Molekulargenetische Diagnostik
Praxis Dr. Mato Nagel

Polypeptide N-acetylgalactosaminyltransferase 3

Das vom GALNT3-Gen kodierte Protein UDP-GalNAc ist für die O-Glykosilierung des Proproteins (FGF23) verantwortlich. Die O-Glycosilierung ist für die Aktivierung des FGF23 verantwortlich, so dass funktionsmindernde Mutationen zu einer verstärkten FGF23-Abbau und damit zu einer verminderten Sekretion führen. Inaktivierende Mutation führen zur autosomal rezessiven hyperphosphatämischen familiären Tumorcalcinose.

Genregulation

Das vom GALNT3-Gen kodierte Protein UDP-GalNAc ist für die

Diagnostik:

Clinic Untersuchungsmethoden Familienuntersuchung
Bearbeitungszeit 5
Probentyp genomic DNA
Clinic Untersuchungsmethoden Direkte Sequenzierung der proteinkodierenden Bereiche eines Gens
Bearbeitungszeit 25
Probentyp genomic DNA
Clinic Untersuchungsmethoden Hochdurchsatz-Sequenzierung
Bearbeitungszeit 25
Probentyp genomic DNA

Krankheiten:

Hyperphosphatämische familiäre Tumorcalcinose
FGF23
GALNT3
KL

Referenzen:

1.

Steinherz R et. al. (1985) Elevated serum calcitriol concentrations do not fall in response to hyperphosphatemia in familial tumoral calcinosis.

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2.

Lyles KW et. al. (1985) Genetic transmission of tumoral calcinosis: autosomal dominant with variable clinical expressivity.

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3.

Slavin RE et. al. (1993) Familial tumoral calcinosis. A clinical, histopathologic, and ultrastructural study with an analysis of its calcifying process and pathogenesis.

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4.

Bennett EP et. al. (1996) cDNA cloning and expression of a novel human UDP-N-acetyl-alpha-D-galactosamine. Polypeptide N-acetylgalactosaminyltransferase, GalNAc-t3.

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5.

Zara J et. al. (1996) Cloning and expression of mouse UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-T3.

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6.

Bennett EP et. al. (1998) Genomic organization and chromosomal localization of three members of the UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferase family.

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7.

MCPHAUL JJ et. al. (1961) Heterotopic calcification, hyperphosphatemia and angioid streaks of the retina.

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8.

Topaz O et. al. (2004) Mutations in GALNT3, encoding a protein involved in O-linked glycosylation, cause familial tumoral calcinosis.

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9.

Frishberg Y et. al. (2005) Identification of a recurrent mutation in GALNT3 demonstrates that hyperostosis-hyperphosphatemia syndrome and familial tumoral calcinosis are allelic disorders.

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10.

Ichikawa S et. al. (2005) A novel GALNT3 mutation in a pseudoautosomal dominant form of tumoral calcinosis: evidence that the disorder is autosomal recessive.

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11.

Specktor P et. al. (2006) Hyperphosphatemic familial tumoral calcinosis caused by a mutation in GALNT3 in a European kindred.

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12.

Kato K et. al. (2006) Polypeptide GalNAc-transferase T3 and familial tumoral calcinosis. Secretion of fibroblast growth factor 23 requires O-glycosylation.

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13.

Ichikawa S et. al. (2006) Tumoral calcinosis presenting with eyelid calcifications due to novel missense mutations in the glycosyl transferase domain of the GALNT3 gene.

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14.

Ichikawa S et. al. (2007) Novel GALNT3 mutations causing hyperostosis-hyperphosphatemia syndrome result in low intact fibroblast growth factor 23 concentrations.

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15.

Barbieri AM et. al. (2007) Two novel nonsense mutations in GALNT3 gene are responsible for familial tumoral calcinosis.

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16.

Laleye A et. al. (2008) Tumoral calcinosis due to GALNT3 C.516-2A >T mutation in a black African family.

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17.

Ichikawa S et. al. (2010) Clinical variability of familial tumoral calcinosis caused by novel GALNT3 mutations.

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