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Proc. Natl. Acad. Sci. USA
Vol. 94, pp. 10362-10366, September 1997
Medical Sciences

Search for the pathogenesis of the differing phenotype in two compound heterozygote Hungarian brothers with the same genotypic triosephosphate isomerase deficiency

Susan Hollán*,dagger , Mária Magócsi*, Elfrieda FodorDagger , Margit Horányi*, Veronika Harsányidagger , and Tibor FarkasDagger ,

* National Institute of Hematology and Immunology, and dagger  National Blood Transfusion Center, H-1113 Budapest, Hungary; and Dagger  Institute of Biochemistry, Biological Research Center, Hungarian Academy of Sciences, H-6701 Szeged, Hungary

Contributed by Tibor Farkas, July 2, 1997

In a Hungarian family with triosephosphate isomerase (TPI) deficiency, two compound heterozygote brothers were found with the same severe decrease in TPI activity, but only one of them had the classical symptoms. In search for the pathogenesis of the differing phenotype of the same genotypic TPI deficiency, an increase in red cell membrane fluidity was found. There were roughly 100% and 30% more 16:0/20:4 and 18:0/20:4 diacyl-phosphatidylcholine species in erythrocytes from the two TPI-deficient brothers than in the probes from healthy controls. The activities of acethylcholinesterase and calmodulin induced Ca2+ ATPase were significantly enhanced in erythrocytes from the propositus as compared with those of the neurologically symptom-free brother and other members of the TPI-deficient family as well as to those from healthy controls. Both enzymes are crucially involved in the function of nerve cells. The observed differences in membrane fluidity and enzyme activities between the erythrocytes from the phenotypically differing TPI-deficient brothers underline the importance of investigations into the effect of biophysical changes in the lipid environment of the membrane proteins on the development of disseminated focal neurological disorders of unknown pathogenic origin.


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