Properties of nuclear and cytosolic ecdysteroid receptors from an epithelial cell line from Chironomus tentans

1992 ◽  
Vol 38 (2) ◽  
pp. 81-91 ◽  
Author(s):  
A. Turberg ◽  
K.-D. Spindler
1993 ◽  
Vol 23 (1) ◽  
pp. 159-164 ◽  
Author(s):  
Andreas Fretz ◽  
Andrea Lübbert ◽  
Ulrich Markmann-Mulisch ◽  
Margarethe Spindler-Barth ◽  
Klaus-Dieter Spindler

1992 ◽  
Vol 47 (3-4) ◽  
pp. 280-284 ◽  
Author(s):  
Klaus-Dieter Spindler ◽  
Margarethe Spindler-Barth ◽  
Andreas Turberg ◽  
Günter Adam

Abstract The two brassinosteroids, 22S′,23S′-homobrassinolide and 22S′,23S′-homocastasterone are weak competitors of the binding of [3H]ponasterone A to the intracellular ecdysteroid receptor from the epithelial cell line from Chironom us tentans. The relative affinities to the ecdysteroid receptor are 0.001 for both brassinosteroids as compared to 20-OH-ecdysone and 0.1 in comparison to ecdysone. Both substances exert morphological effects similar to those observed with 20-OH-ecdysone. Like moulting hormones both brassinosteroids inhibit chitin synthesis. However, these effects were observed only at rather high concentrations (10-5 to 10-4 m) which were cytotoxic for 22 S′,23 S′-homobrassinolide.


1991 ◽  
Vol 46 (11-12) ◽  
pp. 1089-1093 ◽  

Acetylcholinesterase (AchE) can be induced in a non-neuronal, epithelial cell line from Chironomus tentans by the moulting hormone 20-OH-ecdysone. Maximal response is reached after 7 days. The increase in enzymatic activity can be suppressed by simultaneous incubation with inhibitors of transcription and translation. The potency of various steroid hormones to induce AchE coincides with their affinity to the ecdysteroid hormone receptor. AchE from Chironomus is tightly bound to membranes and cannot be solubilized by heparin or collagenase treatment. Incubation under conditions where phospholipase C is most active releases activity into the supernatant. If phospholipase is applied in addition, the amount of solubilized enzyme increases, but there is still membrane-bound activity left. This is in accordance with a globular form of AchE linked to membranes by a phospholipid-anchor. The enzyme sediments as a single peak of 5.4 S.


1986 ◽  
Vol 25 ◽  
pp. 103
Author(s):  
M. Spindler-Barth ◽  
R. Krahwinkel ◽  
V. Kanmann ◽  
A. Turberg ◽  
M. Lezzi ◽  
...  

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