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Research Article Free access | 10.1172/JCI114591
Second Department of Internal Medicine, Kumamoto University Medical School, Japan.
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Second Department of Internal Medicine, Kumamoto University Medical School, Japan.
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Second Department of Internal Medicine, Kumamoto University Medical School, Japan.
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Second Department of Internal Medicine, Kumamoto University Medical School, Japan.
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Second Department of Internal Medicine, Kumamoto University Medical School, Japan.
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Second Department of Internal Medicine, Kumamoto University Medical School, Japan.
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Second Department of Internal Medicine, Kumamoto University Medical School, Japan.
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Second Department of Internal Medicine, Kumamoto University Medical School, Japan.
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Second Department of Internal Medicine, Kumamoto University Medical School, Japan.
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Second Department of Internal Medicine, Kumamoto University Medical School, Japan.
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Published May 1, 1990 - More info
In paroxysmal nocturnal hemoglobinuria (PNH), impaired glycosyl-phosphatidylinositol (PI)-anchoring of membrane proteins such as decay-accelerating factor has been known to lead to increased susceptibility to complement. Moreover, abnormal expression of non-PI-anchoring glycoproteins such as C3b/C4b receptor (CR1) or glycophorin-alpha also has been shown in PNH. Therefore, we biochemically analyzed glycosphingolipids (GSL) as one of the membrane glycoconjugates of PNH erythrocytes. Erythrocytes of all seven PNH patients showed altered expression of sialosyl GSL (gangliosides) as compared with the control erythrocytes of healthy donors. Both a sialosylparagloboside (IV6NeuAc-nLc4Cer) among four major gangliosides and some minor gangliosides in normal erythrocytes variably disappeared in erythrocytes from the peripheral blood of PNH patients. As one of the possible mechanisms of altered expression of gangliosides in PNH erythrocytes, structural analysis suggested impaired sialylation of GSL. These results suggest not only the altered metabolism of gangliosides in PNH erythrocytes, but also a metabolic disorder of membrane glycoconjugates as a new feature of PNH.
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