scholarly journals Ultrastructural changes during the enhancement of cellular 3-hydroxy-3-methyl-glutaryl-coenzyme A reductase in a Chinese hamster cell mutant resistant to compactin (ML 236B).

1983 ◽  
Vol 8 (3) ◽  
pp. 309-312 ◽  
Author(s):  
Akinori Masuda ◽  
Michihiko Kuwano ◽  
Tatsuo Shimada
1982 ◽  
Vol 2 (11) ◽  
pp. 1354-1361 ◽  
Author(s):  
A Masuda ◽  
S Akiyama ◽  
M Kuwano

A fungal metabolite, ML236B (Compactin), isolated from Penicillium citrinum, is a specific inhibitor of 3-hydroxy-3-methylglutaryl (HMG)-coenzyme A reductase (EC 1.1.1.34). Three ML236B-resistant (ML236Br) mutants, MF-1, MF-2, and MF-3, were isolated from V79 after N-methyl-N'-nitro-N-nitrosoguanidine mutagenesis. The fluctuation test showed 2.2 X 10(-6) mutants per cell per generation of a spontaneous mutation frequency of ML236Br clones. These ML236Br clones showed a four- to fivefold-higher resistance to the drug than did their parental V79. Radioactive acetate, but not mevalonate, incorporation into the sterol fraction increased about 10-fold in ML236Br clones in comparison with that in V79. The cellular level of HMG-coenzyme A reductase in three ML236Br mutants was found to be a few-fold higher than that of V79 when cultured in the presence of lipoproteins. The 125I-labeled low-density lipoprotein-binding assay showed binding activity in three ML236Br clones comparable to that of the parental V79 cells. By contrast, an internalization assay of 125I-labeled low-density lipoprotein into the cells showed significantly reduced activity in three ML236Br clones in comparison with V79.


1982 ◽  
Vol 2 (11) ◽  
pp. 1354-1361
Author(s):  
A Masuda ◽  
S Akiyama ◽  
M Kuwano

A fungal metabolite, ML236B (Compactin), isolated from Penicillium citrinum, is a specific inhibitor of 3-hydroxy-3-methylglutaryl (HMG)-coenzyme A reductase (EC 1.1.1.34). Three ML236B-resistant (ML236Br) mutants, MF-1, MF-2, and MF-3, were isolated from V79 after N-methyl-N'-nitro-N-nitrosoguanidine mutagenesis. The fluctuation test showed 2.2 X 10(-6) mutants per cell per generation of a spontaneous mutation frequency of ML236Br clones. These ML236Br clones showed a four- to fivefold-higher resistance to the drug than did their parental V79. Radioactive acetate, but not mevalonate, incorporation into the sterol fraction increased about 10-fold in ML236Br clones in comparison with that in V79. The cellular level of HMG-coenzyme A reductase in three ML236Br mutants was found to be a few-fold higher than that of V79 when cultured in the presence of lipoproteins. The 125I-labeled low-density lipoprotein-binding assay showed binding activity in three ML236Br clones comparable to that of the parental V79 cells. By contrast, an internalization assay of 125I-labeled low-density lipoprotein into the cells showed significantly reduced activity in three ML236Br clones in comparison with V79.


Author(s):  
Wouter W. Wiegant ◽  
René M. Overmeer ◽  
Barbara C. Godthelp ◽  
Paul P.W. van Buul ◽  
Małgorzata Z. Zdzienicka

1988 ◽  
Vol 14 (6) ◽  
pp. 527-539 ◽  
Author(s):  
Dennis Peffley ◽  
Jon Miyake ◽  
Sherry Leonard ◽  
Charles Gunten ◽  
Michael Sinensky

1995 ◽  
Vol 337 (2) ◽  
pp. 119-129 ◽  
Author(s):  
Gerald W.C.T Verhaegh ◽  
Wim Jongmans ◽  
Bruno Morolli ◽  
Nicolaas G.J Jaspers ◽  
Govert P van der Schans ◽  
...  

FEBS Letters ◽  
1985 ◽  
Vol 186 (2) ◽  
pp. 219-223 ◽  
Author(s):  
Michael Sinensky ◽  
Judy Logel ◽  
Robin Schnitzer-Polokoff ◽  
Rae Ann Norcross

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