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Science 9 December 1988:
Vol. 242. no. 4884, pp. 1446 - 1448
DOI: 10.1126/science.2904699

Articles

Science, Vol 242, Issue 4884, 1446-1448
Copyright © 1988 by American Association for the Advancement of Science


articles

Metabolic correction of defects in the lipid anchoring of Thy-1 in lymphoma mutants

D Gupta, A Tartakoff, and E Tisdale

Department of Pathology, Case Western Reserve University, Cleveland, OH 44106.

Many plasma membrane proteins, including Thy-1, are anchored by a carboxyl terminal glycophospholipid. This unit is absent from the Thy-1 of several lymphoma mutants that synthesize the Thy-1 polypeptide but fail to express it at the cell surface. Recessive mutants of complementation groups A to C, E, and F contain Thy-1 mRNA of normal size, which suggests that their Thy-1 polypeptide is normal. To identify possible metabolic lesions, each mutant was grown with various supplements. The class F and B mutants exhibited a reversible induction of surface lipid anchored Thy-1 when grown with the aminoglycoside G418. Other aminoglycosides, sugars, and ethanolamine were inactive. These unexpected observations are discussed in the context of lipid anchor biosynthesis.


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Phosphatidylinositol Phospholipase C Is Activated Allosterically by the Aminoglycoside G418. 2-DEOXY-2-FLUORO-SCYLLO-INOSITOL-1-O-DODECYLPHOSPHONATE AND ITS ANALOGS INHIBIT GLYCOSYLPHOSPHATIDYLINOSITOL PHOSPHOLIPASE C.
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