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  • Articles  (68)
  • Life and Medical Sciences
  • SOLAR PHYSICS
  • 1985-1989  (46)
  • 1980-1984  (22)
  • 1940-1944
  • Chemistry and Pharmacology  (68)
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  • Articles  (68)
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  • 1
    ISSN: 0730-2312
    Keywords: elastase inhibitors ; β-lactams ; lung damage ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Human polymorphonuclear leukocyte elastase (PMN elastase) is inhibited by L-659, 286 (7α-methoxy-8-oxo-3-[[(1,2,5,6-tetrahydro-2-methyl-5,6-dioxo-1,2,4-triaz-in-3-yl)thio]methyl]-5-thia-1-aza-6R-bicyclo [4.2.O]oct-2-ene-2-pyrrolidine carboxamide-5,-dioxide) with a Ki of 0.4 μM. This inhibition is time-dependent, rapid, and only slowly reversible, with a t1/2 of 〉 3 days at 25°C. L-659, 286 is also highly selective for PMN elastase, as it does not inhibit thrombin, trypsin, papain, plasmin, chymotrypsin, or cathepsin G. L-659, 286 administered intratracheally inhibits lung damage caused by administration via the same route of human PMN elastase into hamsters. In marmosets, L-659, 286 is cleared from blood very rapidly after an intravenous injection but is recovered in bronchoalveolar lavage fluid for several hours after intratracheal administration.
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  • 2
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 20 (1982), S. 283-292 
    ISSN: 0730-2312
    Keywords: insulin receptor ; basic somatomedin receptor ; human placenta ; peptide maps ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The disuccinimidy! suberate, affinity-labeling procedure, and proteolytic mapping techniques have been employed to characterize further the human placental receptors for insulin and basic somatomedin. Electrophoretic analysis of the basic somatomedin receptor, selectively crosslinked to 125I basic somatomedin in the presence of excess native insulin revealed, under reducing conditions, major labeled constituents of 270-280 and 125-140 kd, substantiating our previous work employing a photoaffinity labeling reagent. Affinity labeling also demonstrated the presence of less intensely labeled components with apparent molecular weights of 40 and 45 kd but failed to reveal a distinct 90- to 100-kd species observed in parallel experiments with insulin. In the absence of β-mercaptoethanol, all components specifically labeled with 125I basic somatomedin migrated in the 300- to 400-kd range. In comparison, selective affinity labeling of the insulin receptor in the presence of excess native basic somatomedin revealed components, upon electrophoresis under reducing conditions, with apparent molecular weights of 270-280, 125-140, 90-100, and 40 kd. The major insulin-labeled component (125-140 kd) comigrated with the major constituent (125-140 kd) selectively labeled with basic somatomedin. When digestion was performed prior to solubilization, chymotryptic and tryptic proteolysis of the membrane-localized selectively labeled insulin, and basic somatomedin receptors yielded quite similar gel electrophoretic maps. However, when digestion was done subsequent to solubilization, chymotryptic and tryptic proteolysis of selectively labeled insulin and basic somatomedin receptors solubilized in SDS yielded similar but not identical gel electrophoretic maps. We conclude that the receptors for basic somatomedin and insulin are highly homologous structures with respect to their disulfide crosslinked composition, and with respect to the size of the major components detected by selective affinity-labeling procedures. Nevertheless, the detection of electrophoretically distinct labeled receptor components upon analysis of specifically labeled intact or proteolytically digested receptors points to subtle differences between the polypeptide compositions of the two receptors.
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  • 3
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 37 (1988), S. 1-9 
    ISSN: 0730-2312
    Keywords: colon cancer ; metastasis ; mucins ; electrophoresis ; lectins ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: We have found that polyacrylamide gel electrophoresis in 3% gels in the presence of sodium dodecyl sulfate is suitable for the separation of cellular glycoproteins having molecular weights ranging from 200,000 to 1,000,000. The gels secured on a rigid support (Gelbond) allow blotting techniques with lectins and antibodies for the detection of glycoproteins. Using these methods we have separated lysates of HT-29 human colon carcinoma cells and detected at Jeast four distinct high molecular weight Sialoglycoproteins having molecular weights of 900,000, 740.000, 560,000, and 450,000. The expression of the 9000,000 component, as revealed by wheat germ agglutinin binding, was much higher in a subline of HT-29 cells established from liver metastases in a nude mouse than it was in the parental cells. The relative intensity of wheat germ agglutinin binding to these four sialoglycoprotein components differs depending upon their growth phase in vitro. These glycoproteins were also detectable by the binding of peanut agglutinin, provided the glycoproteins were previously treated in the gels with mild acid to remove the sialic acid from their carbohydrate chains, suggesting that mucin-type carbohydrate chains are present on these glycoproteins. The same set of glycoproteins can be detected by metabolic labeling of the cells with [3H] glucosamine in tissue culture. Very similar glycoprotein profiles are revealed by metabolic labeling of fresh colon carcinoma tissues with [3H] glucosamine in vitro.
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  • 4
    ISSN: 0730-2312
    Keywords: oncogenes ; vitamin A ; thyroid hormones ; mammary cells ; cancer ; epithelial cells ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: We have investigated the actions of transforming growth factor (TGF) type α on epidermal growth factor (EGF) receptor mRNA expression in MDA-468 human mammary carcinoma cells in serum-free media. We found that exposure of MDA-468 cells to TGFα results in elevated levels of EGF receptor mRNA. This increase in mRNA accumulation showed time and dose dependence. Addition of TGFβ1 enhanced the accumulation of EGF receptor mRNA induced by TGFα in a time and dose-dependent manner. We also found that triiodothyronine at physiological concentrations exerts synergistic control on the action of TGFα alone, or in association with TGFβ1, on EGF receptor mRNA expression. Similarly, retinoic acid treatment also enhanced in a time- and dose-dependent manner the TGFα-dependent response of EGF receptor mRNA and acted synergistically with TGFβ1. The results described here suggest that optimum regulation of EGF receptor gene expression by TGFα is a complex process involving synergistic interactions with heterologous growth factors and hormones.
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  • 5
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 22 (1983), S. 15-29 
    ISSN: 0730-2312
    Keywords: Rhodopseudomonas sphaeroides ; photosynthetic membrane synthesis ; cell cycle ; freeze fracture ; macromolecule distribution ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The steady-state biosynthesis of the photosynthetic membrane (ICM) of Rhodopseudomonas sphaeroides has been reviewed. At moderate light intensities, 500 ft-c, preexisting ICM serves as the insertion matrix for newly synthesized membrane components. Whereas the bulk of the membrane protein, protein-pigment complexes, and pigments are inserted into preexisting ICM throughout the cell cycle, phospholipid is transferred from outside the ICM to the ICM only at the time of cell division. Because the site of cellular phospholipid synthesis is the cytoplasmic membrane, these results infer that despite the physical continuity of cytoplasmic membrane and ICM, there must exist between these membranous domains a “barrier” to the free diffusion of cellular phospholipid. The cyclical alternation in protein to phospholipid ratio of the ICM infers major structural and functional alternations, such as changes in the protein to lipid ratio of the membrane, specific density of the membrane, lipid structure within the membrane, and the rate of cyclic electron flow. When biochemical studies are correlated with detailed electron microscopic investigations we can further conclude that the number of photosynthetic units within the plane of the membrane can vary by nearly a factor of two over the course of the cell cycle. The average physical size of the photosynthetic units is constant for a given light intensity but inversely proportional to light intensity. The distribution of photosynthetic unit size classes within the membrane can be interpreted as suggesting that the “core” of the photosynthetic unit (reaction center plus fixed antenna complex) is inserted into the membrane coordinately as a structural entity. The variable antenna complex is, on the other hand, inserted independent of the “core” and randomly associates with both old and new core complexes. Finally, we conclude that there is substantial substructure to the distribution of photosynthetic units within the ICM, ie, they are highly ordered and exist in a defined spatial orientation to one another.
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  • 6
    ISSN: 0730-2312
    Keywords: fatty acid-binding protein ; mechanism of action ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Mammary-derived growth inhibitor (MDGI), a polypeptide growth inhibitor isolated from lactating bovine mammary tissue, previously shown to have extensive sequence homology with fatty acid-binding proteins, was demonstrated to meet the criteria of a fatty acid-binding protein. The protein was found to bind [3H]palmitic acid in a saturable manner and to be complexed with endogeneous free fatty acids. [3H]palmitic acid, when bound to the protein, was more rapidly taken up by the target cells (human mammary carcinoma cells [MaTu]) than was free [3H]palmitic acid, suggesting a lipid carrier function for the inhibitor. It is suggested that the fatty acid-binding properties of MDGI may relate to its ability to inhibit cell growth in vitro and to regulate other cellular functions.
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  • 7
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 39 (1989), S. 117-128 
    ISSN: 0730-2312
    Keywords: growth factor ; aFGF ; immunoassay ; eye ; vitreous body ; cornea ; retina ; lens ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: During the last ten years, several groups, including the present authors, have detected growth factor activities in various ocular tissues, and the presence of a ubiquitous Eye-Derived Growth Factor (EDGF) has been described. More recently, isolation and characterization of this growth factor activity from the retina led to the identification of two molecules. These molecules were shown to be identical to other growth factors isolated from neuronal and non-neuronal tissues and are now designated as acidic and basic fibroblast growth factor (aFGF, bFGF). The biological function and the reason for the ubiquitous distribution of these factors remain unclear. Understanding may be improved by quantification of this distribution in various tissues during development. In the present study, specific polyclonal antibodies were raised against acidic FGF, aFGF was determined in various ocular tissues by enzyme immunoassay, and the localization of immuno-reactive aFGF by immunohistological staining with fluorescent antibodies or with enzyme- or gold-labeled antibodies was studied.In almost all tissues tested aFGF was found; but the retina, cornea, and vitreous body contained the highest levels of aFGF per gram of tissue. In the retina, aFGF was associated primarily with the nerve fiber layer and the inner and outer segments of the photoreceptors, whereas corneal aFGF was detected in the cytoplasma of the basal layer of epithelial cells.
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  • 8
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 19 (1982), S. 293-304 
    ISSN: 0730-2312
    Keywords: reverse-transcription ; strand-displacement synthesis ; heteroduplex DNA ; DNA H-structures ; proviral integration ; homologous recombination ; transduction ; recombination models ; RNA tumor viruses ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The avian retroviruses - and probably other retroviruses as well - undergo a variety of recombinational events with relatively high efficiency. An understanding of the molecular basis of these events should provide insight into the important biological properties these agents exhibit when they become integrated into somatic or germ-line host cells, when they exchange genetic information among themselves, or when they transduce host cell genes. In this article we review molecular models for homologous recombination, against a background of the other types of recombination events that arc typical of these viruses. It seems probable that the retroviruses will provide useful models for analysis of a variety of DNA rearrangements known to occur in eukaryotic cells.
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  • 9
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 19 (1982), S. 383-394 
    ISSN: 0730-2312
    Keywords: epidermal growth factor ; receptors ; endocytosis ; cell surface ; response kinetics ; compartmentation ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: We have investigated the stimulation of fluid phase endocytosis by epidermal growth factor (EGF) in normal human fibroblasts using 125I-labeled polyvinylpyrrolidone (125I-PVP) as a fluid phase marker. We found that EGF initially induced a thereefold increase in the rate of 125I-PVP uptake. This initial burst of fluid uptake terminated within 10 min. Thereafter, the rate of fluie uptake in EGF-treated cells was approximately 40% higher than in control cells. To identify the cellular site of EGF action in stimulating fluid phase endocytosis, we examined the kinetics of the induction of this response as well as the kinetics of cell surface binding and internalization of 125I-EGF. Although there was no detectable lag between binding of EGF to the cell surface and its internalization, the kinetics of the two processes were quite different. Significantly, the kinetics of induction of 125I-PVP uptake matched the kinetics of binding of 125I-EGF to its cell surface receptors, indicating that the signal for the increase in fluid phase endocytosis is generated at the cell surface. To determine if EGF-stimulated fluid phase endocytosis was related to EGF-stimulated endocytosis of its own receptor, we compared the EGF dose dependency and time course of the two processes. Although the stimulated endocytosis of the EGF receptor was not saturable with respect to the concentration of EGF used, the stimulation of fluid phase endocytosis was half maximal at an EGF concentration of 1 ng/ml and saturated at a concentration of 5 ng/ml. Also, the stimulation of fluid phase endocytosis was sevenfold greater initially after adding EGF than after a 30-min continuous incubation with the hormone, whereas the enhanced clearance of the EGF receptor did not change during this time period. We conclude that the EGF-stimulated increase in fluid phase endocytosis is not directly coupled to EGF-stimulated endocytosis of its own receptor but instead to a separate signal generated at the cell surface.
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  • 10
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 20 (1982), S. 29-39 
    ISSN: 0730-2312
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Additional Material: 9 Ill.
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