Sciatin Is a Transferrin‐Like Polypeptide

Markelonis, George J.; Bradshaw, Ralph A.; Oh, Tae Hwan; Johnson, Jeri L.; Bates, Owen J.

doi:10.1111/j.1471-4159.1982.tb03949.x

Cited by 61 publications

(19 citation statements)

References 41 publications

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“…Previous studies have demonstrated considerable biochemical and immunologic similarities among EETf, OTf, nerve-derived Tf, and CSTf (Hirai, 1981;Markelonis et al, 1982;Beach et al, 1983Beach et al, , 1985. The current studies confirm some of the previous observations and shed new light on the antigenic properties of these proteins.…”

Section: Discussionsupporting

confidence: 90%

“…Pertinent to this point is the developmentally regulated dependence of postmitotic neuroblasts on transferrin in culture (Aizenman et al, 1986). The peripheral counterpart of oligodendrocytes, the Schwann cell, may also be capable of Tf synthesis and may be the source of nerve-derived Tf in our studies (Popiela et al, 1983(Popiela et al, , 1984 and those of others (Markelonis et al, 1982;. Although sera certainly contain ample amounts of circulating Tf (Aisen and Listowsky, 1980) the postmitotic dependence of myotubes on Tf might have specificity requirements (Ozawa et al, 1983).…”

Section: Discussionmentioning

confidence: 82%

“…In only one case, however, has the evidence been strong enough and the factor, nerve growth factor (NGF),' purified. Several laboratories, including our own, have shown that extracts of adult nerve (Festoff and Oh, 1977;Ontell and Dunn, 1978;Ozawa and Hagiwara, 1981;Ozawa and Kohama, 1978;Ozawa et al, 1983;Beach et al, 1983Beach et al, , 1985, embryonic central or peripheral nervous system Levin et al, 1984;Markelonis, 1982), or serum of adult chickens (Ozawa and Hagiwara, 1981;Ii et al, 1977;Oh et al, 1986) contained a factor that was capable of replacing embryo extract in myogenic development in tissue culture. This substance was given several names: MTF (Ozawa and Hagiwara, 1981), sciatin (Markelonis et al, 1982), SNP (Festoff and Oh, 1977;, and NTF (Popiela and Ellis, 1981).…”

Section: Introductionmentioning

confidence: 95%

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Monoclonal antibody detects embryonic epitope specific for nerve‐derived transferrin

Festoff

Muñoz

Patel

et al. 1989

J of Neuroscience Research

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Monoclonal antibodies were generated against transferrin purified from chick embryo extract by fusing spleen cells from BALB/c mice immunized against embryonic transferrin, with myeloma cells. Antibodies produced by the selected hybridoma clones were all type IgG. Twelve clones were selected for secretion of antibodies to the embryo extract-derived transferrin, and three clones were studied extensively. Immunoblotting was used to demonstrate antibody binding to several avian transferrin proteins derived from adult chicken serum, adult chicken peripheral nerves, and ovotransferrin. Screening and detailed epitope analysis were accomplished by solid-phase immunoassay. The results indicated that two clones, 2G9.1 and 2B11.1, recognized the embryonic and egg antigens in preference to the adult proteins. However, a third clone, 6H2.1, recognized the nerve-derived transferrin preferentially to both the embryonic and adult serum antigens. None of the clones recognized the serum-derived transferrin in preference to the other antigens. These results indicate that embryonic epitope(s) are conserved in the nerve- but not the serum-derived transferrin. They also show that the neural antigen has site(s) distinct from the embryonic proteins. No changes in displacement curves were observed after these proteins were digested with neuraminidase, indicating that the epitope differences discovered are not intimately related to sialic acid residues on the various transferrins.

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Section: Discussionsupporting

confidence: 90%

Section: Discussionmentioning

confidence: 82%

Section: Introductionmentioning

confidence: 95%

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Monoclonal antibody detects embryonic epitope specific for nerve‐derived transferrin

Festoff

Muñoz

Patel

et al. 1989

J of Neuroscience Research

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“…The beads were washed twice in PBS. To load iron onto the apotransferrin, the beads were resuspended in 50 mM Tris-HCl, pH 8.0, 10 mM NaHCO 3 , 1 mM ferric citrate (Markelonis et al, 1982); incubated for 3 h at room temperature; and then overnight at 4°C with rotation. Beads were washed twice in PBS and resuspended in PBS to a final concentration of ϳ2 ϫ 10 6 beads/l.…”

Section: Bead Experimentsmentioning

confidence: 99%

Repeated Cycles of Rapid Actin Assembly and Disassembly on Epithelial Cell Phagosomes

Yam

Theriot

2004

MBoC

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We have found that early in infection of the intracellular pathogen Listeria monocytogenes in Madin-Darby canine kidney epithelial cells expressing actin conjugated to green fluorescent protein, F-actin rapidly assembles (ϳ25 s) and disassembles (ϳ30 s) around the bacteria, a phenomenon we call flashing. L. monocytogenes strains unable to perform actin-based motility or unable to escape the phagosome were capable of flashing, suggesting that the actin assembly occurs on the phagosome membrane. Cycles of actin assembly and disassembly could occur repeatedly on the same phagosome. Indirect immunofluorescence showed that most bacteria were fully internalized when flashing occurred, suggesting that actin flashing does not represent phagocytosis. Escherichia coli expressing invA, a gene product from Yersinia pseudotuberculosis that mediates cellular invasion, also induced flashing. Furthermore, polystyrene beads coated with E-cadherin or transferrin also induced flashing after internalization. This suggests that flashing occurs downstream of several distinct molecular entry mechanisms and may be a general consequence of internalization of large objects by epithelial cells. INTRODUCTIONBacterial pathogens such as Salmonella, Yersinia, and Listeria have a variety of mechanisms that allow them to enter and survive in eukaryotic cells. Their ability to survive intracellularly can protect them from host defenses and allow them to cross epithelial barriers. To enter eukaryotic cells, these invasive bacteria actively induce their own uptake by phagocytosis in normally nonphagocytic cells. Internalized bacteria either survive within the phagosome, encapsulated by the host cell membrane, or they escape from the phagosome and disseminate throughout the cytoplasm and to neighboring cells (reviewed in Cossart and Sansonetti, 2004). Modulation of the host cell actin cytoskeleton by invasive bacteria allows them to control many of these steps, including attachment and entry into cells, survival in the phagosome, and movement in the cytoplasm.One bacterium with an intracellular niche is Listeria monocytogenes, a food-borne pathogen responsible for meningitis, meningoencephalitis, septicemia, gastroenteritis, and abortions (reviewed in Cossart and Lecuit, 1998). Two L. monocytogenes proteins, internalin (InlA) and internalin B (InlB), can interact with the host cell surface proteins E-cadherin, gC1q-R, and Met to induce bacterial uptake into nonphagocytic cells (Mengaud et al., 1996;Braun et al., 2000;Shen et al., 2000). Uptake of bacteria is driven by actin polymerization and membrane extension (reviewed in Cossart and Sansonetti, 2004). Once inside the cell, L. monocytogenes escapes from the phagosome into the cytoplasm. In the cytoplasm, L. monocytogenes nucleates actin filaments that assemble into actin clouds around the bacteria and then into polarized comet tails. The actin comet tails propel the movement of L. monocytogenes within the cytoplasm of an infected cell and into neighboring cells (Tilney and Portnoy, 1989;Mounier e...

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“…HoloTf is required for proliferation of nearly all normal and transformed cells in defined, serum-free medium [Barnes and Sato, 1980], and is important primarily for progression through the cell cycle [Pardee et al, 1981]. According to several investigators [Markelonis et al, 1982;Meek and Adamson, 1985], peripheral nerves are particularly rich in holoTf. HoloTf is present in neurons and SCs of sciatic nerves and becomes concentrated over 20-fold in the nerve during limb regeneration.…”

Section: Introductionmentioning

confidence: 99%

HoloTransferrin but Not ApoTransferrin Prevents Schwann Cell De-Differentiation in Culture

et al. 2002

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Schwann cells (SCs) in culture, without the presence of axons, become de-differentiated, reaching a condition similar to that of their precursor cells. The cytoplasmic accumulation of transferrin (Tf) in the myelinated peripheral nerve has been reported and data in the literature support a role for apoTf in myelination in the CNS. In the present report, we used SC cultures to evaluate the capacity of apoTf and holoTf to prevent cell de-differentiation promoted by fetal calf serum deprivation. SCs incubated in a serum-free medium showed a decrease in the expression of myelin basic protein (MBP) and P₀, markers of mature myelin-forming SCs, together with an increase in the levels of p75NTR and glial fibrillary acidic protein, markers of immature SCs. Treatment with holoTf prevented the decrease in expression of MBP and P₀ and the increase in p75NTR. ApoTf was unable to prevent these changes except when iron was added to the cultures. These results suggest a role for holoTf in the regulation of myelin formation by SCs.

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Sciatin Is a Transferrin‐Like Polypeptide

Cited by 61 publications

References 41 publications

Monoclonal antibody detects embryonic epitope specific for nerve‐derived transferrin

Monoclonal antibody detects embryonic epitope specific for nerve‐derived transferrin

Repeated Cycles of Rapid Actin Assembly and Disassembly on Epithelial Cell Phagosomes

HoloTransferrin but Not ApoTransferrin Prevents Schwann Cell De-Differentiation in Culture

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