{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T10:53:06Z","timestamp":1790679186677,"version":"4.1.0"},"reference-count":22,"publisher":"Oxford University Press (OUP)","issue":"4","license":[{"start":{"date-parts":[[2005,4,1]],"date-time":"2005-04-01T00:00:00Z","timestamp":1112313600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/open_access\/funder_policies\/chorus\/standard_publication_model"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2005,4,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>Background: Fabry disease is an X-linked lysosomal storage disorder resulting from a deficiency of the lysosomal hydrolase, \u03b1-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.<\/jats:p>\n               <jats:p>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.<\/jats:p>\n               <jats:p>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.<\/jats:p>\n               <jats:p>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.<\/jats:p>","DOI":"10.1373\/clinchem.2004.041418","type":"journal-article","created":{"date-parts":[[2005,2,3]],"date-time":"2005-02-03T20:24:35Z","timestamp":1107462275000},"page":"688-694","source":"Crossref","is-referenced-by-count":49,"title":["Urinary Lipid Profiling for the Identification of Fabry Hemizygotes and Heterozygotes"],"prefix":"10.1093","volume":"51","author":[{"given":"Maria","family":"Fuller","sequence":"first","affiliation":[{"name":"Lysosomal Diseases Research Unit and National Referral Laboratory,"},{"name":"Department of Paediatrics, University of Adelaide, Adelaide, South Australia, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Peter C","family":"Sharp","sequence":"first","affiliation":[{"name":"Department of Genetic Medicine, Women\u2019s and Children\u2019s Hospital, North Adelaide, South Australia, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tina","family":"Rozaklis","sequence":"first","affiliation":[{"name":"Lysosomal Diseases Research Unit and National Referral Laboratory,"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Phillip D","family":"Whitfield","sequence":"first","affiliation":[{"name":"Lysosomal Diseases Research Unit and National Referral Laboratory,"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David","family":"Blacklock","sequence":"first","affiliation":[{"name":"Lysosomal Diseases Research Unit and National Referral Laboratory,"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"John J","family":"Hopwood","sequence":"first","affiliation":[{"name":"Lysosomal Diseases Research Unit and National Referral Laboratory,"},{"name":"Department of Paediatrics, University of Adelaide, Adelaide, South Australia, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Peter J","family":"Meikle","sequence":"first","affiliation":[{"name":"Lysosomal Diseases Research Unit and National Referral Laboratory,"},{"name":"Department of Paediatrics, University of Adelaide, Adelaide, South Australia, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2005,4,1]]},"reference":[{"key":"2020022800555373400_R1","doi-asserted-by":"crossref","unstructured":"Brady RO, Gal AE, Bradley RM, Martensson E, Warshaw AL, Laster L. Enzymatic defect in Fabry\u2019s disease. Ceramide trihexosidase deficiency. N Engl J Med1967;276:1163-1167.","DOI":"10.1056\/NEJM196705252762101"},{"key":"2020022800555373400_R2","unstructured":"Desnick RJ, Ioannou YA, Eng CM. Fabry disease: \u03b1-galactosidase A deficiency. Scriver CR Beaudet AC Sly WS Valle D eds. The metabolic and molecular bases of inherited disease, 7th ed2001:3733-3774 McGraw-Hill New York. ."},{"key":"2020022800555373400_R3","doi-asserted-by":"crossref","unstructured":"von Scheidt W, Eng CM, Fitzmaurice TF, Erdmann E, Hubner G, Olsen EG, et al. An atypical variant of Fabry\u2019s disease with manifestations confined to the myocardium. N Engl J Med1991;324:395-399.","DOI":"10.1056\/NEJM199102073240607"},{"key":"2020022800555373400_R4","doi-asserted-by":"crossref","unstructured":"Nakao S, Kodama C, Takenaka T, Tanaka A, Yasumoto Y, Yoshida A, et al. 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