scholarly journals Destruction of Mouse Skin Sebaceous Glands by Actinomycin D*

1967 ◽  
Vol 49 (3) ◽  
pp. 309-313 ◽  
Author(s):  
Motoo Hozumi ◽  
Fred G. Bock
1991 ◽  
Vol 275 (2) ◽  
pp. 459-467 ◽  
Author(s):  
A Maschio ◽  
P M Brickell ◽  
D Kioussis ◽  
A L Mellor ◽  
D Katz ◽  
...  

We have generated transgenic mice carrying the entire guinea-pig alpha-lactalbumin gene. Lactating transgenic mice expressed high levels of correctly initiated and processed guinea-pig alpha-lactalbumin mRNA in the secretory epithelium of their mammary glands, and secreted guinea-pig alpha-lactalbumin in their milk. Transcripts were detectable after 7 days of pregnancy, indicating that the transgene was under correct hormonal control. Whereas no or negligible transcription was detectable in all other tissues tested, high levels of transcripts were found in the skin of lactating transgenic mice. Guinea-pig alpha-lactalbumin protein was undetectable in the skin, however. In situ hybridization analysis showed that expression was localized to the undifferentiated cells in the basal layer of the sebaceous glands. Further studies revealed high levels of endogenous beta-casein mRNA in normal lactating mouse skin, demonstrating that the transcription of milk protein genes in lactating mouse skin is a normal event, and is not peculiar to the transgene. This surprising finding highlights the developmental relationship of the mammary gland to other specialized structures of the skin, supports a role for epithelial-extracellular matrix interactions in the regulation of milk protein gene expression in vivo, and identifies the skin as a particularly accessible model system in which to study the regulation of milk protein gene expression. In addition, the guinea-pig alpha-lactalbumin gene will be a source of regulatory sequences with which to direct heterologous gene expression to the sebaceous glands of transgenic mice.


1965 ◽  
Vol 53 (6) ◽  
pp. 1353-1360 ◽  
Author(s):  
H. V. Gelboin ◽  
M. Klein ◽  
R. R. Bates

2016 ◽  
Vol 25 (3) ◽  
pp. 187-193 ◽  
Author(s):  
Yong Li ◽  
Stefan W. Stoll ◽  
Sahil Sekhon ◽  
Caroline Talsma ◽  
Maya I. Camhi ◽  
...  

Nature ◽  
1966 ◽  
Vol 210 (5035) ◽  
pp. 541-543 ◽  
Author(s):  
W. G. FLAMM ◽  
W. B. COUNTS ◽  
M. R. BANERJEE

Author(s):  
Awtar Krishan ◽  
Dora Hsu

Cells exposed to antitumor plant alkaloids, vinblastine and vincristine sulfate have large proteinacious crystals and complexes of ribosomes, helical polyribosomes and electron-dense granular material (ribosomal complexes) in their cytoplasm, Binding of H3-colchicine by the in vivo crystals shows that they contain microtubular proteins. Association of ribosomal complexes with the crystals suggests that these structures may be interrelated.In the present study cultured human leukemic lymphoblasts (CCRF-CEM), were incubated with protein and RNA-synthesis inhibitors, p. fluorophenylalanine, puromycin, cycloheximide or actinomycin-D before the addition of crystal-inducing doses of vinblastine to the culture medium. None of these compounds could completely prevent the formation of the ribosomal complexes or the crystals. However, in cells pre-incubated with puromycin, cycloheximide, or actinomycin-D, a reduction in the number and size of the ribosomal complexes was seen. Large helical polyribosomes were absent in the ribosomal complexes of cells treated with puromycin, while in cells exposed to cycloheximide, there was an apparent reduction in the number of ribosomes associated with the ribosomal complexes (Fig. 2).


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