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SLC39A8 Deficiency: A Disorder of Manganese Transport and Glycosylation

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SLC39A8 Deficiency: A Disorder of Manganese Transport and Glycosylation. / Park, Julien H; Hogrebe, Max; Grüneberg, Marianne; DuChesne, Ingrid; von der Heiden, Ava L; Reunert, Janine; Schlingmann, Karl P; Boycott, Kym M; Beaulieu, Chandree L; Mhanni, Aziz A; Innes, A Micheil; Hörtnagel, Konstanze; Biskup, Saskia; Gleixner, Eva M; Kurlemann, Gerhard; Fiedler, Barbara; Omran, Heymut; Rutsch, Frank; Wada, Yoshinao; Tsiakas, Konstantinos; Santer, René; Nebert, Daniel W; Rust, Stephan; Marquardt, Thorsten.

In: AM J HUM GENET, Vol. 97, No. 6, 03.12.2015, p. 894-903.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Park, JH, Hogrebe, M, Grüneberg, M, DuChesne, I, von der Heiden, AL, Reunert, J, Schlingmann, KP, Boycott, KM, Beaulieu, CL, Mhanni, AA, Innes, AM, Hörtnagel, K, Biskup, S, Gleixner, EM, Kurlemann, G, Fiedler, B, Omran, H, Rutsch, F, Wada, Y, Tsiakas, K, Santer, R, Nebert, DW, Rust, S & Marquardt, T 2015, 'SLC39A8 Deficiency: A Disorder of Manganese Transport and Glycosylation', AM J HUM GENET, vol. 97, no. 6, pp. 894-903. https://doi.org/10.1016/j.ajhg.2015.11.003

APA

Park, J. H., Hogrebe, M., Grüneberg, M., DuChesne, I., von der Heiden, A. L., Reunert, J., Schlingmann, K. P., Boycott, K. M., Beaulieu, C. L., Mhanni, A. A., Innes, A. M., Hörtnagel, K., Biskup, S., Gleixner, E. M., Kurlemann, G., Fiedler, B., Omran, H., Rutsch, F., Wada, Y., ... Marquardt, T. (2015). SLC39A8 Deficiency: A Disorder of Manganese Transport and Glycosylation. AM J HUM GENET, 97(6), 894-903. https://doi.org/10.1016/j.ajhg.2015.11.003

Vancouver

Park JH, Hogrebe M, Grüneberg M, DuChesne I, von der Heiden AL, Reunert J et al. SLC39A8 Deficiency: A Disorder of Manganese Transport and Glycosylation. AM J HUM GENET. 2015 Dec 3;97(6):894-903. https://doi.org/10.1016/j.ajhg.2015.11.003

Bibtex

@article{697acafea1374192b1035b237cd77f18,
title = "SLC39A8 Deficiency: A Disorder of Manganese Transport and Glycosylation",
abstract = "SLC39A8 is a membrane transporter responsible for manganese uptake into the cell. Via whole-exome sequencing, we studied a child that presented with cranial asymmetry, severe infantile spasms with hypsarrhythmia, and dysproportionate dwarfism. Analysis of transferrin glycosylation revealed severe dysglycosylation corresponding to a type II congenital disorder of glycosylation (CDG) and the blood manganese levels were below the detection limit. The variants c.112G>C (p.Gly38Arg) and c.1019T>A (p.Ile340Asn) were identified in SLC39A8. A second individual with the variants c.97G>A (p.Val33Met) and c.1004G>C (p.Ser335Thr) on the paternal allele and c.610G>T (p.Gly204Cys) on the maternal allele was identified among a group of unresolved case subjects with CDG. These data demonstrate that variants in SLC39A8 impair the function of manganese-dependent enzymes, most notably β-1,4-galactosyltransferase, a Golgi enzyme essential for biosynthesis of the carbohydrate part of glycoproteins. Impaired galactosylation leads to a severe disorder with deformed skull, severe seizures, short limbs, profound psychomotor retardation, and hearing loss. Oral galactose supplementation is a treatment option and results in complete normalization of glycosylation. SLC39A8 deficiency links a trace element deficiency with inherited glycosylation disorders.",
author = "Park, {Julien H} and Max Hogrebe and Marianne Gr{\"u}neberg and Ingrid DuChesne and {von der Heiden}, {Ava L} and Janine Reunert and Schlingmann, {Karl P} and Boycott, {Kym M} and Beaulieu, {Chandree L} and Mhanni, {Aziz A} and Innes, {A Micheil} and Konstanze H{\"o}rtnagel and Saskia Biskup and Gleixner, {Eva M} and Gerhard Kurlemann and Barbara Fiedler and Heymut Omran and Frank Rutsch and Yoshinao Wada and Konstantinos Tsiakas and Ren{\'e} Santer and Nebert, {Daniel W} and Stephan Rust and Thorsten Marquardt",
note = "Copyright {\textcopyright} 2015 The American Society of Human Genetics. Published by Elsevier Inc. All rights reserved.",
year = "2015",
month = dec,
day = "3",
doi = "10.1016/j.ajhg.2015.11.003",
language = "English",
volume = "97",
pages = "894--903",
journal = "AM J HUM GENET",
issn = "0002-9297",
publisher = "Cell Press",
number = "6",

}

RIS

TY - JOUR

T1 - SLC39A8 Deficiency: A Disorder of Manganese Transport and Glycosylation

AU - Park, Julien H

AU - Hogrebe, Max

AU - Grüneberg, Marianne

AU - DuChesne, Ingrid

AU - von der Heiden, Ava L

AU - Reunert, Janine

AU - Schlingmann, Karl P

AU - Boycott, Kym M

AU - Beaulieu, Chandree L

AU - Mhanni, Aziz A

AU - Innes, A Micheil

AU - Hörtnagel, Konstanze

AU - Biskup, Saskia

AU - Gleixner, Eva M

AU - Kurlemann, Gerhard

AU - Fiedler, Barbara

AU - Omran, Heymut

AU - Rutsch, Frank

AU - Wada, Yoshinao

AU - Tsiakas, Konstantinos

AU - Santer, René

AU - Nebert, Daniel W

AU - Rust, Stephan

AU - Marquardt, Thorsten

N1 - Copyright © 2015 The American Society of Human Genetics. Published by Elsevier Inc. All rights reserved.

PY - 2015/12/3

Y1 - 2015/12/3

N2 - SLC39A8 is a membrane transporter responsible for manganese uptake into the cell. Via whole-exome sequencing, we studied a child that presented with cranial asymmetry, severe infantile spasms with hypsarrhythmia, and dysproportionate dwarfism. Analysis of transferrin glycosylation revealed severe dysglycosylation corresponding to a type II congenital disorder of glycosylation (CDG) and the blood manganese levels were below the detection limit. The variants c.112G>C (p.Gly38Arg) and c.1019T>A (p.Ile340Asn) were identified in SLC39A8. A second individual with the variants c.97G>A (p.Val33Met) and c.1004G>C (p.Ser335Thr) on the paternal allele and c.610G>T (p.Gly204Cys) on the maternal allele was identified among a group of unresolved case subjects with CDG. These data demonstrate that variants in SLC39A8 impair the function of manganese-dependent enzymes, most notably β-1,4-galactosyltransferase, a Golgi enzyme essential for biosynthesis of the carbohydrate part of glycoproteins. Impaired galactosylation leads to a severe disorder with deformed skull, severe seizures, short limbs, profound psychomotor retardation, and hearing loss. Oral galactose supplementation is a treatment option and results in complete normalization of glycosylation. SLC39A8 deficiency links a trace element deficiency with inherited glycosylation disorders.

AB - SLC39A8 is a membrane transporter responsible for manganese uptake into the cell. Via whole-exome sequencing, we studied a child that presented with cranial asymmetry, severe infantile spasms with hypsarrhythmia, and dysproportionate dwarfism. Analysis of transferrin glycosylation revealed severe dysglycosylation corresponding to a type II congenital disorder of glycosylation (CDG) and the blood manganese levels were below the detection limit. The variants c.112G>C (p.Gly38Arg) and c.1019T>A (p.Ile340Asn) were identified in SLC39A8. A second individual with the variants c.97G>A (p.Val33Met) and c.1004G>C (p.Ser335Thr) on the paternal allele and c.610G>T (p.Gly204Cys) on the maternal allele was identified among a group of unresolved case subjects with CDG. These data demonstrate that variants in SLC39A8 impair the function of manganese-dependent enzymes, most notably β-1,4-galactosyltransferase, a Golgi enzyme essential for biosynthesis of the carbohydrate part of glycoproteins. Impaired galactosylation leads to a severe disorder with deformed skull, severe seizures, short limbs, profound psychomotor retardation, and hearing loss. Oral galactose supplementation is a treatment option and results in complete normalization of glycosylation. SLC39A8 deficiency links a trace element deficiency with inherited glycosylation disorders.

U2 - 10.1016/j.ajhg.2015.11.003

DO - 10.1016/j.ajhg.2015.11.003

M3 - SCORING: Journal article

C2 - 26637979

VL - 97

SP - 894

EP - 903

JO - AM J HUM GENET

JF - AM J HUM GENET

SN - 0002-9297

IS - 6

ER -