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  • 1995-1999  (3)
  • 1999
  • 1995  (3)
  • Cell & Developmental Biology  (3)
  • 1
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 165 (1995), S. 367-375 
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The expression of the 72 kD inducible heat shock protein (hsp72) has been reported to be cell cycle associated in unheated, synchronized HeLa cells. In this study, flow cytomerty was used to investigate hsp72 levels through the cell cycle in HeLa cells by dual labeling with propidium iodide and antibodies against hsp72. The entire cell cycle distribution of hsp72 could be measured in a single sample of asynchronously growing cells. For unheated cells, the level of hsp72 increased about 30% from G1 to S phase, with about a 65% increase in G2/M, probably due to cell size differences. Neither mitotic selection nor serum stimulation induced a higher level of hsp72 than in the control cells. Western blot analysis of hsp72 from Hoechst-stained cells sorted from G1, mid-S, or G2/M showed that G1 cells had the lowest level of hsp72, with about a 30% increase in S phase and a 60% increase in G2/M, in good agreement with the flow cytometry results. These data conflict with previous reporty by other laboratories which showed a 3-fold higher level of hsp72 in S phase than in G1 or G2. In contrast, heat shock (both acute and chronic) led to a non-uniform increase in hsp72 through the cell cycle. Most cells in mid S phase had high levels of hsp72, and a larger range in the levels of hsp72 were found in G1 and late S/G2/M phase cells. © 1995 Wiley-Liss, Inc.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 164 (1995), S. 491-498 
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: RNA blots of total cellular RNA isolated from quiescent and endothelin (ET-1)-stimulated normal rat kidney (NRK) cells demonstrated that ET-1 induced the expression of c-jun, jun B, and c-fos mRNA in a time-dependent manner with maximal expression of mRNA by 1 hr after the addition of ET-1. Five hundred picomolal ET-1 was sufficient to induce maximal mRNA expression. These data agreed with saturation experiments which demonstrated that maximal binding of [125I]ET-1 was achieved at concentrations greater than 100 pM. The Kd and Bmax values for [125I]ET-1 binding to NRK membranes were 20.5 pM and 22.2 fmol/mg protein, respectively. Competition experiments for the binding of [125I]ET-1 to NRK membranes demonstrated that ET-1 was a more potent inhibitor (Ki = 0.047 nM) than ET-3 (Ki = 10.8 nM). No specific binding of [125I]ET-3 (40 or 500 pM) to NRK membranes could be observed. The expression of c-jun, jun B, and c-fos mRNA was inhibited by the endothelin type A receptor (ET)-selective antagonist, BQ-123. Thus, these data demonstrate that ET-1 mediates the expression of immediate response gene mRNA in NRK cells via the ETA receptor. ET-1 stimulation of NRK cells also upregulated EGF receptors, providing a possible mechanism for ET-1 complementation of epidermal growth factor (EGF) mitogenicity in NRK cells. © 1995 Wiley-Liss, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    BioEssays 17 (1995), S. 129-138 
    ISSN: 0265-9247
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The plasma membrane of polarized epithelial cells is divided into apical and basolateral surfaces, with different compositions. Proteins can be sent directly from the trans-Golgi network (TGN) to either surface, or can be sent first to one surface and then transcytosed to the other. The glycosyl phosphatidylinositol anchor is a signal for apical targeting. Signals in the cytoplasmic domain containing a β-turn determine basolateral targeting and retrieval, and are related to other sorting signals. Transcytosed proteins, such as the polymeric immunoglobulin receptor (plgR), are endocytosed from the basolateral surface and then accumulate in a tubular compartment concentrated underneath the apical surface. This compartment, tentatively termed the apical recycling compartment, may be a central sorting station, as it apparently receives material from both surfaces and sorts them for delivery to the correct surface. Delivery to the apical surface from both the TGN and the apical recycling compartment appears to be regulated by protein kinases A and C, and endocytosis from the apical surface is also regulated by kinases. Transcytosis of the plgR is additionally regulated by phosphorylation of the plgR and by ligand binding to the plgR. Regulation of traffic in polarized epithelial cells plays a central role in cellular homeostasis, response to external signals and differentiation.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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