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Research Article Free access | 10.1172/JCI116393

Hereditary tyrosinemia type I. Self-induced correction of the fumarylacetoacetase defect.

E A Kvittingen, H Rootwelt, P Brandtzaeg, A Bergan, and R Berger

Institute of Clinical Biochemistry, University of Oslo, Rikshospitalet Oslo, Norway.

Find articles by Kvittingen, E. in: PubMed | Google Scholar

Institute of Clinical Biochemistry, University of Oslo, Rikshospitalet Oslo, Norway.

Find articles by Rootwelt, H. in: PubMed | Google Scholar

Institute of Clinical Biochemistry, University of Oslo, Rikshospitalet Oslo, Norway.

Find articles by Brandtzaeg, P. in: PubMed | Google Scholar

Institute of Clinical Biochemistry, University of Oslo, Rikshospitalet Oslo, Norway.

Find articles by Bergan, A. in: PubMed | Google Scholar

Institute of Clinical Biochemistry, University of Oslo, Rikshospitalet Oslo, Norway.

Find articles by Berger, R. in: PubMed | Google Scholar

Published April 1, 1993 - More info

Published in Volume 91, Issue 4 on April 1, 1993
J Clin Invest. 1993;91(4):1816–1821. https://doi.org/10.1172/JCI116393.
© 1993 The American Society for Clinical Investigation
Published April 1, 1993 - Version history
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Abstract

Two Norwegian patients with chronic tyrosinemia type I showed > 50% residual fumarylacetoacetase activity in liver samples obtained during liver transplantation. The enzyme characteristics of both patients were comparable with those of a normal control. Immunohistochemistry on liver sections from these patients and from three other Norwegian tyrosinemia patients revealed a mosaicism of fumarylacetoacetase immunoreactivity corresponding completely or partly to some of the regenerating nodules. This appearance of enzyme protein is presumably induced by the disease process. The mechanism involved remains unclear and could be caused by a genetic alteration, regained translation of messenger RNA, or to enhanced stability of an abnormal enzyme.

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