Localization of p43 placental isoferritin in human maternal-fetal tissue interface

Maymon, Ron; Jauniaux, Eric; Greenwold, Natalie; Moroz, Chaya

doi:10.1067/mob.2000.104145

Cited by 20 publications

(17 citation statements)

References 17 publications

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“…It is noteworthy that in the current study PLIF expression was exhibited by immunohistochemical staining in syncytiotrophoblast cells of human placenta (8 weeks of gestation). This is compatible with the previous report on the expression of PLF (11).…”

Section: Discussionsupporting

confidence: 83%

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PLIF, a Novel Human Ferritin Subunit from Placenta with Immunosuppressive Activity

Moroz

Traub

Maymon

et al. 2002

Journal of Biological Chemistry

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Ferritin is a ubiquitous iron storage protein existing in multiple isoforms composed of 24 heavy and light chain subunits. We describe here a third ferritin-related subunit cloned from human placenta cDNA library and named PLIF (placental immunomodulatory ferritin). The PLIF coding region is composed of ferritin heavy chain (FTH) sequence lacking the 65 C-terminal amino acids, which are substituted with a novel 48 amino acid domain (C48). In contrast to FTH, PLIF mRNA does not include the iron response element in the 5-untranslated region, suggesting that PLIF synthesis is not regulated by iron. The linkage between the FTH and C48 domains created a restriction site for EcoRI. PLIF protein was found to localize in syncytiotrophoblasts of placentas (8 weeks of gestation) at the fetal-maternal interface. Increased levels of PLIF transcript and protein were also detected in the breast carcinoma cell lines T47D and MCF-7 but not in the benign corresponding cell line HBL-100. In vitro, PLIF was shown to down-modulate mixed lymphocyte reactions and to inhibit the proliferation of peripheral blood mononuclear cells stimulated with OKT3. The accumulated data indicate that PLIF is an embryonic immune factor involved in down-modulating the maternal immune recognition of the embryo toward anergy. This mechanism may have been adapted by breast cancer cells over expressing PLIF.

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Section: Discussionsupporting

confidence: 83%

“…However, it was also shown that PLF is down-regulated in those cells at 17 weeks of gestation up to term (11). This may explain the current observation of the proportionally low PLIF mRNA transcripts exhibited in the tissue mRNA blot, as it was obtained from term placenta.…”

Section: Discussionsupporting

confidence: 37%

PLIF, a Novel Human Ferritin Subunit from Placenta with Immunosuppressive Activity

Moroz

Traub

Maymon

et al. 2002

Journal of Biological Chemistry

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“…179 New forms of ferritin may be involved in certain situations: Moroz and coworkers have described a novel isoform of ferritin that is elevated in the serum of patients with neoplastic breast disease as well as during pregnancy and HIV infection. [180][181][182] Molecular explanations for the perturbations of ferritin in cancer have been slow to advance, with often conflicting conclusions. For example, Modjtahedi et al 183 studied subclones of an SW 613-W human colon carcinoma cell line that differ in their ability to develop tumors in nude mice.…”

Section: Oncogenes Cancer and Ferritinmentioning

confidence: 99%

Regulation of ferritin genes and protein

Torti

2002

Blood

986

819

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“…59 There is also evidence for a placental-specific ferritin heavy chain homolog with immunosuppressive activity. 60 Immunohistochemical studies of ferritin expression in syncytiotrophoblasts are conflicting, with the majority of reports showing a lack of expression, 25,[61][62][63] while others demonstrate some staining. 64,65 (Table 1) This discrepancy may be due to the use of antibodies that react differentially with each isoferritin.…”

Section: Figurementioning

confidence: 99%

“…In contrast to the syncytiotrophoblast, fetal villous stromal cells consistently show pronounced ferritin staining. 25,61,62,64,65 This raises the possibility that villous stroma may serve as a buffer between the syncytiotrophoblast and fetal circulation to ensure adequate, but not excessive, iron supply. Whether synthesis and degradation of ferritin in the stromal cells respond to fetal iron demand is unknown.…”

Section: Figurementioning

confidence: 99%