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  • 1
    Electronic Resource
    Electronic Resource
    Evidence for Involvement of the Carboxy Terminus of Helix 1 of Growth Hormone in Receptor Binding: Use of Charge Reversal Mutagenesis to Account for Calcium Dependence of Binding and for Design of Higher Affinity Analogs (1994)
    s.l. : American Chemical Society
    Biochemistry 33 (1994), S. 11724-11733 
    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/bi00205a008
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Comparative analysis of CNS populations in knockout mice with altered growth hormone responsiveness (2004)
    Oxford, UK : Blackwell Science Ltd
    European journal of neuroscience 19 (2004), S. 0 
    Details
    ISSN: 1460-9568
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Recently we have shown that growth hormone (GH) inhibits neuronal differentiation and that this process is blocked by suppressor of cytokine signalling-2 (SOCS2). Here we examine several cortical and subcortical neuronal populations in GH hyper-responsive SOCS2 null (−/−) mice and GH non-responsive GH receptor null (GHR−/−) mice. While SOCS2−/− mice showed a 30% decrease in density of NeuN positive neurons in cortex compared to wildtype, GHR−/− mice showed a 25% increase even though brain size was decreased. Interneuron sub-populations were variably affected, with a slight decrease in cortical parvalbumin expressing interneurons in SOCS2−/− mice and an increase in cortical calbindin and calretinin and striatal cholinergic neuron density in GHR−/− mice. Analysis of glial cell numbers in cresyl violet or glial fibrillary acidic protein (GFAP) stained sections of cortex showed that the neuron : glia ratio was increased in GHR−/− mice and decreased in SOCS2−/− mice. The astrocytes in GHR−/− mice appeared smaller, while they were larger in SOCS2−/− mice. Neuronal soma size also varied in the different genotypes, with smaller striatal cholinergic neurons in GHR−/− mice. While the size of layer 5 pyramidal neurons was not significantly different from wildtype, SOCS2−/− neurons were larger than GHR−/− neurons. In addition, primary dendritic length was similar in all genotypes but dendritic branching of pyramidal neurons in the cortex appeared sparser in GHR−/− and SOCS2−/− mice. These results suggest that GH, possibly regulated by SOCS2, has multiple effects on central nervous system (CNS) development and maturation, regulating the number and size of multiple neuronal and glial cell types.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.0953-816X.2004.03308.x
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  • 3
    Electronic Resource
    Electronic Resource
    Caveolins in the repair phase of acute renal failure after oxidative stress (2004)
    Melbourne, Australia : Blackwell Science Pty
    Nephrology 9 (2004), S. 0 
    Details
    ISSN: 1440-1797
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: SUMMARY:  Ischaemia-reperfusion and toxic injury are leading causes of acute renal failure (ARF). Both of these injury initiators use secondary mediators of damage in oxygen-derived free radicals. Several recent publications about ischaemia-reperfusion and toxin-induced ARF have indicated that plasma membrane structures called caveolae, and their proteins, the caveolins, are potential participants in protecting or repairing renal tissues. Caveolae and caveolins have previously been ascribed many functions, a number of which may mediate cell death or survival of injured renal cells. This review proposes possible pathophysiological mechanisms by which altered caveolin-1 expression and localization may affect renal cell survival following oxidative stress.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1440-1797.2004.00356.x
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  • 4
    Electronic Resource
    Electronic Resource
    Model for growth hormone receptor activation based on subunit rotation within a receptor dimer (2005)
    [s.l.] : Nature Publishing Group
    Nature structural & molecular biology 12 (2005), S. 814-821 
    Details
    ISSN: 1545-9985
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] Growth hormone is believed to activate the growth hormone receptor (GHR) by dimerizing two identical receptor subunits, leading to activation of JAK2 kinase associated with the cytoplasmic domain. However, we have reported previously that dimerization alone is insufficient to activate full-length ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nsmb977
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  • 5
    Electronic Resource
    Electronic Resource
    Expression of growth hormone receptor/binding protein gene in liver and anterior pituitary
    Amsterdam : Elsevier
    Biology of the Cell 79 (1993), S. 85 
    Details
    ISSN: 0248-4900
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/0248-4900(93)90278-M
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  • 6
    Electronic Resource
    Electronic Resource
    Growth hormone receptor and serum binding protein: purification, cloning and expression (1987)
    [s.l.] : Nature Publishing Group
    Nature 330 (1987), S. 537-543 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] A putative growth hormone receptor from rabbit liver and the growth hormone binding protein from rabbit serum have the same ammo-terminal amino-acid sequence, indicating that the binding protein corresponds to the extracellular hormone-binding domain of the liver receptor. The complete ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/330537a0
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  • 7
    Electronic Resource
    Electronic Resource
    Growth hormone receptor expression in the nucleus and cytoplasm of normal and neoplastic cells (1998)
    Springer
    Histochemistry and cell biology 109 (1998), S. 141-159 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  Growth hormone (GH) exerts its regulatory functions in controlling metabolism, balanced growth and differentiated cell expression by acting on specific receptors which trigger a phosphorylation cascade, resulting in the modulation of numerous signalling pathways dictating gene expression. A panel of five monoclonal antibodies was used in mapping the presence and somatic distribution of the GH receptor by immunohistochemistry in normal and neoplastic tissues and cultured cells of human, rat and rabbit origin. A wide distribution of the receptor was observed in many cell types. Not all cells expressing cytoplasmic GH receptors displayed nuclear immunoreactivity. In general, the relative proportion of positive cells and intensity of staining was higher in neoplastic cells than in normal tissue cells. Immunoreactivity showed subcellular localisation of the GH receptor in cell membranes and was predominantly cytoplasmic, but strong nuclear immunoreaction was also apparent in many instances. Intense immunoreactivity was also observed in the cellular Golgi area of established cell lines and cultured tissue-derived cells in exponential growth phase, indicating cells are capable of GH receptor synthesis. The presence of intracellular GH receptor, previously documented in normal tissues of mostly animal origin, is the result of endoplasmic reticulum and Golgi localisation. Heterogeneity of immunoreactivity was found in normal and neoplastic tissue with a variable range of positive cells. The nuclear localisation of immunoreactivity is the result of nuclear GH receptor/binding protein, identically to the cytosolic and plasma GH-binding protein, using a panel of five monoclonal antibodies against the GH receptor extracellular region. The expression of GH receptors, not only on small proliferating tumour cells such as lymphocytes, but also on well differentiated cells including keratinocytes, suggests that GH is necessary not only for differentiation of progenitor cells, but also for their subsequent clonal expansion, differentiation and maintenance.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004180050212
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  • 8
    Electronic Resource
    Electronic Resource
    Vinculin localization and actin stress fibers differ in thyroid cells organized as monolayers or follicles (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 32 (1995), S. 318-331 
    Details
    ISSN: 0886-1544
    Keywords: cytoskeleton ; cyclic AMP ; vinculin ; E-cadherin ; ZO-1 ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: In epithelial cells interactions between the actin cytoskeleton and cell-cell junctions regulate paracellular permeability and partcipate in morphogenesis. We have studied the relationship between supracellular morphology and actin-junction interactions using primary cultures of porcine thyroid cells grown either as three-dimensional follicles or as open monolayers. Regardless of morphology, thyroid cells assembled occluding and adhesive junctions containing ZO-1 and E-cadherin, respectively, and showed F-actin staining in apical microvilli and a perijunctional ring. In monolayers, actin stress fibers were also observed in the apical and basal poles of cells, where they terminated in the vinculin-rich zonula adherens and in cell-substrate focal adhesions, respectively. Surprisingly, we were unable to detect vinculin localization in follicular cells, which also did not form stress fibers. Immunoblotting confirmed significantly greater vinculin in triton-insoluble fractions from monolayer cells compared with follicular cells. Incubation of monolayers with 8 chloro(phenylthio)-cyclic AMP decreased the level of immunodetectable vinculin in the zonula adherens, indicating that junctional incorporation of vinculin was regulated by cyclic AMP. In monolayer cultures, cytochalasin D (1 μM) caused actin filaments to aggregate associated with retraction of cells from one another and the disruption of cell junctions. Despite morphologically similar perturbations of actin organization in follicular cultures treated with cytochalasin D, junctional staining of ZO-1 and E-cadherin was preserved and cells remained adherent to one another. We conclude that in cultured thyroid cells structural and functional associations between actin filaments and cellular junctions differ depending upon the supracellular morphology in which cells are grown. One important underlying mechanism appears to be regulation of vinculin incorporation into adhesive junctions by cyclic AMP. © 1995 Wiley-Liss, Inc.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970320408
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