Fabry disease: Characterization of α-galactosidase A double mutations and the D313Y plasma enzyme pseudodeficiency allele
Fabry disease, an X‐linked inborn error of glycosphingolipid catabolism, results from mutations in the gene encoding the lysosomal exoglycohydrolase, α‐galactosidase A (α‐Gal A; GLA). In two unrelated classically affected males, two α‐Gal A missense mutations were identified: R112C + D313Y (c.334C&g...
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Published in | Human mutation Vol. 22; no. 6; pp. 486 - 492 |
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Abstract | Fabry disease, an X‐linked inborn error of glycosphingolipid catabolism, results from mutations in the gene encoding the lysosomal exoglycohydrolase, α‐galactosidase A (α‐Gal A; GLA). In two unrelated classically affected males, two α‐Gal A missense mutations were identified: R112C + D313Y (c.334C>T + c.937G>T) and C172G + D313Y (c.514T>G + c.937G>T). The D313Y lesion was previously identified in classically affected males as the single mutation [Eng et al., 1993] or in cis with another missense mutation, D313Y + G411D (c.937G>T + c.1232G>A) [Guffon et al., 1998]. To determine whether the D313Y mutation was a deleterious mutation or a coding region sequence variant, the frequency of D313Y in normal X‐chromosomes, as well as its enzymatic activity and subcellular localization in COS‐7 cells was determined. D313Y occurred in 0.45% of 883 normal X‐chromosomes, while the R112C, C172G, and G411D missense mutations were not detected in over 500 normal X‐chromosomes. Expression of D313Y in COS‐7 cells resulted in& tilde;60% of wild‐type enzymatic activity and showed lysosomal localization, while R112C, C172G, G411D, and the double‐mutated constructs had markedly reduced or no detectable activity and were all retained in the endoplasmic reticulum. The expressed D313Y enzyme was stable at lysosomal pH (pH 4.6), while at neutral pH (pH 7.4), it had decreased activity. A molecular homology model of human α‐Gal A, based on the X‐ray crystal structure of chicken α‐galactosidase B (α‐Gal B; α‐N‐acetylgalactosaminidase) was generated [Garman et al., 2002], which provided evidence that D313Y did not markedly disrupt the α‐Gal A enzyme structure. Thus, D313Y is a rare exonic variant with about 60% of wild‐type activity in vitro and reduced activity at neutral pH, resulting in low plasma α‐Gal A activity. Hum Mutat 22:486–492, 2003. © 2003 Wiley‐Liss, Inc. |
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AbstractList | Fabry disease, an X-linked inborn error of glycosphingolipid catabolism, results from mutations in the gene encoding the lysosomal exoglycohydrolase, alpha-galactosidase A (alpha-Gal A; GLA). In two unrelated classically affected males, two alpha-Gal A missense mutations were identified: R112C + D313Y (c.334C>T + c.937G>T) and C172G + D313Y (c.514T>G + c.937G>T). The D313Y lesion was previously identified in classically affected males as the single mutation [Eng et al., 1993] or in cis with another missense mutation, D313Y + G411D (c.937G>T + c.1232G>A) [Guffon et al., 1998]. To determine whether the D313Y mutation was a deleterious mutation or a coding region sequence variant, the frequency of D313Y in normal X-chromosomes, as well as its enzymatic activity and subcellular localization in COS-7 cells was determined. D313Y occurred in 0.45% of 883 normal X-chromosomes, while the R112C, C172G, and G411D missense mutations were not detected in over 500 normal X-chromosomes. Expression of D313Y in COS-7 cells resulted in approximately 60% of wild-type enzymatic activity and showed lysosomal localization, while R112C, C172G, G411D, and the double-mutated constructs had markedly reduced or no detectable activity and were all retained in the endoplasmic reticulum. The expressed D313Y enzyme was stable at lysosomal pH (pH 4.6), while at neutral pH (pH 7.4), it had decreased activity. A molecular homology model of human alpha-Gal A, based on the X-ray crystal structure of chicken alpha-galactosidase B (alpha-Gal B; alpha-N-acetylgalactosaminidase) was generated [Garman et al., 2002], which provided evidence that D313Y did not markedly disrupt the alpha-Gal A enzyme structure. Thus, D313Y is a rare exonic variant with about 60% of wild-type activity in vitro and reduced activity at neutral pH, resulting in low plasma alpha-Gal A activity. Fabry disease, an X-linked inborn error of glycosphingolipid catabolism, results from mutations in the gene encoding the lysosomal exoglycohydrolase, alpha-galactosidase A (alpha-Gal A; GLA). In two unrelated classically affected males, two alpha-Gal A missense mutations were identified: R112C + D313Y (c.334C>T + c.937G>T) and C172G + D313Y (c.514T>G + c.937G>T). The D313Y lesion was previously identified in classically affected males as the single mutation [Eng et al., 1993] or in cis with another missense mutation, D313Y + G411D (c.937G>T + c.1232G>A) [Guffon et al., 1998]. To determine whether the D313Y mutation was a deleterious mutation or a coding region sequence variant, the frequency of D313Y in normal X-chromosomes, as well as its enzymatic activity and subcellular localization in COS-7 cells was determined. D313Y occurred in 0.45% of 883 normal X-chromosomes, while the R112C, C172G, and G411D missense mutations were not detected in over 500 normal X-chromosomes. Expression of D313Y in COS-7 cells resulted in approximately 60% of wild-type enzymatic activity and showed lysosomal localization, while R112C, C172G, G411D, and the double-mutated constructs had markedly reduced or no detectable activity and were all retained in the endoplasmic reticulum. The expressed D313Y enzyme was stable at lysosomal pH (pH 4.6), while at neutral pH (pH 7.4), it had decreased activity. A molecular homology model of human alpha-Gal A, based on the X-ray crystal structure of chicken alpha-galactosidase B (alpha-Gal B; alpha-N-acetylgalactosaminidase) was generated [Garman et al., 2002], which provided evidence that D313Y did not markedly disrupt the alpha-Gal A enzyme structure. Thus, D313Y is a rare exonic variant with about 60% of wild-type activity in vitro and reduced activity at neutral pH, resulting in low plasma alpha-Gal A activity. Fabry disease, an X‐linked inborn error of glycosphingolipid catabolism, results from mutations in the gene encoding the lysosomal exoglycohydrolase, α‐galactosidase A (α‐Gal A; GLA). In two unrelated classically affected males, two α‐Gal A missense mutations were identified: R112C + D313Y (c.334C>T + c.937G>T) and C172G + D313Y (c.514T>G + c.937G>T). The D313Y lesion was previously identified in classically affected males as the single mutation [Eng et al., 1993] or in cis with another missense mutation, D313Y + G411D (c.937G>T + c.1232G>A) [Guffon et al., 1998]. To determine whether the D313Y mutation was a deleterious mutation or a coding region sequence variant, the frequency of D313Y in normal X‐chromosomes, as well as its enzymatic activity and subcellular localization in COS‐7 cells was determined. D313Y occurred in 0.45% of 883 normal X‐chromosomes, while the R112C, C172G, and G411D missense mutations were not detected in over 500 normal X‐chromosomes. Expression of D313Y in COS‐7 cells resulted in& tilde;60% of wild‐type enzymatic activity and showed lysosomal localization, while R112C, C172G, G411D, and the double‐mutated constructs had markedly reduced or no detectable activity and were all retained in the endoplasmic reticulum. The expressed D313Y enzyme was stable at lysosomal pH (pH 4.6), while at neutral pH (pH 7.4), it had decreased activity. A molecular homology model of human α‐Gal A, based on the X‐ray crystal structure of chicken α‐galactosidase B (α‐Gal B; α‐N‐acetylgalactosaminidase) was generated [Garman et al., 2002], which provided evidence that D313Y did not markedly disrupt the α‐Gal A enzyme structure. Thus, D313Y is a rare exonic variant with about 60% of wild‐type activity in vitro and reduced activity at neutral pH, resulting in low plasma α‐Gal A activity. Hum Mutat 22:486–492, 2003. © 2003 Wiley‐Liss, Inc. |
Author | Desnick, Robert J. Yasuda, Makiko Maire, Irene Burnett, Roger M. Benson, Stacy D. Shabbeer, Junaid |
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Snippet | Fabry disease, an X‐linked inborn error of glycosphingolipid catabolism, results from mutations in the gene encoding the lysosomal exoglycohydrolase,... Fabry disease, an X-linked inborn error of glycosphingolipid catabolism, results from mutations in the gene encoding the lysosomal exoglycohydrolase,... |
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SubjectTerms | Alleles alpha-Galactosidase - chemistry alpha-Galactosidase - genetics alpha-Galactosidase - metabolism Amino Acid Substitution Animals Catalytic Domain Cercopithecus aethiops Chickens COS Cells DNA - chemistry DNA - genetics DNA Mutational Analysis Endoplasmic Reticulum - enzymology Enzyme Stability Fabry disease Fabry Disease - blood Fabry Disease - enzymology Fabry Disease - genetics GLA Humans Hydrogen-Ion Concentration lysosomal storage disease Lysosomes - enzymology Male Models, Molecular Mutation mutation analysis Plasmids - genetics Protein Structure, Secondary Protein Structure, Tertiary pseudodeficiency Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism structural homology model Transfection |
Title | Fabry disease: Characterization of α-galactosidase A double mutations and the D313Y plasma enzyme pseudodeficiency allele |
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