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  • Cell & Developmental Biology  (5)
  • 1985-1989  (5)
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  • 1
    Electronic Resource
    Electronic Resource
    Heat shock stimulates the release of arachidonic acid and the synthesis of prostaglandins and leukotriene B4 in mammalian cells (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 141 (1989), S. 325-333 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Heat shock has a profound influence on the metabolism and behavior of eukaryotic cells. We have examined the effects of heat shock on the release from cells of arachidonic acid and its bioactive eicosanoid metabolites, the prostaglandins and leukotrienes. Heat shock (42-45°) increased the rate of arachidonic acid release from human, rat, murine, and hamster cells. Arachidonate accumulation appeared to be due, at least partially, to stimulation of a phospholipase A2 activity by heat shock and was accompanied by the accumulation of lysophosphatidyl-inositol and lysophosphatidylcholine in membranes. Induction of arachidonate release by heat did not appear to be mediated by an increase in cell Ca+ +. Stimulation of arachidonate release by heat shock in hamster fibroblasts was quantitatively similar to the receptor-mediated effects of β thrombin and bradykinin. The effects of heat shock and β thrombin on arachidonate release were inhibited by glucocorticoids. Increased arachidonate release in heat-shocked cells was accompanied by the accelerated accumulation of cyclooxygenase products prostaglandin E2 and prostaglandin F2α and by 5-lipoxygenase metabolite leukotriene B4. Elevated concentrations of arachidonic acid and metabolites may be involved in the cytotoxic effects of hyperthermia, in homeostatic responses to heat shock, and in vascular and inflammatory reactions to stress.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041410214
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Insulin binding and vesicular ingestion in capillary endothelium (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 124 (1985), S. 87-95 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Capillary endothelium can actively regulate vascular permeability of various serum proteins. Hormones such as insulin must interact with this capillary barrier in order to reach their respective target tissues. We have studied the binding and subsequent internalization of 125I-insulin in both native (freshly isolated) and primary cultured capillary endothelium derived from rat epididymal fat pads. Insulin association with the endothelium, internalization and degradation differed between freshly isolated and primary cultured capillaries. Specific binding in freshly isolated and cultured capillaries was temperature dependent, and was competitively inhibited in the presence of unlabelled insulin. Primary cultures of capillaries grown to confluence did not exhibit specific binding of insulin. Despite the lack of specific receptors for insulin, cultured cells vesicularly internalized insulin. Greater than 50% of the total associated insulin was not degraded by cultured endothelium. Morphological examinations using ferritin labelled insulin localized insulin associated to the capillary endothelial cell membrane and sequestered within pinocytotic vesicles. Incubation of freshly isolated capillaries with insulin stimulated the fluid phase endocytosis of 14C-sucrose; however, insulin had no effect on fluid phase endocytosis in cultured capillaries. These results indicate that capillary endothelium, isolated from rat epididymal fat, exhibit specific receptors for insulin. Binding of insulin to the capillary membrane is followed by internalization into cytoplasmic vesicles and partial degradation.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041240115
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  • 3
    Electronic Resource
    Electronic Resource
    Mechanism of sucrose uptake by isolated rat hepatocytes (1987)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 133 (1987), S. 175-180 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The transport of molecules by nonspecific endocytosis has been described in many cell types, but it has not been characterized in hepatocytes. Because of its central role in the clearance of solutes from portal blood, endocytosis might represent a significant mode of cellular transport. We investigated the mechanism of sucrose uptake in an isolated hepatocyte system. Liver cells were isolated by perfusion and collagenization of rat liver, followed by differential centrifugation. Hepatocytes were then incubated with 14C-sucrose and harvested by spinning through oil in microfuge tubes. Radioactivity was standardized against DNA content. We found that sucrose uptake is concentration-dependent from 5 μM to 100 mM and follows first-order kinetics. Washout studies indicate that exocytosis is responsible for the dynamic equilibrium reached. Arrhenius analysis of temperature dependence yields a linear plot (Ea = 14.2 Kcal/mol). In addition, sucrose uptake is independent of cellular ATP levels. We conclude that sucrose is transported by fluid-phase micropinocytosis in isolated hepatocytes and that this transport mechanism may be important in the uptake of diverse molecules into liver cells.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041330123
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  • 4
    Electronic Resource
    Electronic Resource
    Investigation of adenylate energy charge, phosphorylation potential, and ATP concentration in cells stressed with starvation and heat (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 124 (1985), S. 261-268 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: We have attempted to determine the appropriate parameter of energy status assoiciated with the survival of CHO fibroblasts under starvation conditions. Survival correlated well with adenylate energy charge (EC) but not so well with the phosphorylation potential or ATP concentration. Starved cells exhibited the capacity to resist (transiently) decreases in both EC and survival. A fall in EC was associated with decreased survival. Using this correlation, we subsequently investigated whether killing after thermal stress occurred by a mechanism analogous to starvation, perhaps due to inhibition of energy yielding pathways. This hypothesis proved to be false; over 99% of cells were killed before a decrease was observed in any of the parameters of energy status. Cells were, however, sensitized to heat under nutritionally deprived conditions, a finding which may be significant for tumor treatment by heat in vivo.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041240214
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  • 5
    Electronic Resource
    Electronic Resource
    Heat stress stimulates inositol trisphosphate release and phosphorylation of phosphoinositides in CHO and Balb C 3T3 cells (1987)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 130 (1987), S. 369-376 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Exposure of eukaryotic cells to elevated temperature leads to profound switches in cell metabolism and gene expression which may be involved in cellular homeostatic mechanisms. We have investigated the effect of heat shock (45°C) on the metabolism of the phosphoinositides, a class of phospholipids involved in the function of Ca2+-linked membrane receptors. Heat shock led to stimulation of phosphoinositide turnover in HA1-CHO and Balb C 3T3 cells, resulting in the rapid accumulation of inositol trisphosphate (lP3). Mitogenic and α1 adrenergic stimulation, with serum or phenylephrine, led to similar increases in lP3. Heat shock also caused rapid increase in phosphorylation of polyphosphoinositides (PPl). Prolonged exposure to heat 〉15 min at 45°C led to progressive cellular toxicity which was associated with depletion of PPl. This decline in PPl concentration appeared to result from inhibition of PPl resynthesis. In this respect, heat may resemble some other types of cellular stresses in stimulating membrane phospholipases to deplete classes of membrane phospholipids. The induction of PPl turnover may, therefore, be involved in both plelotropic responses to brief heat shock and toxicity resulting from prolonged thermal stress.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041300309
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