demonstrates that cotranslational translocation is dependent upon the J-domain of Sec63p. Biochemistry 42 (2003) 7171-7177
28. McCracken A.A., and Brodsky J.L. Assembly of ER-associated protein degradation in vitro: dependence on cytosol, calnexin, and ATP. J Cell Biol 132 (1996) 291-298
29. Ng W., Sergeyenko T., Zeng N., Brown J.D., and Romisch K. Characterization of the proteasome interaction with the Sec61 channel in the endoplasmic reticulum. J Cell Sci 120 (2007) 682-691
30. Plemper R.K., Bohmler S., Bordallo J., Sommer T., and Wolf D.H. Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation. Nature 388 (1997) 891-895
31. Hendershot L.M. The ER chaperone BiP is a master regulator of ER function. Mt Sinai J Med 71 (2004) 289-297
32. Gillece P., Pilon M., and Romisch K. The protein translocation channel mediates glycopeptide export across the endoplasmic reticulum membrane. Proc Natl Acad Sci USA 97 (2000) 4609-4614
33. Alder N.N., Shen Y., Brodsky J.L., Hendershot L.M., and Johnson A.E. The molecular mechanisms underlying BiP-mediated gating of the Sec61 translocon of the endoplasmic reticulum. J Cell Biol 168 (2005) 389-399
34. Hamman B.D., Hendershot L.M., and Johnson A.E. BiP maintains the permeability barrier of the ER membrane by sealing the lumenal end of the translocon pore before and early in translocation. Cell 92 (1998) 747-758
35. Meyer H.A., Grau H., Kraft R., Kostka S., Prehn S., Kalies K.U., et al. Mammalian Sec61 is associated with Sec62 and Sec63. J Biol Chem 275 (2000) 14550-14557
36. Tyedmers J., Lerner M., Bies C., Dudek J., Skowronek M.H., Haas I.G., et al. Homologs of the yeast Sec complex subunits Sec62p and Sec63p are abundant proteins in dog pancreas microsomes. Proc Natl Acad Sci USA 97 (2000) 7214-7219
37. Kawaai K., Hisatsune C., Kuroda Y., Mizutani A., Tashiro T., and Mikoshiba K. 80K-H interacts with inositol 1,4,5-trisphosphate (IP3) receptors and regulates IP3-induced calcium release activity. J Biol Chem 284 (2009) 372-380
38. Li Y.M., Mitsuhashi T., Wojciechowicz D., Shimizu N., Li J., Stitt A., et al. Molecular identity and cellular distribution of advanced glycation endproduct receptors: relationship of p60 to OST-48 and p90 to 80K-H membrane proteins. Proc Natl Acad Sci USA 93 (1996) 11047-11052
39. Gkika D., Mahieu F., Nilius B., Hoenderop J.G., and Bindels R.J. 80K-H as a new Ca2+ sensor regulating the activity of the epithelial Ca2+ channel transient receptor potential cation channel V5 (TRPV5). J Biol Chem 279 (2004) 26351-26357
40. Brule S., Faure R., Dore M., Silversides D.W., and Lussier J.G. Immunolocalization of vacuolar system-associated protein-60 (VASAP-60). Histochem Cell Biol 119 (2003) 371-381
41. Hodgkinson C.P., Mander A., and Sale G.J. Identification of 80K-H as a protein involved in GLUT4 vesicle trafficking. Biochem J 388 (2005) 785-793
42. Kanai M., Goke M., Tsunekawa S., and Podolsky D.K. Signal transduction pathway of human fibroblast growth factor receptor 3. Identification of a novel 66-kDa phosphoprotein. J Biol Chem 272 (1997) 6621-6628
43. Forough R., Lindner L., Partridge C., Jones B., Guy G., and Clark G. Elevated 80K-H protein in breast cancer: a role for FGF-1 stimulation of 80K-H. Int J Biol Markers 18 (2003) 89-98
44. Waanders E., Croes H.J., Maass C.N., te Morsche R.H., van Geffen H.J., Van Krieken J.H., et al. Cysts of PRKCSH mutated polycystic liver disease patients lack hepatocystin but express Sec63p. Histochem Cell Biol 129 (2008) 301-310
45. Trombetta E.S., Simons J.F., and Helenius A. Endoplasmic reticulum glucosidase II is composed of a catalytic subunit, conserved from yeast to mammals, and a tightly bound noncatalytic HDEL-containing subunit. J Biol Chem 271 (1996) 27509-27516
46. Trombetta E.S., Fleming K.G., and Helenius A. Quaternary and domain structure of glycoprotein processing glucosidase II. Biochemistry 40 (2001) 10717-10722
47. Anelli T., and Sitia R. Protein quality control in the early secretory pathway. EMBO J 27 (2008) 315-327
48. Deprez P., Gautschi M., and Helenius A. More than one glycan is needed for ER glucosidase II to allow entry of glycoproteins into the calnexin/calreticulin cycle. Mol Cell 19 (2005) 183-195
49. Ruddock L.W., and Molinari M. N-Glycan processing in ER quality control. J Cell Sci 119 (2006) 4373-4380
50. D'Alessio C., Fernandez F., Trombetta E.S., and Parodi A.J. Genetic evidence for the heterodimeric structure of glucosidase II. The effect of disrupting the subunit-encoding genes on glycoprotein folding. J Biol Chem 274 (1999) 25899-25905
51. Wilkinson B.M., Purswani J., and Stirling C.J. Yeast GTB1 encodes a subunit of glucosidase II required for glycoprotein processing in the endoplasmic reticulum. J Biol Chem 281 (2006) 6325-6333
52. Pelletier M.F., Marcil A., Sevigny G., Jakob C.A., Tessier D.C., Chevet E., et al. The heterodimeric structure of glucosidase II is required for its activity, solubility, and localization in vivo. Glycobiology 10 (2000) 815-827
53. Treml K., Meimaroglou D., Hentges A., and Bause E. The alpha- and beta-subunits are required for expression of catalytic activity in the hetero-dimeric glucosidase II complex from human liver. Glycobiology 10 (2000) 493-502
54. Waanders E., Lameris A.L., Op den Camp H.J., Pluk W., Gloerich J., Strijk S.P., et al. Hepatocystin is not secreted in cyst fluid of hepatocystin mutant polycystic liver patients. J Proteome Res 7 (2008) 2490-2495
55. Stigliano I.D., Caramelo J.J., Labriola C.A., Parodi A.J., and D'Alessio C. Glucosidase II beta subunit modulates N-glycan trimming in fission yeasts and mammals. Mol Biol Cell 20 (2009) 3974-3984
56. Waanders E., Van Krieken J.H., Lameris A.L., and Drenth J.P. Disrupted cell adhesion but not proliferation mediates cyst formation in polycystic liver disease. Mod Pathol 21 (2008) 1293-1302
57. Jacob G.S. Glycosylation inhibitors in biology and medicine. Curr Opin Struct Biol 5 (1995) 605-611
58. Arendt C.W., Dawicki W., and Ostergaard H.L. Alternative splicing of transcripts encoding the alpha- and beta-subunits of mouse glucosidase II in T lymphocytes. Glycobiology 9 (1999) 277-283
59. Mehta A., Zitzmann N., Rudd P.M., Block T.M., and Dwek R.A. Alpha-glucosidase inhibitors as potential broad based anti-viral agents. FEBS Lett 430 (1998) 17-22
60. Free R.B., Hazelwood L.A., Cabrera D.M., Spalding H.N., Namkung Y., Rankin M.L., et al. D-1 and D-2 dopamine receptor expression is regulated by direct interaction with the chaperone protein calnexin. J Biol Chem 282 (2007) 21285-21300
61. Baldwin T.A., Gogela-Spehar M., and Ostergaard H.L. Specific isoforms of the resident endoplasmic reticulum protein glucosidase II associate with the CD45 protein-tyrosine phosphatase via a lectin-like interaction. J Biol Chem 275 (2000) 32071-32076
62. Harada Y., Li H., Li H., and Lennarz W.J. Oligosaccharyltransferase directly binds to ribosome at a location near the translocon-binding site. Proc Natl Acad Sci USA 106 (2009) 6945-6949
63. Sun L., Eklund E.A., Chung W.K., Wang C., Cohen J., and Freeze H.H. Congenital disorder of glycosylation id presenting with hyperinsulinemic hypoglycemia and islet cell hyperplasia. J Clin Endocrinol Metab 90 (2005) 4371-4375
64. Kranz C., Sun L., Eklund E.A., Krasnewich D., Casey J.R., and Freeze H.H. CDG-Id in two siblings with partially different phenotypes. Am J Med Genet A 143A (2007) 1414-1420
65. Denecke J., Kranz C., Kemming D., Koch H.G., and Marquardt T. An activated 5′ cryptic splice site in the human ALG3 gene generates a premature termination codon insensitive to nonsense-mediated mRNA decay in a new case of congenital disorder of glycosylation type Id (CDG-Id). Hum Mutat 23 (2004) 477-486
66. Weinstein M., Schollen E., Matthijs G., Neupert C., Hennet T., Grubenmann C.E., et al. CDG-IL: an infant with a novel mutation in the ALG9 gene and additional phenotypic features. Am J Med Genet A 136 (2005) 194-197
67. Frank C.G., Grubenmann C.E., Eyaid W., Berger E.G., Aebi M., and Hennet T. Identification and functional analysis of a defect in the human ALG9 gene: definition of congenital disorder of glycosylation type IL. Am J Hum Genet 75 (2004) 146-150
68. Vleugels W., Keldermans L., Jaeken J., Butters T.D., Michalski J.C., Matthijs G., et al. Quality control of glycoproteins bearing truncated glycans in an ALG9-defective (CDG-IL) patient. Glycobiology 19 (2009) 910-917
69. Eklund E.A., Newell J.W., Sun L., Seo N.S., Alper G., Willert J., et al. Molecular and clinical description of the first US patients with congenital disorder of glycosylation Ig. Mol Genet Metab 84 (2005) 25-31
70. Grubenmann C.E., Frank C.G., Kjaergaard S., Berger E.G., Aebi M., and Hennet T. ALG12 mannosyltransferase defect in congenital disorder of glycosylation type lg. Hum Mol Genet 11 (2002) 2331-2339
71. Kranz C., Basinger A.A., Gucsavas-Calikoglu M., Sun L., Powell C.M., Henderson F.W., et al. Expanding spectrum of congenital disorder of glycosylation Ig (CDG-Ig): sibs with a unique skeletal dysplasia, hypogammaglobulinemia, cardiomyopathy, genital malformations, and early lethality. Am J Med Genet A 143A (2007) 1371-1378
72. Damen G., de K.H., Huijmans J., den H.J., and Sinaasappel M. Gastrointestinal and other clinical manifestations in 17 children with congenital disorders of glycosylation type Ia, Ib, and Ic. J Pediatr Gastroenterol Nutr 38 (2004) 282-287
73. Eklund E.A., Sun L., Yang S.P., Pasion R.M., Thorland E.C., and Freeze H.H. Congenital disorder of glycosylation Ic due to a de novo deletion and an hALG-6 mutation. Biochem Biophys Res Commun 339 (2006) 755-760
74. Grunewald S., De V.R., and Jaeken J. Abnormal lysosomal inclusions in liver hepatocytes but not in fibroblasts in congenital disorders of glycosylation (CDG). J Inherit Metab Dis 26 (2003) 49-54
75. Chantret I., Dancourt J., Dupre T., Delenda C., Bucher S., Vuillaumier-Barrot S., et al. A deficiency in dolichyl-P-glucose:Glc1Man9GlcNAc2-PP-dolichyl alpha3-glucosyltransferase defines a new subtype of congenital disorders of glycosylation. J Biol Chem 278 (2003) 9962-9971
76. Eklund E.A., Sun L., Westphal V., Northrop J.L., Freeze H.H., and Scaglia F. Congenital disorder of glycosylation (CDG)-Ih patient with a severe hepato-intestinal phenotype and evolving central nervous system pathology. J Pediatr 147 (2005) 847-850
77. Schollen E., Frank C.G., Keldermans L., Reyntjens R., Grubenmann C.E., Clayton P.T., et al. Clinical and molecular features of three patients with congenital disorders of glycosylation type Ih (CDG-Ih) (ALG8 deficiency). J Med Genet 41 (2004) 550-556
78. De Praeter C.M., Gerwig G.J., Bause E., Nuytinck L.K., Vliegenthart J.F., Breuer W., et al. A novel disorder caused by defective biosynthesis of N-linked oligosaccharides due to glucosidase I deficiency. Am J Hum Genet 66 (2000) 1744-1756
79. Bovee J.V., Cleton-Jansen A.M., Wuyts W., Caethoven G., Taminiau A.H., Bakker E., et al. EXT-mutation analysis and loss of heterozygosity in sporadic and hereditary osteochondromas and secondary chondrosarcomas. Am J Hum Genet 65 (1999) 689-698
80. Pei Y., Watnick T., He N., Wang K., Liang Y., Parfrey P., et al. Somatic PKD2 mutations in individual kidney and liver cysts support a "two-hit" model of cystogenesis in type 2 autosomal dominant polycystic kidney disease. J Am Soc Nephrol 10 (1999) 1524-1529
81. Waanders E., te Morsche R.H., de Man R.A., Jansen J.B., and Drenth J.P. Extensive mutational analysis of PRKCSH and SEC63 broadens the spectrum of polycystic liver disease. Hum Mutat 27 (2006) 830
82. Haeuptle M.A., Pujol F.M., Neupert C., Winchester B., Kastaniotis A.J., Aebi M., et al. Human RFT1 deficiency leads to a disorder of N-linked glycosylation. Am J Hum Genet 82 (2008) 600-606
83. Iancu T.C., Mahajnah M., Manov I., Cherurg S., Knopf C., and Mandel H. The liver in congenital disorders of glycosylation: ultrastructural features. Ultrastruct Pathol 31 (2007) 189-197