Molecular order in mucolipidosis II and III nomenclature [1]

American Journal of Medical Genetics, Part A

Volumn 146, Issue 4, 2008, Pages 512-513

  Cathey, Sara S ^a   Kudo, Mariko ^b   Tiede, Stephan ^c   Raas Rothschild, Annick ^d   Braulke, Thomas ^e   Beck, Michael ^f   Taylor, Harold A ^a   Canfield, William M ^b   Leroy, Jules G ^a   Neufeld, Elizabeth F ^g   McKusick, Victor A ^h  

^a GREENWOOD GENETIC CENTER   (United States)

^b GENZYME CORPORATION   (United States)

^c UNIVERSITY HOSPITAL SCHLESWIG HOLSTEIN   (Germany)

^d HADASSAH HEBREW UNIVERSITY MEDICAL CENTER   (Israel)

^e UNIVERSITY OF HAMBURG   (Germany)

^f JOHANNES GUTENBERG UNIVERSITY   (Germany)

^g UNIVERSITY OF CALIFORNIA   (United States)

^h JOHNS HOPKINS HOSPITAL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

LYSOSOME ENZYME; MANNOSE 6 PHOSPHATE; URIDINE TRIPHOSPHATE GLUCOSE 1 PHOSPHATE URIDYLYLTRANSFERASE;

CHROMOSOME 16P; DISEASE CLASSIFICATION; ENZYME SYNTHESIS; GENE; GENE LOCATION; GENE MUTATION; GNPTG GENE; HUMAN; LETTER; MOLECULAR GENETICS; MUCOLIPIDOSIS; MUCOLIPIDOSIS TYPE 1; MUCOLIPIDOSIS TYPE 2; NOMENCLATURE; PRIORITY JOURNAL; URINARY EXCRETION;

CONGRESSES AS TOPIC; HUMANS; MUCOLIPIDOSES; TERMINOLOGY AS TOPIC; TRANSFERASES (OTHER SUBSTITUTED PHOSPHATE GROUPS);

EID: 38849161560     PISSN: 15524825     EISSN: 15524833     Source Type: Journal    
DOI: 10.1002/ajmg.a.32193     Document Type: Letter

References (16)

1. Bao M, Booth JL, Elmendorf BJ, Canfield WM. 1996. Bovine UDP-N-acetylglucosamine: Lysosomal enzyme N-acetylglucosamine-1- phosphotransferase. I. Purification and subunit structure. J Biol Chem 271:31437-31445.
2. Cathey S, Friez M, Wood T, Eaves K, Leroy J. 2007. Exploring mucolipidosis II and III. Mol Genet Metab 90:240.
3. Hasilik A, Neufeld EF. 1980. Biosynthesis of lysosomal enzyme in fibroblasts. Phosphorylation of mannose residues. J Biol Chem 255:4946-4950.
4. Hasilik A, Waheed A, von Figura K. 1981. Enzymatic phosphorylation of lysosomal enzymes in the presence of UDP-N-acetylglucosamine. Absence of the activity in I-cell fibroblasts. Biochem Biophys Res Commun 98:761-767.
5. Honey NK, Mueller OT, Little LE, Miller AL, Shows TB. 1982. Mucolipidosis III is genetically heterogeneous. Proc Natl Acad Sci USA 79:7420-7424.
6. Kaplan A, Achord DT, Sly WS. 1977. Phosphohexosyl components of a lysosomal enzyme are recognized by pinocytosis receptors on human fibroblasts. Proc Natl Acad Sci USA 74:2026-2030.
7. Kudo M, Bao M, D'Souza A, Ying F, Pan H, Roe BA, Canfield WM. 2005. The α- and β-subunits of the human UPD-N-acetylglucosamine: Lysosomal enzyme N-acetylglucosamine-1-phosphotransferase are encoded by a single cDNA. J Biol Chem 280:36141-36149.
8. Kudo M, Brem MS, Canfield WM. 2006. Mucolipidosis II (I-cell disease) and mucolipidosis IIIA (classical pseudo-Hurler polydystrophy) are caused by mutations in the GlcNAc-phosphotransferase α/β-subunits precursor gene. Am J Hum Genet 78:451-463.
9. Leroy JG, Spranger JW, Feingold M, Opitz JM, Crocker AC. 1971. I-cell disease: A clinical picture. J Pediatr 79:360-365.
10. Maroteaux P, Lamy M. 1966. La pseudopolydystrophie de Hurler. Presse Méd 74:2889-2892.
11. OMIM. 2007. Online Mendelian Inheritance in Man. http://www.ncbi.nlm.nih. gov/omim/.
12. Paik KH, Song SM, Ki CS, Hu H-W, Kim JS, Min KH, Chang SH, Yoo EJ, Lee IJ, Kwan EK, Han SJ, Jin D-K. 2005. Identification of mutations in the GNPTA (MGC4170) gene coding for GlcNAc-phosphotransferase α/β subunits in Korean patients with mucolipidosis Type II or Type IIIA. Hum Mut 26:308-314.
13. Raas-Rothschild A, Cormier-Daire V, Bao M, Genin E, Salomon R, Brewer K, Zeigler M, Mandel H, Toth S, Roe B, Munnich A, Canfield WM. 2000. Molecular basis of variant pseudo-Hurler polydystrophy (mucolipidosis IIIC). J Clin Invest 105:673-681.
14. Reitman ML, Varki A, Kornfeld S. 1981. Fibroblasts from patients with I-cell disease and pseudo-Hurler polydystrophy are deficient in uridine 5′-diphosphate N-acetylglucosamine: Glycoprotein N-acetylglucosaminylphosphotransferase activity. J Clin Invest 67:1574-1579.
15. Shows TB, Mueller OT, Honey NK, Wright CE, Miller AL. 1982. Genetic heterogeneity of I-Cell disease is demonstrated by complementation of lysosomal enzyme processing mutants. Am J Med Genet 12:343-353.
16. Tiede S, Storch S, Lübke T, Henrissat B, Bargal R, Raas-Rothschild A, Braulke T. 2005. Mucolipidosis II is caused by mutations in GNPTA encoding the α/β GlcNAc-1-phosphotransferase. Nat Med 11:1109-1112.