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Research Article Free access | 10.1172/JCI114220

Complementary DNA for the folate binding protein correctly predicts anchoring to the membrane by glycosyl-phosphatidylinositol.

S W Lacey, J M Sanders, K G Rothberg, R G Anderson, and B A Kamen

Department of Internal Medicine, University of Texas Southwestern Medical Center, Dallas 75235.

Find articles by Lacey, S. in: PubMed | Google Scholar

Department of Internal Medicine, University of Texas Southwestern Medical Center, Dallas 75235.

Find articles by Sanders, J. in: PubMed | Google Scholar

Department of Internal Medicine, University of Texas Southwestern Medical Center, Dallas 75235.

Find articles by Rothberg, K. in: PubMed | Google Scholar

Department of Internal Medicine, University of Texas Southwestern Medical Center, Dallas 75235.

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

Department of Internal Medicine, University of Texas Southwestern Medical Center, Dallas 75235.

Find articles by Kamen, B. in: PubMed | Google Scholar

Published August 1, 1989 - More info

Published in Volume 84, Issue 2 on August 1, 1989
J Clin Invest. 1989;84(2):715–720. https://doi.org/10.1172/JCI114220.
© 1989 The American Society for Clinical Investigation
Published August 1, 1989 - Version history
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Abstract

Membrane bound and soluble forms of a high-affinity folate binding protein have been found in kidney, placenta, serum, milk, and in several cell lines. The two forms have similar binding characteristics for folates, are immunologically cross-reactive and based upon limited amino acid sequence data, are nearly identical. Based upon pulse-chase experiments, a precursor-product relationship has been suggested. The membrane form has been shown to mediate the transport of folate in cells grown in physiological concentrations of folate. A function for the soluble form has not yet been identified. We constructed a cDNA library from a human carcinoma cell line, Caco-2, which expresses the membrane form abundantly. The library was screened and a near full-length cDNA for the folate binder was isolated. Transfection of COS cells with the cDNA inserted in an expression vector resulted in marked overexpression of a membrane-associated folate binder as assessed by direct binding of radiolabeled folate and by indirect immunofluorescence. The deduced amino acid sequence is not consistent with a typical membrane spanning domain but rather with a signal for anchoring via a glycosyl-phosphatidylinositol linkage. Release of the binder with a phosphatidylinositol-specific phospholipase C strongly supports this hypothesis.

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