Investigations on myelinogenesis in vitro: Regulation of 5?-nucleotidase activity by thyroid hormone in cultures of dissociated cells from embryonic mouse brain

1984 ◽  
Vol 11 (3) ◽  
pp. 263-270 ◽  
Author(s):  
G. Shanker ◽  
G. S. Rao ◽  
R. A. Pieringer
Keyword(s):  
Thyroid Hormone ◽  
Mouse Brain ◽  
Nucleotidase Activity ◽  
Embryonic Mouse ◽  
Dissociated Cells

Investigations on myelinogenesis in vitro: II. The occurrence and regulation of protein kinases by thyroid hormone in primary cultures of cells dissociated from embryonic mouse brain

1987 ◽  
Vol 7 (2) ◽  
pp. 159-165 ◽  
Author(s):  
G. Shanker ◽  
R. A. Pieringer
Keyword(s):  
Thyroid Hormone ◽  
Protein Kinase ◽  
Protein Kinases ◽  
Mouse Brain ◽  
Primary Cultures ◽  
Calf Serum ◽  
Phosphatidyl Serine ◽  
Protein Kinase Activity ◽  
Embryonic Mouse

The occurrence and regulation by thyroid hormone of four protein kinases (cyclic AMP independent and dependent, calcium/calmodulin stimulated, and calcium/phosphatidyl serine stimulated protein kinases) was studied in primary cultures of cells dissociated from embryonic mouse brain. Serum from a thyroidectomized calf, which contained low levels of L-3,5,3′-triiodothyronine, T3 (<25 ng/100 ml), and thyroxine, T4 (<1 μg/100 ml) was used in the culture medium in place of normal calf-serum (T3, 130 ng/100 ml; T4 5.9 μg/100 ml) to render the cultures responsive to exogenously added T3. Cultures grown in hypothyroid calf-serum containing medium had less cAMP dependent and independent protein kinase activity than control cultures grown in normal calf-serum containing medium. However, this activity was restorable to a considerable degree if the cultures grown in hypothyroid calf serum containing medium were supplemented with L-3,5,3′-triiodothyronine (T3). The presence of calcium/calmodulin stimulated protein kinase was also distinctly observed. In comparison, the activity of calcium/phosphatidyl serine stimulated protein kinase was less than the other protein kinases.

scholarly journals Studies on the expression of the microtubule-associated protein, tau, during mouse brain development, with newly isolated complementary DNA probes.

1984 ◽  
Vol 98 (3) ◽  
pp. 1090-1097 ◽  
Author(s):  
D G Drubin ◽  
D Caput ◽  
M W Kirschner
Keyword(s):  
Brain Development ◽  
Mouse Brain ◽  
Tau Protein ◽  
Bovine Brain ◽  
In Vitro Translation ◽  
Embryonic Mouse ◽  
Complementary Dna ◽  
Mouse Brain Development

Tau protein is a collection of closely related polypeptides that associate with microtubules in vivo and stimulate their assembly in vitro. Using an affinity-purified antiserum against bovine brain tau protein, we found that the number and amount of tau polypeptides changes dramatically during mouse brain development. The different forms appear to result from changes in tau mRNA since in vitro translation products reflect the qualitative and quantitative changes found in vivo. To study the mRNA and genomic complexity of tau protein, we used tau mRNA, purified from polysomes with tau antiserum, to isolate embryonic mouse tau complementary DNA clones. With these probes we have determined that embryonic tau protein is translated from a 6-kb mRNA that persists throughout brain development.

scholarly journals Influence of thyroid hormone on the in vitro translational activity of specific mRNAs in the rat heart.

1983 ◽  
Vol 258 (12) ◽  
pp. 7738-7745 ◽  
Author(s):  
W H Dillmann ◽  
A Barrieux ◽  
W E Neeley ◽  
P Contreras
Keyword(s):  
Thyroid Hormone ◽  
Rat Heart ◽  
Translational Activity ◽  
Specific Mrnas
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