Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/17344
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Type: Journal article
Title: Urinary lipid profiling for the identification of Fabry hemizygotes and heterozygotes
Author: Fuller, M.
Sharp, P.
Rozaklis, T.
Whitfield, P.
Blacklock, D.
Hopwood, J.
Meikle, P.
Citation: Clinical Chemistry, 2005; 51(4):688-694
Publisher: Amer Assoc Clinical Chemistry
Issue Date: 2005
ISSN: 0009-9147
1530-8561
Statement of
Responsibility: 
Maria Fuller, Peter C. Sharp, Tina Rozaklis, Phillip D. Whitfield, David Blacklock, John J. Hopwood, and Peter J. Meikle
Abstract: BACKGROUND:Fabry disease is an X-linked lysosomal storage disorder resulting from a deficiency of the lysosomal hydrolase, alpha-galactosidase, for which enzyme replacement therapy is now available. In this study, we aimed to identify Fabry heterozygotes not only for genetic counseling of families but because it is becoming increasingly obvious that many heterozygous (carrier) females are symptomatic and should be considered for treatment. METHODS:We measured 29 individual lipid species, including ceramide, glucosylceramide, lactosylceramide, and ceramide trihexoside, in urine samples from Fabry hemizygotes and heterozygotes and from control individuals by electrospray ionization tandem mass spectrometry. Individual analyte species and analyte ratios were analyzed for their ability to differentiate the control and patient groups. RESULTS:The Fabry hemizygotes had increased concentrations of the substrate for the deficient enzyme, ceramide trihexoside, as well as lactosylceramide and ceramide, along with decreased concentrations of both glucosylceramide and sphingomyelin. Ratios of these analytes improved differentiation between the control and Fabry groups, with the Fabry heterozygotes generally falling between the Fabry hemizygotes and the control group. CONCLUSIONS:These lipid profiles hold particular promise for the identification of Fabry individuals, may aid in the prediction of phenotype, and are potentially useful for the monitoring of therapy in patients receiving enzyme replacement.
Keywords: Humans; Fabry Disease; Lipids; Spectrometry, Mass, Electrospray Ionization; Reproducibility of Results; Heterozygote; Homozygote
Rights: © 2005 The American Association for Clinical Chemistry
RMID: 0020050248
DOI: 10.1373/clinchem.2004.041418
Appears in Collections:Paediatrics publications

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