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  • Cell & Developmental Biology  (2,761)
  • Inorganic Chemistry  (1,709)
  • Computational Chemistry and Molecular Modeling  (433)
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  • 1
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    American Journal of Anatomy 195 (1992), S. 276-289 
    ISSN: 0002-9106
    Keywords: TGF-β-4 ; Expression ; Development ; Chicken ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Expression of TGF-β4 mRNA and protein was studied in the developing chicken embryo using specific cDNA probes and antibodies for chicken TGF-β4. Expression of TGF-β4 mRNA was detected by day 4 of incubation (Hamburger and Hamilton stage 22, E4) by RNA Northern blot analysis and increased with developmental age until day 12 of incubation (stage 38, E12) where it was detected in every embryonic tissue examined, with expression being highest in smooth muscle and lowest in the kidney. The steady-state level of expression of TGF-β4 mRNA remained relatively constant in most embryonic tissues through day 19 (stage 45, E19). In situ hybridization analysis detected TGF-β4 mRNA as early as the “definitive primitive streak” stage (stage 4); during neurulation (stage 10), TGF-β4 mRNA was detected in all three germ layers, including neuroectoderm. Following neurulation, TGF-β4 mRNA was detected in the neural tube, notochord, ectoderm, endoderm, sclerotome, and myotome, but not dermotome at stage 16. By day 6 of incubation (stage 29, E6), TGF-β4 mRNA was localized in several tissues including heart, lung, and gizzard. Immunohistochemical staining analysis also showed expression of TGF-β4 protein in all three germ layers as early as stage 4 in various cell types in qualitatively similar locations as TGF-β4 mRNA. These results suggest that TGF-β4 may play an important role in the development of many tissues in the chicken. © 1993 Wiley Liss, Inc.
    Additional Material: 9 Ill.
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  • 2
    ISSN: 0003-276X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 117 (1983), S. 333-341 
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: A new, gentle technique has been developed for washing of the retinal interphotoreceptor space (IPS) to obtain soluble components of the extracellular matrix (ECM). Using this method, we have determined that the major soluble coustituent of monkey IPS is a 146,000 Mr glycoprotein, which binds [3H]retinol, sediments on sucrose gradients at 7S and has an Rf of 0.42 on native gel electrophoresis. Using size-exclusion high performance liquid chromatography, the apparent molecular weight of the native protein was calculated to be 250,000 daltons. In contrast to previous studies, no 15,000-dalton cellular retinol-binding protein (CRBP) or 33,000-dalton cellular retinaldehydebinding protein (CRALBP) was observed in the IPS wash, indicating that these proteins are probably not involved in retinol transport between retina and pigment epithelium (PE). In the supernatant fraction of retinal homogenates that contains soluble intracellular proteins as well as extracellular constituents, the 146,000 Mr protein was closely associated with a 93,000 Mr protein that could be separated on SDS-gel electrophoresis; the 93,000 Mr protein was not found in the IPS wash. The 146,000 Mr interphotoreceptor retinol-binding protein (IRBP) may function in extracellular retinol transport in the IPS.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The isolation and characterization of a mutant murine T-cell lymphoma (S49) with altered purine metabolism is described. This mutant, AU-100, was isolated from a mutagenized populatio of S49 cells by virtue of its resistance to 0.1 mM 6-azauridine in semisolid agarose. The AU-100 cells are resistant to adenosine mediated cytotoxicity but are extraordinarily sensitive to killing by guanosine.High performance liquid chromatography of AU-100 cells extracts has demonstrated that intracellular levels of GTP, IMP, and GMP are all elevated about 3-fold over those levels found in wild type cells. The AU-100 cells also contain an elevated intracellular level of pyrophosphoribosylphosphate (PPriboseP), which as in wild type cells is diminished by incubation of AU-100 cells with adenosine. However AU-100 cells synthesize purines de novo at a rate less than 35% of that found in wild type cells.In other growth rate experiments, the AU-100 cell line was shown to be resistant to 6-thioguanine and 6-mercaptopurine. Levels of hypoxanthine-guanine phosphoribosyltransferase (HGPRTase) measured in AU-100 cell extracts, however, are 50-66% greater than those levels of HGPRTase found in wild type cell extracts. Nevertheless this mutant S49 cell line cannot efficiently incorporate labeled hypoxanthine into nucleotides since the salvage enzyme HGPRTase is inhibited in vivo.The AU-100 cell line was found to be 80% deficient in adenylosuccinate synthetase, but these cells are not auxotrophic for adenosine or other purines. The significant alterations in the control of purine de novo and salvage metabolism caused by the defect in adenylosuccinate synthetase are mediated by the resulting increased levels of guanosine necleotides.
    Additional Material: 6 Ill.
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  • 5
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 98 (1979), S. 527-537 
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The glycosaminoglycans (GAG) of human cultured normal glial and malignant glioma cell lines were studied using 35S-sulphate or 3H-glucosamine as markers. 35S-labelled GAG were assayed by precipitation with cetylpyridinium chloride; 3H-labelled sulphated GAG and 3H-labelled hyaluronic acid were quantitated after separation on a DEAE-cellulose column. The net production of GAG and the distribution, composition and turnover of GAG were similar in all of the normal cell lines tested, but showed a great variability in the malignant cell lines. Most of the glioma cell lines produced more hyaluronic acid and less sulphated GAG than the normal cell lines, but exceptions were noted. The GAG of the trypsin susceptible (pericellular) pool of normal glial cells consisted mainly of heparan sulphate with only minor amounts of other GAG. The analogous material of most glioma cells showed hyaluronic acid as the major GAG. Material liberated by trypsin from EDTA-detached cells (membrane fraction) was enriched in heparan sulphate as compared to the entire pericellular pool. Substrate attached material (SAM) left with the plastic dish after EDTA treatment of normal cultures was rich in heparan sulphate, whereas SAM of glioma cells lacked heparan sulphate or showed greatly reduced amounts of this component. Release of newly synthesized GAG to the extracellular medium was a rapid process in the normal cells but was more or less delayed in the glioma cells. The extracellular medium of the malignant glioma cultures was consistently poor in dermatan sulphate, as compared to that of normal cultures.
    Additional Material: 1 Ill.
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  • 6
    ISSN: 0095-9898
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 0095-9898
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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  • 8
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Infection of confluent human umbilical vein endothelial cells by the parasite Trypanosoma cruzi results in the appearance of an altered heparan sulfate proteoglycan (HSPG) isolated from the extracellular matrix of infected endothelial cells (ECMi). HSPG from ECMi differed from HSPG obtained from the extracellular matrix of uninfected endothelial cells (ECMu) by virtue of an 8-10-fold increase in sulfation and a different elution pattern using DEAE Sepharose chromatography. Analysis of the HSPG that binds to acidic fibroblast growth factor (aFGF) revealed that infection increased the proportion of HSPG that binds to aFGF by 35%. Heparitinase and alkaline borohydride treatment of aFGF-binding HSPG and chromatographic resolution on Sepharose CL4B column revealed an infection-associated 10-fold increase in sulfation of the GAG side chain with no significant change in the migration of the core protein. In addition, the aFGF binding HSPG isolated from ECMi demonstrated a markedly attenuated synergistic mitogenic activity with aFGF in a cell proliferation assay. All of the infection associated changes in HSPG could be demonstrated in HSPG obtained from uninfected endothelial cell cultures grown on ECMi. Hence, the ECMi is associated with signals capable of modulating the ECM associated metabolism of uninfected endothelial cells. This facility of ECMi was also shown to extend to patterns of Gs protein synthesis as revealed by Western blot analysis. The observation that the ECM produced by infected endothelial cells can direct the synthetic patterns of uninfected endothelial cells in a manner uniquely observed in infected endothe-lial cells suggests a plausible pathway by which infection of only a few cells can ultimately result in the coordinate responses of neighboring uninfected cells.
    Additional Material: 4 Ill.
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  • 9
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Transforming growth factor-beta (TGF-β) autoregulates its expression in several mammalian cell types. We now report that addition of TGF-βs 1, 2, and 3 to primary chicken embryo cells differentially affects expression of the messenger RNAs for the different TGF-β isoforms depending on the cell type. In cultured sternal chondrocytes, addition of TGF-βs 1, 2, or 3 results in an increase in the steady-state levels of the messenger RNAs for TGF-βs 2 and 3, but does not change expression of TGF-β4 mRNA. In contrast, in cultured cardiac myocytes, addition of TGF-βs 1, 2, or 3 results in an increase in expression of TGF-βs 3 and 4 mRNAs, but does not change expression of TGF-β2 mRNA. Moreover, expression of TGF-βs 2, 3, and 4 mRNAs is not affected by addition of any of the TGF-βs to fibroblasts. Addition of platelet-derived growth factor (PDGF), epidermal growth factor (EGF), or interleukin-1 (IL-1) to these chicken cells also has differential effects on expression of the different TGF-β mRNAs depending on the cell type. Retinoic acid also has contrasting effects on chondrocytes and myocytes either increasing or decreasing, respectively, expression of TGF-βs 2 and 3 mRNAs and TGF-β2 protein. Our results indicate a complex pattern of regulation of the different TGF-β genes by themselves as well as by PDGF, EGF, IL-1, dexamethasone, TPA, and retinoic acid in chicken embryo cells.
    Additional Material: 5 Ill.
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  • 10
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Zeitschrift für anorganische Chemie 588 (1990), S. 77-83 
    ISSN: 0044-2313
    Keywords: Chemistry ; Inorganic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Description / Table of Contents: Single Crystal Investigation on AgF2For the first time single crystals of AgF2 (black, metalic bright) have been obtained by heating AgF2 powder under a mixture of HF and F2 in autoclaves at 400°C. It crystallizes orthorhombic in the space group Pbca - D2h15 (Nr. 61) - with a = 556.8(1), b = 583.1(1) and c = 510.1(1) pm; Z = 4.The Madelung Part of Lattice Energy, MAPLE, and the Effective Coordination Number, ECoN, via the Mean Fictive Ionic Radii, MEFIR, are calculated and discussed.
    Notes: Erstmals wurden schwarze, metallisch glänzende Einkristalle von AgF2 durch Erhitzen des mikrokristallinen AgF2 dargestellt (Monel-Autoklaven, T ≈ 400°C, HF/F2-Gemisch, 4 d). Die röntgenographische Untersuchung (a = 556,8(1); = 583,1(1); c = 510,1(1) pm; Z = 4; Parameter siehe Text) bestätigt die aus Neutronenbeugungsuntersuchung ermittelte Raumgruppe Pbca - D2h15 (Nr. 61) und ergibt Lageparameter, die mit den damals ermittelten Werten praktisch übereinstimmen. Der Madelunganteil der Gitterenergie, MAPLE, sowie Effektive Koordinationszahlen, ECoN, werden über Mittlere Fiktive Ionenradien, MEFIR, berechnet und diskutiert.
    Additional Material: 1 Ill.
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