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  • 1
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Experimental Cell Research 56 (1969), S. 265-268 
    ISSN: 0014-4827
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Comparative Biochemistry and Physiology -- Part A: Physiology 90 (1988), S. 809 
    ISSN: 0300-9629
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Molecular Cell Research 1222 (1994), S. 477-482 
    ISSN: 0167-4889
    Keywords: Protein kinase C ; Regulatory volume decrease ; Regulatory volume increase ; Sodium/potassium/chloride cotransport
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Reviews on Biomembranes 864 (1986), S. 1-31 
    ISSN: 0304-4157
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Biomembranes 266 (1972), S. 206-216 
    ISSN: 0005-2736
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Biomembranes 1110 (1992), S. 199-201 
    ISSN: 0005-2736
    Keywords: (Ehrlich ascites tumor cell) ; Actin ; Cytochalasin B ; Microfilament ; Sodium/potassium/chloride cotransport ; Volume regulation
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    The journal of membrane biology 163 (1998), S. 97-110 
    ISSN: 1432-1424
    Keywords: Key words: Patch clamp — Ca2+- and voltage-dependence — Regulatory Volume Decrease — Tamoxifen — Niflumic acid — Mg2+
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract. A Ca2+-activated (I Cl,Ca) and a swelling-activated anion current (I Cl,vol) were investigated in Ehrlich ascites tumor cells using the whole cell patch clamp technique. Large, outwardly rectifying currents were activated by an increase in the free intracellular calcium concentration ([Ca2+] i ), or by hypotonic exposure of the cells, respectively. The reversal potential of both currents was dependent on the extracellular Cl− concentration. I Cl,Ca current density increased with increasing [Ca2+] i , and this current was abolished by lowering [Ca2+] i to 〈1 nm using 1,2-bis-(o-aminophenoxy)ethane-N,N,N′,N′-tetra-acetic acid (BAPTA). In contrast, activation of I Cl,vol did not require an increase in [Ca2+] i . The kinetics of I Cl,Ca and I Cl,vol were different: at depolarized potentials, I Cl,Ca as activated in a [Ca2+] i - and voltage-dependent manner, while at hyperpolarized potentials, the current was deactivated. In contrast, I Cl,vol exhibited time- and voltage-dependent deactivation at depolarized potentials and reactivation at hyperpolarized potentials. The deactivation of I Cl,vol was dependent on the extracellular Mg2+ concentration. The anion permeability sequence for both currents was I − 〉 Cl− 〉 gluconate. I Cl,Ca was inhibited by niflumic acid (100 μm), 5-Nitro-2-(3-phenylpropylamino)benzoic acid (NPPB, 100 μm) and 4,4′-diisothiocyano-2,2′-stilbenedisulfonic acid (DIDS, 100 μm), niflumic acid being the most potent inhibitor. In contrast, I Cl,vol was unaffected by niflumic acid (100 μm), but abolished by tamoxifen (10 μm). Thus, in Ehrlich cells, separate chloride currents, I Cl,Ca and I Cl,vol, are activated by an increase in [Ca2+] i and by cell swelling, respectively.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    The journal of membrane biology 173 (2000), S. 19-29 
    ISSN: 1432-1424
    Keywords: Key words: Lysophosphatidic acid — [Ca2+]i— Whole cell currents — pHi— F-actin cytoskeleton
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract. The present study aimed at elucidating the initial intracellular lysophosphatidic acid (LPA)-induced signaling events, in order to investigate the sequence in which LPA affects the intracellular concentration of free, cytosolic Ca2+, [Ca2+] i , ion channels, the F-actin cytoskeleton, cell volume and the Na+/H+ exchanger. We found that stimulation of Ehrlich cells with LPA induced a transient, concentration-dependent increase in [Ca2+] i , which is due to Ca2+ release from intracellular Ins(1,4,5)P3-sensitive stores as well as an influx of Ca2+. The EC50 values for LPA-induced Ca2+ mobilization were estimated at 0.03 nm and 0.4 nm LPA in the presence and absence of extracellular Ca2+, respectively. The LPA-induced increase in [Ca2+] i resulted in (i) co-activation of Ca2+-activated, charybdotoxin (ChTX)-sensitive K+ and niflumic acid-sensitive Cl− currents; (ii) a subsequent cell shrinkage and increased polymerization of F-actin, and (iii) activation of a Na+/H+ exchange, resulting in a concentration-dependent intracellular alkalinization. The EC50 value for the LPA-induced rate of alkalinization was estimated at 0.37 nm LPA. When cell shrinkage was prevented, the LPA-induced activation of the Na+/H+ exchanger was impaired. In conclusion, the initial signaling events induced by LPA involves activation of volume regulatory mechanisms.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Springer
    The journal of membrane biology 151 (1996), S. 159-173 
    ISSN: 1432-1424
    Keywords: Key words: LTD4— LTD4-receptors — Desensitization — Ca2+— Ca2+-depletion — BAPTA — Volume regulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract. Stimulation with leukotriene D4 (LTD4) (3–100 nm) induces a transient increase in the free intracellular Ca2+ concentration ([Ca2+] i ) in Ehrlich ascites tumor cells. The LTD4-induced increase in [Ca2+] i is, however, significantly reduced in Ca2+-free medium (2 mm EGTA), and under these conditions stimulation with a low LTD4 concentration (3 nm) does not result in any detectable increase in [Ca2+] i . Addition of LTD4 (3–100 nm) moreover accelerates the KCl loss seen during Regulatory Volume Decrease (RVD) in cells suspended in a hypotonic medium. The LTD4-induced (100 nm) acceleration of the RVD response is also seen in Ca2+-free medium and also at 3 nm LTD4, indicating that LTD4 can open K+- and Cl−-channels without any detectable increase in [Ca2+] i . Buffering cellular Ca2+ with BAPTA almost completely blocks the LTD4-induced (100 nm) acceleration of the RVD response. Thus, the reduced [Ca2+] i level after BAPTA-loading or buffering of [Ca2+] i seems to inhibit the LTD4-induced stimulation of the RVD response even though the LTD4-induced cell shrinkage is not necessarily preceded by any detectable increase in [Ca2+] i . The LTD4 receptor antagonist L649,923 (1 μm) completely blocks the LTD4-induced increase in [Ca2+] i and inhibits the RVD response as well as the LTD4-induced acceleration of the RVD response. When the LTD4 receptor is desensitized by preincubation with 100 nm LTD4, a subsequent RVD response is strongly inhibited. In conclusion, the present study supports the notion that LTD4 plays a role in the activation of the RVD response. LTD4 seems to activate K+ and Cl− channels via stimulation of a LTD4 receptor with no need for a detectable increase in [Ca2+] i .
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    The journal of membrane biology 160 (1997), S. 47-58 
    ISSN: 1432-1424
    Keywords: Key words: Arachidonic acid release — Cytosolic phospholipase A2— Phospholipase D — G-proteins — Cell volume regulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract. Ehrlich ascites tumor cells, loaded with 3H-labeled arachidonic acid and 14C-labeled stearic acid for two hours, were washed and transferred to either isotonic or hypotonic media containing BSA to scavenge the labeled fatty acids released from the cells. During the first two minutes of hypo-osmotic exposure the rate of 3H-labeled arachidonic acid release is 3.3 times higher than that observed at normal osmolality. Cell swelling also causes an increase in the production of 14C-stearic acid-labeled lysophosphatidylcholine. This indicates that a phospholipase A2 is activated by cell swelling in the Ehrlich cells. Within the same time frame there is no swelling-induced increase in 14C-labeled stearic acid release nor in the synthesis of phosphatidyl 14C-butanol in the presence of 14C-butanol. Furthermore, U7312, an inhibitor of phospholipase C, does not affect the swelling induced release of 14C-labeled arachidonic acid. Taken together these results exclude involvement of phospholipase A1, C and D in the swelling-induced liberation of arachidonic acid. The swelling-induced release of 3H-labeled arachidonic acid from Ehrlich cells as well as the volume regulatory response are inhibited after preincubation with GDPβS or with AACOCF3, an inhibitor of the 85 kDa, cytosolic phospholipase A2. Based on these results we propose that cell swelling activates a phospholipase A2—perhaps the cytosolic 85 kDa type—by a partly G-protein coupled process, and that this activation is essential for the subsequent volume regulatory response.
    Type of Medium: Electronic Resource
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