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  • 1
    Electronic Resource
    Electronic Resource
    Chemical modification of the plasma membrane polypeptides of cultured mammalian cells as an aid to studying protein turnover (1974)
    s.l. : American Chemical Society
    Biochemistry 13 (1974), S. 4846-4855 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00720a025
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  • 2
    Electronic Resource
    Electronic Resource
    Interferon-tau (1993)
    [s.l.] : Nature Publishing Group
    Nature 362 (1993), S. 583-583 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] SIR — lan Tizzard (Nature 361, 676; 1993) is not alone in his puzzlement over interferon nomenclature. However, he is incorrect in his assumption that interferon-tau (INF-t) had their origins as a typographical error, namely as the result of the inadvertent substitution of x for Y on a word ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/362583c0
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  • 3
    Electronic Resource
    Electronic Resource
    Finding the funding for agriculture (1998)
    [s.l.] : Macmillan Magazines Ltd.
    Nature 394 (1998), S. 517-517 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] SirI appreciate the timely appearance of the article and editorial on the support of US agricultural science (Nature 394, 207; 1998& Nature 394, 210; 211; 1998). They ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/28934
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  • 4
    Electronic Resource
    Electronic Resource
    Interferon-like sequence of ovine trophoblast protein secreted by embryonic trophectoderm (1987)
    [s.l.] : Nature Publishing Group
    Nature 330 (1987), S. 377-379 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Ovine trophoblast protein-1 (oTP-1) is the major secretory product synthesized by the sheep conceptus between days 13 and 21 of pregnancy3'6. The protein consists of 3-4 isoelectric variants (pi 5.5-5.8) of relative molecular mass (Mr) -18,000 (18K) (Fig. 1a). For cell-free translation ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/330377a0
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  • 5
    Electronic Resource
    Electronic Resource
    Uteroferrin contains complex and high mannose-type oligosaccharides when synthesized in vitro (1991)
    Springer
    Molecular and cellular biochemistry 105 (1991), S. 107-117 
    Details
    ISSN: 1573-4919
    Keywords: iron transport ; uteroferrin ; glycoprotein ; pregnancy ; swine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract Mature uteroferrin (Uf; MΓ = 35,500) is a progesterone-induced acid phosphatase secreted by the pig uterus. It contains a single, unphosphorylated, high mannose-type oligosaccharide. Endometrial explants cultured in vitro secrete Uf with a MΓ of 37,000 (37k Uf) having phosphorylated high mannose oligosaccharides. In this report we demonstrate that 37k Uf contains two N-linked oligosaccharides which are a mixture of complex and high mannose-type oligosaccharides. The complex-type glycopeptides are biantennary and a portion may be fucosylated on the GlcNac of the chitobiose core proximal to the peptide. Only a portion of the high mannose-type oligosaccharides are phosphorylated. The remainder appear to be typical Man6-4GlcNac2 oligosaccharides found on mature Uf.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00227750
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  • 6
    Electronic Resource
    Electronic Resource
    Possible function of carbohydrate on glycoproteins secreted by the pig uterus during pregnancy (1986)
    Springer
    Molecular and cellular biochemistry 72 (1986), S. 67-79 
    Details
    ISSN: 1573-4919
    Keywords: glycoprotein ; oligosaccharide ; uteroferrin ; placenta ; pregnancy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract Uteroferrin is a purple iron-containing acid phosphatase secreted by the porcine uterus under the influence of the hormone, progesterone. It is synthesized by the glandular epithelial cells of the uterine endometrium and during pregnancy is taken up by specialized structures (areolae) opposite each uterine gland. Uteroferrin is then released into the fetal circulation and cleared by the liver or fetal kidney. A major role in iron transport to the fetus has been proposed. Uteroferrin, as purified from uterine secretions of pigs, possesses mainly high mannose (predominately Man5 and Man6 chains. These oligosaccharide chains of uteroferrin appear to be responsible for its binding and uptake by reticuloendothelial cells of the fetal liver which is the major site of erythropoiesis of the fetus. Uteroferrin, although implicated in transplantal iron transport, also possesses many of the properties of a lysosomal enzyme and, when newly synthesized, carries the so-called lysosomal recognition marker, mannose 6-phosphate. The phosphate group is masked by a covering N-acetylglucosamine residue, a feature which may account for its secretion rather than retention within lysosomes. Evidence is also presented that the oligosaccharide chains of newly synthesized uteroferrin are larger than those of the mature form and are trimmed after secretion. The phosphate group is also removed. It is not clear whether uteroferrin carbohydrate is implicated in the movement of the glycoprotein across the placenta as well as its uptake by the fetal liver.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00230636
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  • 7
    Electronic Resource
    Electronic Resource
    Expression of interleukin-6 in porcine, ovine, and bovine preimplantation conceptuses (1992)
    New York, NY [u.a.] : Wiley-Blackwell
    Molecular Reproduction and Development 32 (1992), S. 324-330 
    Details
    ISSN: 1040-452X
    Keywords: Embryo ; Implantation ; Interferon ; Interleukin-6 ; Pig ; Reverse transcription-polymerase chain reaction ; Trophoblast ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A porcine interleukin-6 (pIL6) cDNA has been cloned from pig spleen cDNA library to provide information that would allow us to study IL-6 mRNA expression during pregnancy of several domestic Artiodactyla. The cDNA is 1058 bp long and with a single open reading frame that encodes a 212 amino acid polypeptide with 28-residue signal sequence. It shares 61% and 43% amino acid sequence identity with human and mouse IL-6, respectively. PCR procedures with primers designed from regions of sequence conserved between human and pig have been used to identify IL-6 cDNA in λgt11 libraries constructed from day 15-16 (sheep), day 17 (cattle), and day 13-17 (pig) conceptus mRNA. The presence of IL-6 mRNA in elongating preimplantation ovine (days 13-25), porcine (days 13-21), and bovine (days 16-20) conceptuses was also demonstrated by PCR after reverse transcription of total ribonucleic acid with reverse transcriptase and by solution hybridization with a pIL-6 cRNA probe. These observations suggest that IL-6 is a product of these early conceptuses and may be involved in early maternal responses to the presence of an embryo within the uterus.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mrd.1080320404
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  • 8
    Electronic Resource
    Electronic Resource
    Expression of bovine trophoblast interferons by in vitro-derived blastocysts is correlated with their morphological quality and stage of development (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Molecular Reproduction and Development 36 (1993), S. 1-6 
    Details
    ISSN: 1040-452X
    Keywords: Blastocyst ; Embryo ; Embryonic development ; In vitro fertilization ; Trophectoderm ; Trophoblast interferon ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Bovine embryos, whether produced naturally or by in vitro techniques, exhibit considerable variability in morphological quality and develop at different rates. Our objectives have been to determine whether initial expression of trophoblast interferon (IFN-τ) was a reflection of conceptus stage of development or age and whether there was an effect of embryo quality on the amount of IFN-τ produced. Early blastocysts (N =187) were selected at the onset of blastocoele formation and cultured individually. Embryo quality (excellent, good, or fair: E, G, or F) and developmental stage (early, expanded and hatched blastocysts: BL, EBL, and HBL, respectively) were used in a 3 x 3 factorial complete randomized block design, each block (n = 4) consisting of batches of embryos produced from oocytes in different collections. Quality and developmental stage of embryos and IFN-τ released into the medium were assessed every 24 h. Production of IFN-τ (units/embryo/24 h) was greater (P 〈 0.01) among hatched blastocysts (HBL; 0.91 ± 0.08) than expanded blastocysts (EBL; 0.23 ± 0.04) and early blastocysts (BL; 0.05 ± 0.08). Embryos of similar developmental stage but differing by 2 days in age released equal amounts of IFN-τ. Expression of antiviral activity increased (P 〈 0.05) from 27% to 57% to 100% as development proceeded from BL to EBL and to HBL respectively. More IFN-τ was produced by HBL graded G (1.0 ± 0.1) or E (1.3 ± 0.1) than by those of F quality (0.5 ± 0.1). All blastocysts, whatever their quality and developmental stage, contained IFN-± mRNA. Therefore, developmental stage and quality of the embryos significantly influence the expression of IFN-±. The amount produced may be a useful objective indicator of embryo quality. © 1993 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mrd.1080360102
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  • 9
    Electronic Resource
    Electronic Resource
    Endocytosis of wheat germ agglutinin binding sites from the cell surface into a tubular endosomal network (1990)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 143 (1990), S. 1-12 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: By using fluorescence and electron microscopy, the endocytic pathway encountered by cell surface components after they had bound wheat germ agglutinin (WGA) was visualized. The majority of these components are thought to consist of sialylated glycoproteins (HMWAG) that represent a subpopulation of the total cell surface proteins but most of the externally disposed plasma membrane proteins of the cell. Examination of semi-thin sections by medium- and high-voltage electron microscopy revealed the three-dimensional organization of vesicular and tubular endosomes. Binding of either fluorescein isothiocyanate-, horseradish peroxidase-, or ferritin-conjugated WGA to cells at 4°C showed that the HMWAG were distributed uniformly over the cell surface. Warming of surface-labeled cells to 37°C resulted in the endocytosis of WGA into peripheral endo-somes via invagination of regions of both coated and uncoated membrane. The peripheral endosome appeared as isolated complexes comprising a vesicular element (300-400 nm diam.) surrounded by and continuous with tubular cister-nae (45-60 nm diam.), which did not interconnect the endosomes. After 30 min or more label also became localized in a network of anastomosing tubules (45-60 nm diam.) that were located in the centrosomal region of the cell. Endocytosed WGA-HMWAG complexes did not become associated with cisternae of the Golgi apparatus, although tubular and vesicular endosomes were noted in the vicinity of the trans-Golgi region. The accumulation of WGA-HMWAG in the endosomes within the centrosomal region was inhibited when cells were incubated at 18°C. None of these compartments contained acid phosphatase activity, a result that is consistent with other data that the HMWAG do not pass through lysosomes initially. The kinetics of labeling were consistent with the interpretation that recycling of most of the WGA binding surface glycoproteins occurred rapidly from early peripheral endosomes followed by the late trans-Golgi compartment. In conclusion, a portion of cell surface glycoproteins are routed to a complex arrangement of tubular and vesicular compartments following endocytosis that includes a putative post-endosomal, tubular reticulum that appears to be separate from the trans-most Golgi saccule.
    Additional Material: 12 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041430102
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  • 10
    Electronic Resource
    Electronic Resource
    Rapid endocytosis and recycling of wheat germ agglutinin binding sites on CHO cells: Evidence for two compartments in a nondegradative pathway (1990)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 144 (1990), S. 52-61 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The internalization and recycling of CHO cell plasma membrane components have been quantified by using iodinated wheat germ agglutinin (WGA) as an adsorptive tracer. Most of these binding sites are thought to be composed of a subpopulation of plasma membrane proteins called high-molecular-weight acidic glycoproteins (HMWAG). Greater than 90% of the WGA bound on the cell surface can be removed by brief treatment with N-acetylglucosamine (GlcNAc). At 37°C, endocytosis of WGA that had been allowed to bind to the surface at 4°C is curvilinear with an initial rapid phase occurring with a t1/2 of 6-8 min. Within 20 min, accumulation has slowed gradually to steady-state with 65% of the cell-associated WGA located intracellularly or resistant to remova by GlcNAc. These portions are unaffected by increasing the extracellular concentration of WGA from 0.003 μM. By using pulse-chase experiments, the observed decrease in rate of endocytosis is shown to be due to return of the WGA-HMWAG complexes to the cell surface. More than 60% of the WGA that had been internalized is recycled within 30 min, with a mean t1/12 of 17 min. Recycling involved at least two intracellular populations where a significant fraction ( 〈 30%) of the WGA-HMWAG complexes are lost gradually from the rapidly recycling pool. Most of the WGA-HMWAG complexes that had internalized are not delivered to the lysosome. These results demonstrate the magnitude of rapid and continuous recycling of WGA binding sites between the cell surface and endosomes in fibroblasts.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041440108
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