Congenital disorders of glycosylation. Part II. Defects of protein O-glycosylation

• Autorzy: Cylwik B. , Lipartowska K. , Chrostek L. , Gruszewska E.
• Języki publikacji: EN

Abstrakty

EN

Glycosylation is a form of post-translational modification of proteins and occurs in every living cell. The carbohydrate chains attached to the proteins serve various functions. There are two main types of protein glycosylation: N-glycosylation and O-glycosylation. In this paper, we describe the O-glycosylation process and currently known congenital disorders of glycosylation associated with defects of protein O-glycosylation. This process takes place in the cis Golgi apparatus after N-glycosylation and folding of the proteins. The O-glycosylation is essential in the biosynthesis of mucins, the formation of proteoglycan core proteins and blood group proteins. Most common forms of O-glycans are the mucin-type glycans. There are more than 20 known disorders related to O-glycosylation disturbances. We review 8 of the following diseases linked to defects in the synthesis of O-xylosylglycans, O-N acetylgalactosaminylglycans, O-xylosyl/N-acetylglycans, O-mannosylglycans, and O-fucosylglycans: multiple exostoses, progeroid variant of Ehlers-Danlos syndrome, progeria, familial tumoral calcinosis, Schneckenbecken dysplasia, Walker-Warburg syndrome, spondylocostal dysostosis type 3, and Peter's plus syndrome. Causes of these diseases include gene mutations and deficiency of proteins (enzymes). Their diagnosis includes syndromic presentation, organ-specific expression and laboratory findings.

Słowa kluczowe

EN

congenital disorder; glycosylation; protein O-glycosylation; O-glycosylation; genetic defect; diagnostics

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2013
• Tom: 60
• Numer: 3
• Opis fizyczny: p.361-368,fig.,ref.

Twórcy

autor

Cylwik B.

• Department of Biochemical Diagnostics, Medical University of Bialystok, Bialystok, Poland

autor

Lipartowska K.

• Department of Biochemical Diagnostics, Medical University of Bialystok, Bialystok, Poland

autor

Chrostek L.

• Department of Biochemical Diagnostics, Medical University of Bialystok, Bialystok, Poland

autor

Gruszewska E.

• Department of Biochemical Diagnostics, Medical University of Bialystok, Bialystok, Poland

Bibliografia

• Beighton P, Sujansky E, Patzak B, Portele KA (1993) Genetic skeletal dysplasias in the Museum of Pathological Anatomy, Vienna. Am J Med Genet 47: 843-847. 
• Beltran-Valero de Bernabe D, Currier S, Steinbrecher A, Celli J, van Beusekom E, van der Zwaag B, Kayserili H, Merlini L, Chitayat D, Dobyns WB, Cormand B, Lehesjoki AE, Cruces J, Voit T, Walsh CA, van Bokhoven H, Brunner HG (2002) Mutations in the O-mannosyltransferase gene POMT1 give rise to the severe neuronal migration disorder Walker-Warburg syndrome. Am J Hum Genet 71: 1033-1043. 
• Bennett EP, Hassan H, Clausen H (1996) cDNA cloning and expression of a novel human UDP-N-acetyl-α-D-galactosamine. Polypeptide N-acetylgalactosaminyltransferase, GalNAc-t3. J Biol Chem 271: 17006-17012. 
• Brockhausen I, Schachter H, Stanley P (2009) O-GalNAc Glycans. In Essential of Glycobiology. Varki A, Cummings RD, Esko JD, Freeze HH, Stanley P, Bertozzi CR, Hart GW, Etzler ME, 2nd eds, pp 115-127. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York. 
• Chefetz I, Sprecher E (2009) Familial tumoral calcinosis and the role of O-glycosylation in the maintenance of phosphate homeostasis. Biochim Biophys Acta 1792: 847-852. 
• Cormand B, Pihko H, Bayes M, Valanne L, Santavuori P, Talim B, Gershoni-Baruch R, Ahmad A, van Bokhoven H, Brunner HG, Voit T, Topaloglu H, Dobyns WB, Lehesjoki AE (2001) Clinical and genetic distinction between Walker-Warburg syndrome and muscle-eye-brain disease. Neurology 56: 1059-1069. 
• de Jong JG, Wevers RA, Liebrand-van Sambeek R (1992) Measuring urinary glycosaminoglycans in the presence of protein: an improved screening procedure for mucopolysaccharidoses based on dimethylmethylene blue. Clin Chem 38: 803-807. 
• Diesen C, Saarinen A, Pihko H, Rosenlew C, Cormand B, Dobyns WB, Dieguez J, Valanne L, Joensuu T, Lehesjoki AE (2004) POMGnT1 mutation and phenotypic spectrum in muscle-eye-brain disease. J Med Genet 41: e115. 
• Duret MH (1899) Tumeurs multiples and singuliers de bourses sereuses. Bull Mem Soc Ant 74: 725-731.
• Esko JD, Kimata K, Lindahl U (2009) Proteoglycans and Sulfated Glycosaminoglycans. In Essential of Glycobiology. Varki A, Cummings RD, Esko JD, Freeze HH, Stanley P, Bertozzi CR, Hart GW, Etzler ME, 2nd eds, pp 229-248. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York. 
• Faiyaz-Ul-Haque M, Zaidi SH, Al-Ali M, Al-Mureikhi MS, Kennedy S, Al-Thani G, Tsui LC, Teebi AS (2004) A novel missense mutation in the galactosyltransferase-I (B4GALT7) gene in a family exhibiting facioskeletal anomalies and Ehlers-Danlos syndrome resembling the progeroid type. Am J Med Genet A 128A: 39-45. 
• Freeze HH, Haltiwanger RS (2009) Other Classes of ER/Golgi-derived Glycans. In Essential of Glycobiology. Varki A, Cummings RD, Esko JD, Freeze HH, Stanley P, Bertozzi CR, Hart GW, Etzler ME, 2nd eds, pp 163-174. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York. 
• Freeze HH, Schachter H (2009) Genetic Disorders of Glycosylation. In Essential of Glycobiology. Varki A, Cummings RD, Esko JD, Freeze HH, Stanley P, Bertozzi CR, Hart GW, Etzler ME, 2nd eds, pp 585-600. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York. 
• Furuichi T, Kayserili H, Hiraoka S, Nishimura G, Ohashi H, Alanay Y, Lerena J C, Aslanger AD, Koseki H, Cohn DH, Superti-Furga A, Unger S, Ikegawa S (2009) Identification of loss-of-function mutations of SLC35D1 in patients with Schneckenbecken dysplasia, but not with other severe spondylodysplastic dysplasias group diseases. J Med Genet 46: 562-568. 
• Giard JM (1898) Sur la calcification hibernale. Compes Rend Seanes Soc Biol So 1013-1015.
• Heinritz W, Huffmeier U, Strenge S, Miterski B, Zweier C, Leinun S, Bohring A, Mitulla B, Peters U, Froster UG (2009) New mutations of EXT1 and EXT2 genes in German patients with multiple osteochondromas. Ann Hum Genet 73: 283-291. 
• Hess D, Keusch JJ, Oberstein SA, Hennekam RC, Hofsteenge J (2008) Peters Plus syndrome is a new congenital disorder of glycosylation and involves defective O-glycosylation of thrombospondin type 1 repeats. J Biol Chem 283: 7354-7360. 
• Hewitt JE (2009) Abnormal glycosylation of dystroglycan in human genetic disease. Biochim Biophys Acta 1792: 853-861. 
• Hiraoka S, Furuichi T, Nishimura G, Shibata S, Yanagishita M, Rimoin DL, Superti-Furga A, Nikkels PG, Ogawa M, Katsuyama K, Toyoda H, Kinoshita-Toyoda A, Ishida N, Isono K, Sanai Y, Cohn DH, Koseki H, Ikegawa S (2007) Nucleotide-sugar transporter SLC35D1 is critical to chondroitin sulfate synthesis in cartilage and skeletal development in mouse and human. Nature Med 13: 1363-1367. 
• Jaeken J, Hennet T, Matthijs G, Freeze HH (2009) CDG nomenclature: time for a change! Biochim Biophys Acta 1792: 825-826. 
• Jennes I, Entius MM, Van Hul E, Parra A, Sangiorgi L, Wuyts W (2008) Mutation screening of EXT1 and EXT2 by denaturing high-performance liquid chromatography, direct sequencing analysis, fluorescence in situ hybridization, and a new multiplex ligation-dependent probe amplification probe set in patients with multiple osteochondromas. J Mol Diagn 10: 85-92. 
• Jentoft N (1990) Why are proteins O-glycosylated? Trends Biochem Sci 15: 291-294. 
• Kano H, Kobayashi K, Herrmann R, Tachikawa M, Manya H, Nishino I, Nonaka I, Straub V, Talim B, Voit T, Topaloglu H, Endo T, Yoshikawa H, Toda T (2002) Deficiency of α-dystroglycan in muscle-eye-brain disease. Biochem Biophys Res Commun 291: 1283-1286. 
• Kim DS, Hayashi YK, Matsumoto H, Ogawa M, Noguchi S, Murakami N, Sakuta R, Mochizuki M, Michele DE, Campbell KP, Nonaka I, Nishino I (2004) POMT1 mutation results in defective glycosylation and loss of laminin-binding activity in alpha-DG. Neurology 62: 1009-1011. 
• Kresse H, Rosthoj S, Quentin E, Hollmann J, Glossl J, Okada S, Tonnesen T (1987) Glycosaminoglycan-free small proteoglycan core protein is secreted by fibroblasts from a patient with a syndrome resembling progeroid. Am J Hum Genet 41: 436-453. 
• Krooth RS, Macklin MT, Hilbish TF (1961) Diaphysial aclasis (multiple exostoses) on Guam. Am J Hum Genet 13: 340-347. 
• Lawler J, Hynes RO (1986) The structure of human thrombospondin, an adhesive glycoprotein with multiple calcium-binding sites and homologies with several different proteins. J Cell Biol 103: 1635-1648. 
• Legeai-Mallet L, Munnich A, Maroteaux P, Le Merrer M (1997) Incomplete penetrance and expressivity skewing in hereditary multiple exostoses. Clin Genet 52: 12-16. 
• Manya H, Chiba A, Yoshida A, Wang X, Chiba Y, Jigami Y, Margolis RU, Endo T (2004) Demonstration of mammalian protein O-mannosyltransferase activity: coexpresion of POMT1 and POMT2 required for enzymatic activity. Proc Natl Acad Sci USA 101: 500-505. 
• Martinez-Duncker I, Dupre T, Piller V, Piller F, Candelier JJ, Trichet C, Tchernia G, Oriol R, Mollicone R (2005) Genetic complementation reveals a novel human congenital disorder of glycosylation of type II, due to inactivation of the Golgi CMP-sialic acid transporter. Blood 105: 2671-2676. 
• McClatchie S, Bremner AD (1969) Tumoral calcinosis--an unrecognized disease. Br Med J 1: 153-155. 
• Michele DE, Barresi R, Kanagawa M, Saito F, Cohn RD, Satz JS, Dollar J, Nishino I, Kelley RI, Somer H, Straub V, Mathews KD, Moore SA, Campbell KP (2002) Post-translational disruption of dystroglycan-ligand interactions in congenital muscular dystrophies. Nature 418: 417-422. 
• Muraoka M, Kawakita M, Ishida N (2001) Molecular characterization of human UDP-glucuronic acid/UDP-N-acetylgalactosamine transporter, a novel nucleotide sugar transporter with dual substrate specificity. FEBS Lett 495: 87-93. 
• Okajima T, Fukumoto S, Furukawa K, Urano T, Furukawa K (1999) Molecular basis for the progeroid variant of Ehlers-Danlos syndrome: identification and characterization of two mutations in galactosyltransferase I gene. J Biol Chem 274: 28841-28844. 
• OMIM Online Mendelian Inheritance in Man. An Online Catalog of Human Genes and Genetic Disorders.  http://www.omim.org/. (updated 25 January 2013).
• Philippe C, Porter DE, Emerton ME, Wells DE, Simpson AH, Monaco AP (1997) Mutation screening of the EXT1 and EXT2 genes in patients with hereditary multiple exostoses. Am J Hum Genet 61: 520-528. 
• Quentin E, Gladen A, Roden L, Kresse H (1990) A genetic defect in the biosynthesis of dermatan sulfate proteoglycan: galactosyltransferase I deficiency in fibroblasts from a patient with a progeroid syndrome. Proc Natl Acad Sci USA 87: 1342-1346. 
• Ricketts LM, Dlugosz M, Luther KB, Haltiwanger RS, Majerus EM. (2007) O-fucosylation is required for ADAMTS13 secretion. J Biol Chem 282: 17014-17023. 
• Sabatelli P, Columbaro M, Mura I, Capanni C, Lattanzi G, Maraldi NM, Beltràn-Valero de Barnabè D, van Bokoven H, Squarzoni S, Merlini L (2003) Extracellular matrix and nuclear abnormalities in skeletal muscle of a patient with Walker-Warburg syndrome caused by POMT1 mutation. Biochim Biophys Acta 1638: 57-62. 
• Santavuori P, Leisti J, Kruus S (1977) Muscle, eye and brain disease: a new syndrome. Neuropediatrie 8 (Suppl): 553-558.
• Sparrow DB, Chapman G, Wouters MA, Whittock NV, Ellard S, Fatkin D, Turnpenny PD, Kusumi K, Sillence D, Dunwoodie SL (2006) Mutation of the lunatic fringe gene in humans causes spondylocostal dysostosis with a severe vertebral phenotype. Am J Hum Genet 78: 28-37. 
• Spiro RG (2002) Protein glycosylation: nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds. Glycobiology 12: 43R-56R. 
• Ten Hagen KG, Fritz TA, Tabak LA (2003) All in the family: the UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferases. Glycobiology 13: 1R-16R. 
• Topaz O, Bergman R, Mandel U, Maor G, Goldberg R, Richard G, Sprecher E (2005) Absence of intraepidermal glycosyltransferase ppGalNac-T3 expression in familial tumoral calcinosis. Am J Dermatopathol 27: 211-215. 
• Topaz O, Shurman DL, Bergman R, Indelman M, Ratajczak P, Mizrachi M, Khamaysi Z, Behar D, Petronius D, Friedman V, Zelikovic I, Raimer S, Metzker A, Richard G, Sprecher E (2004) Mutations in GALNT3, encoding a protein involved in O-linked glycosylation, cause familial tumoral calcinosis. Nat Genet 36: 579-581. 
• Tucker RP (2004) The thrombospondin type 1 repeat superfamily. Int J Biochem Cell Biol 36: 969-974. 
• Vaith P, Assmann G, Uhlenbruck G (1978) Characterization of the oligosaccharide side chain of apolipoprotein C-III from human plasma very low density lipoproteins. Biochim Biophys Acta 541: 234-240. 
• van Reeuwijk J, Janssen M, van den Elzen C, Beltran-Valero de Bernabe D, Sabatelli P, Merlini L, Boon M, Scheffer H, Brockington M, Muntoni F, Huynen MA, Verrips A, Walsh CA, Barth PG, Brunner HG, van Bokhoven H (2005) POMT2 mutations cause α-dystroglycan hypoglycosylation and Walker-Warburg syndrome. J Med Genet 42: 907-912. 
• Walker AE (1942) Lissencephaly. Arch Neurol Psychiat 48: 13-29.
• Wopereis S, Abd Hamid UM, Critchley A, Royle L, Dwek RA, Morava E, Leroy JG, Wilcken B, Lagerwerf AJ, Huijben KM, Lefeber DJ, Rudd PM, Wevers RA (2006) Abnormal glycosylation with hypersialylated O-glycans in patients with Sialuria. Biochim Biophys Acta 1762: 598-607. 
• Wopereis S, Grunewald S, Huijben KM, Morava E, Mollicone R, van Engelen BG, Lefeber DJ, Wevers RA (2007) Transferrin and apolipoprotein C-III isofocusing are complementary in the diagnosis of N- and O-glycan biosynthesis defects. Clin Chem 53: 180-187. 
• Wopereis S, Grunewald S, Morava E, Penzien JM, Briones P, Garcia-Silva MT, Demacker PN, Huijben KM, Wevers RA (2003) Apolipoprotein C-III isofocusing in the diagnosis of genetic defects in O-glycan biosynthesis. Clin Chem 49: 1839-1845. 
• Wopereis S, Lefeber DJ, Morava E, Wevers RA (2006a) Mechanisms in protein O-glycan Biosynthesis and clinical and molecular aspects of protein O-glycan biosynthesis defects: a review. Clin Chem 52: 574-600. 
• Wopereis S, Morava E, Grunewald S, Mills PB, Winchester BG, Clayton P, Coucke P, Huijben KM, Wevers RA (2005) A combined defect in the biosynthesis of N- and O-glycans in patients with cutis laxa and neurological involvement: the biochemical characteristics. Biochim Biophys Acta 1741: 156-164. 
• Zauner G, Kozak RP, Gardner RA, Fernandes DL, Deelder AM, Wuhrer M (2012) Protein O-glycosylation analysis. Biol Chem 393: 687-708. 
• Zhang W, Vajsar J, Cao P, Breningstall G, Diesen C, Dobyns W, Herrmann R, Lehesjoki AE, Steinbrecher A, Talim B, Toda T, Topaloglu H, Voit T, Schachter H (2003) Enzymatic diagnostic test for muscle-eye-brain type congenital muscular dystrophy using commercially available reagents. Clin Biochem 36: 339-344.