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

Lacey, Stephen W.; Sanders, John M.; Rothberg, Karen G.; Anderson, R. G.; Kamen, Barton A.

doi:10.1172/jci114220

Cited by 218 publications

(132 citation statements)

References 44 publications

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“…The similarity between the cDNA sequences in the open reading frame of pig liver FBP and the published sequence for human placenta FBP [3] was 80 %. Back-translation of the open reading frame revealed 67-73 % similarity of the deduced pig liver FBP sequence to previously published amino acid sequences [2,3,[6][7][8]20] (Figure 2). The deduced amino acid sequence revealed cross-species conservation of 16 cysteine sites, 11 tryp-…”

Section: Sequence Of Pig Liver Fbpsupporting

confidence: 58%

“…Folate-binding proteins (FBPs) have a high affinity for monoglutamyl folates [1] and have been identified in human placenta [2,3], rat [4] and pig kidney [5], bovine milk [6], and human cancer cell lines including KB [2,7] and Caco-2 cells [8]. The nucleotide and amino acid similarities of FBPs from placenta and several different mammalian cells lines [1][2][3]7,8] suggest that they may play a role in folate homeostasis through regulation of transport across intestinal, liver and kidney membranes.…”

Section: Introductionmentioning

confidence: 99%

“…The nucleotide and amino acid similarities of FBPs from placenta and several different mammalian cells lines [1][2][3]7,8] suggest that they may play a role in folate homeostasis through regulation of transport across intestinal, liver and kidney membranes. In this context, previous investigators demonstrated FBPs by gel filtration of rat and human liver plasma membranes [9,10], affinity chromatography of rat [4] and pig [5] renal tubular membranes and by autoradiography of affinity-labelled pig jejunal mucosal proteins separated by gel electrophoresis [11].…”

Section: Introductionmentioning

confidence: 99%

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Folate binding protein: molecular characterization and transcript distribution in pig liver, kidney and jejunum

Hoozen

Ling

Halsted

1996

Biochemical Journal

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Folate-binding protein (FBP) was identified and characterized in a pig liver cDNA library by screening with a 0.6 kb fragment from the cDNA of FBP from a human KB cell cancer line. The cDNA of pig liver FBP included 1230 bp containing 759 bp in the open reading frame with 80 % similarity to the human placenta FBP. The deduced 253 amino acid sequence showed 67-73 % similarity to previous sequences and contained 16 conserved cysteine residues, 11 tryptophan potential folate-

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Section: Sequence Of Pig Liver Fbpsupporting

confidence: 58%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Folate binding protein: molecular characterization and transcript distribution in pig liver, kidney and jejunum

Hoozen

Ling

Halsted

1996

Biochemical Journal

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“…5,6 Intrabodies are potentially suited for antiviral and antitumor gene therapy approaches, and preclinical and clinical studies have been promising. 7,8 One of the more specific tumor markers identified in our laboratory 9 is the a-isoform of the folate receptor (FR), a 38-40 kDa glycosyl-phosphatidyl-inositol-anchored molecule [10][11][12][13] that binds folic acid with high affinity. Detailed immunohistochemical analysis and evaluation of messenger RNA expression revealed moderate levels of FR expression on the cell surface of normal epithelial cells of kidney, lung and breast, and high levels in placental tissue.…”

Section: Introductionmentioning

confidence: 99%

Reversion of transformed phenotype in ovarian cancer cells by intracellular expression of anti folate receptor antibodies

et al. 2003

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The a-folate receptor (FR) is selectively overexpressed in 90% of nonmucinous ovarian carcinomas, whereas no expression is detectable in normal ovarian surface epithelium (OSE). Indirect evidence suggests that FR expression is associated with tumor progression and affects cell proliferation. To evaluate better the role of FR, we developed an approach based on intracellular expression of single-chain (sc) antibodies (intrabody) to downmodulate membrane expression of FR in ovary cancer cells. IGROV-1 and SKOV3 ovarian carcinoma cell lines were transfected with an anti-FR intrabody. Transfectants and parental cells were tested for FR, integrins and anti-FR intrabody expression by fluorescence-activated cell sorting (FACS), reverse transcription and polymerase chain reaction (RT-PCR) and/or immunoblotting. Cell growth characteristics and adhesion properties were evaluated in liquid, semisolid and organotypic cultures. The anti-FR scFv inhibited FR expression from 60 to 99%. At physiological concentrations of folate, proliferation varied directly as a function of FR expression. FR downmodulation was accompanied by reduced colonyforming ability in soft agar, morphological change of the cells, significant enhanced adhesion to laminin or Matrigel, a twoto three-fold increase in a6b4 integrin expression, and a marked reduction in laminin production. In three-dimensional organotypic cultures, anti-FR intrabody-transfected IGROV1 cells grew as a single-ordered layer, reminiscent of normal OSE growth in vivo. In conclusion, the anti-FR intrabody reverses the transformed phenotype in ovary cancer cells and may provide an efficient means to inhibit selectively the growth of these cells.

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“…FBP is anchored to the cell surface by glycosylphosphatidylinositol (GPI; Lacey et al, 1989) and binds folic acid and 5-methyltetrahydrofolate, a predominant folate metabolite in plasma, with a relatively high affinity (Antony, 1992). Folates bound to FBP are incorporated into cells by means of endocytosis (Kamen et al, 1988;Anderson et al, 1992).…”

Section: Introductionmentioning

confidence: 99%

Spatial and temporal expression of folate‐binding protein 1 (Fbp1) is closely associated with anterior neural tube closure in mice

Saitsu

Ishibashi

Nakano

et al. 2002

Developmental Dynamics

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Periconceptional folate supplementation is widely believed to have significant preventive effects on the production of neural tube defects. Folate-binding protein 1 (FBP1) is one of the membrane proteins that mediate cellular uptake of folate. Although recent studies suggest that Fbp1 is essential for neural tube closure, the pattern of Fbp1 expression in embryonic tissues has not been examined in detail. To elucidate how Fbp1 contributes to neural tube closure, we examined the spatial and temporal expression patterns of Fbp1 in the developing neural folds and tube of mouse embryos by in situ hybridization. Fbp1 showed a distinct expression pattern in the neural folds, which preceded initiation of neural tube closure at the cervical region and the prosencephalic/mesencephalic boundary.

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

Cited by 218 publications

References 44 publications

Folate binding protein: molecular characterization and transcript distribution in pig liver, kidney and jejunum

Folate binding protein: molecular characterization and transcript distribution in pig liver, kidney and jejunum

Reversion of transformed phenotype in ovarian cancer cells by intracellular expression of anti folate receptor antibodies

Spatial and temporal expression of folate‐binding protein 1 (Fbp1) is closely associated with anterior neural tube closure in mice

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