The homozygous M712T mutation of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase results in reduced enzyme activities but not in altered overall cellular sialylation in hereditary inclusion body myopathy

Stephan Hinderlich; Ilan Salama; Iris Eisenberg; Tamara Potikha; Lars R. Mantey; Kevin J. Yarema; Rüdiger Horstkorte; Zohar Argov; Menachem Sadeh; Werner Reutter; Stella Mitrani-Rosenbaum

doi:10.1016/j.febslet.2004.04.013

The homozygous M712T mutation of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase results in reduced enzyme activities but not in altered overall cellular sialylation in hereditary inclusion body myopathy

Stephan Hinderlich, Ilan Salama, Iris Eisenberg, Tamara Potikha, Lars R. Mantey, Kevin J. Yarema, Rüdiger Horstkorte, Zohar Argov, Menachem Sadeh, Werner Reutter, Stella Mitrani-Rosenbaum

Research output: Contribution to journal › Article › peer-review

60 Scopus citations

Abstract

Hereditary inclusion body myopathy (HIBM) is a neuromuscular disorder, caused by mutations in UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase, the key enzyme of sialic acid biosynthesis. In Middle Eastern patients a single homozygous mutation occurs, converting methionine-712 to threonine. Recombinant expression of the mutated enzyme revealed slightly reduced N-acetylmannosamine kinase activity, in agreement with the localization of the mutation within the kinase domain. B lymphoblastoid cell lines derived from patients expressing the mutated enzyme also display reduced UDP-N- acetylglucosamine 2-epimerase activity. Nevertheless, no reduced cellular sialylation was found in those cells by colorimetric assays and lectin analysis, indicating that HIBM is not directly caused by an altered overall expression of sialic acids.

Original language	English (US)
Pages (from-to)	105-109
Number of pages	5
Journal	FEBS Letters
Volume	566
Issue number	1-3
DOIs	https://doi.org/10.1016/j.febslet.2004.04.013
State	Published - May 21 2004
Externally published	Yes

Keywords

GNE
GNE, UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
HIBM, hereditary inclusion body myopathy
Hereditary inclusion body myopathy
ManNAc kinase, N-acetylmannosamine kinase
UDP-GlcNAc 2-epimerase, UDP-N-acetylglucosamine 2-epimerase

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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Hinderlich, S., Salama, I., Eisenberg, I., Potikha, T., Mantey, L. R., Yarema, K. J., Horstkorte, R., Argov, Z., Sadeh, M., Reutter, W., & Mitrani-Rosenbaum, S. (2004). The homozygous M712T mutation of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase results in reduced enzyme activities but not in altered overall cellular sialylation in hereditary inclusion body myopathy. FEBS Letters, 566(1-3), 105-109. https://doi.org/10.1016/j.febslet.2004.04.013

The homozygous M712T mutation of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase results in reduced enzyme activities but not in altered overall cellular sialylation in hereditary inclusion body myopathy. / Hinderlich, Stephan; Salama, Ilan; Eisenberg, Iris et al.
In: FEBS Letters, Vol. 566, No. 1-3, 21.05.2004, p. 105-109.

Research output: Contribution to journal › Article › peer-review

Hinderlich, S, Salama, I, Eisenberg, I, Potikha, T, Mantey, LR, Yarema, KJ, Horstkorte, R, Argov, Z, Sadeh, M, Reutter, W & Mitrani-Rosenbaum, S 2004, 'The homozygous M712T mutation of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase results in reduced enzyme activities but not in altered overall cellular sialylation in hereditary inclusion body myopathy', FEBS Letters, vol. 566, no. 1-3, pp. 105-109. https://doi.org/10.1016/j.febslet.2004.04.013

Hinderlich S, Salama I, Eisenberg I, Potikha T, Mantey LR, Yarema KJ et al. The homozygous M712T mutation of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase results in reduced enzyme activities but not in altered overall cellular sialylation in hereditary inclusion body myopathy. FEBS Letters. 2004 May 21;566(1-3):105-109. doi: 10.1016/j.febslet.2004.04.013

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title = "The homozygous M712T mutation of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase results in reduced enzyme activities but not in altered overall cellular sialylation in hereditary inclusion body myopathy",

abstract = "Hereditary inclusion body myopathy (HIBM) is a neuromuscular disorder, caused by mutations in UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase, the key enzyme of sialic acid biosynthesis. In Middle Eastern patients a single homozygous mutation occurs, converting methionine-712 to threonine. Recombinant expression of the mutated enzyme revealed slightly reduced N-acetylmannosamine kinase activity, in agreement with the localization of the mutation within the kinase domain. B lymphoblastoid cell lines derived from patients expressing the mutated enzyme also display reduced UDP-N- acetylglucosamine 2-epimerase activity. Nevertheless, no reduced cellular sialylation was found in those cells by colorimetric assays and lectin analysis, indicating that HIBM is not directly caused by an altered overall expression of sialic acids.",

keywords = "GNE, GNE, UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase, HIBM, hereditary inclusion body myopathy, Hereditary inclusion body myopathy, ManNAc kinase, N-acetylmannosamine kinase, UDP-GlcNAc 2-epimerase, UDP-N-acetylglucosamine 2-epimerase",

author = "Stephan Hinderlich and Ilan Salama and Iris Eisenberg and Tamara Potikha and Mantey, {Lars R.} and Yarema, {Kevin J.} and R{\"u}diger Horstkorte and Zohar Argov and Menachem Sadeh and Werner Reutter and Stella Mitrani-Rosenbaum",

note = "Funding Information: This work was supported by the Fritz-Thyssen-Stiftung, K{\"o}ln, Germany, the German-Israeli Foundation for Science Research & Development, Jerusalem, Israel, the Mizutani Foundation for Glycoscience, Japan, the Fonds der Chemischen Industrie, Frankfurt/Main, Germany, and the Sonnenfeld-Stiftung, Berlin, Germany.",

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doi = "10.1016/j.febslet.2004.04.013",

language = "English (US)",

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T1 - The homozygous M712T mutation of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase results in reduced enzyme activities but not in altered overall cellular sialylation in hereditary inclusion body myopathy

AU - Hinderlich, Stephan

AU - Salama, Ilan

AU - Eisenberg, Iris

AU - Potikha, Tamara

AU - Mantey, Lars R.

AU - Yarema, Kevin J.

AU - Horstkorte, Rüdiger

AU - Argov, Zohar

AU - Sadeh, Menachem

AU - Reutter, Werner

AU - Mitrani-Rosenbaum, Stella

N1 - Funding Information: This work was supported by the Fritz-Thyssen-Stiftung, Köln, Germany, the German-Israeli Foundation for Science Research & Development, Jerusalem, Israel, the Mizutani Foundation for Glycoscience, Japan, the Fonds der Chemischen Industrie, Frankfurt/Main, Germany, and the Sonnenfeld-Stiftung, Berlin, Germany.

PY - 2004/5/21

Y1 - 2004/5/21

N2 - Hereditary inclusion body myopathy (HIBM) is a neuromuscular disorder, caused by mutations in UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase, the key enzyme of sialic acid biosynthesis. In Middle Eastern patients a single homozygous mutation occurs, converting methionine-712 to threonine. Recombinant expression of the mutated enzyme revealed slightly reduced N-acetylmannosamine kinase activity, in agreement with the localization of the mutation within the kinase domain. B lymphoblastoid cell lines derived from patients expressing the mutated enzyme also display reduced UDP-N- acetylglucosamine 2-epimerase activity. Nevertheless, no reduced cellular sialylation was found in those cells by colorimetric assays and lectin analysis, indicating that HIBM is not directly caused by an altered overall expression of sialic acids.

AB - Hereditary inclusion body myopathy (HIBM) is a neuromuscular disorder, caused by mutations in UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase, the key enzyme of sialic acid biosynthesis. In Middle Eastern patients a single homozygous mutation occurs, converting methionine-712 to threonine. Recombinant expression of the mutated enzyme revealed slightly reduced N-acetylmannosamine kinase activity, in agreement with the localization of the mutation within the kinase domain. B lymphoblastoid cell lines derived from patients expressing the mutated enzyme also display reduced UDP-N- acetylglucosamine 2-epimerase activity. Nevertheless, no reduced cellular sialylation was found in those cells by colorimetric assays and lectin analysis, indicating that HIBM is not directly caused by an altered overall expression of sialic acids.

KW - GNE

KW - GNE, UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase

KW - HIBM, hereditary inclusion body myopathy

KW - Hereditary inclusion body myopathy

KW - ManNAc kinase, N-acetylmannosamine kinase

KW - UDP-GlcNAc 2-epimerase, UDP-N-acetylglucosamine 2-epimerase

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The homozygous M712T mutation of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase results in reduced enzyme activities but not in altered overall cellular sialylation in hereditary inclusion body myopathy

Abstract

Keywords

ASJC Scopus subject areas

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