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Biomedical subjects

A Vokaer

Publications and source records attributed to A Vokaer.

31 records · Page 2Linked to original sources
PubMed1975

Cyclic AMP and cyclic GMP concentrations in serum- and density-restricted fibroblast cultures.

Mouse fibroblasts transformed by simian virus 40 (SV3T3 cells) are characterized by cyclic AMP and cyclic GMP levels, respectively, about half and twice those found in growing untransformed 3T3 cells. Density-dependent inhibition of growth is correlated with reduced cyclic GMP concentrations in 3T3 and four different density-restricted revertant lines derived from SV3T3. The levels of cyclic AMP are not increased at confluence. Upon serum restriction, serum-dependent cell lines show a greater increase in intracellular cAMP than serum-insensitive lines. Cyclic GMP levels are greatly reduced, even in serum-insensitive density revertants, but not in SV3T3. Serum readdition to all serum-dependent lines is followed by a rapid decrease in cyclic AMP and increase in cyclic GMP concentrations. The magnitude of these responses is decreased in SV3T3 and density revertants.

Animals↗
PubMed1975

[Viruses and mammary carcinogenesis].

Bittner virus has been extensively studied by recent electron microscopy and molecular biology techniques. The structure, the biochemical, physical and antigenic properties of the RNA tumor viruses - i.e. the mouse mammary tumor virus (MMTV) - are well known. Recent observations in human tissues of particles similar to animal viruses that are known to be oncogenic have raised the hypothesis of the role of viruses in human cancer. In mice, breast cancer can be caused by a virus - the Bittner virus or MMTV - that is usually transmitted from mother to offspring in the milk. The discovery of such virus particles in human milks and breast cancer tissues could provide data about a viral aetiology of human breast cancer.

Animals↗
PubMed1974

Phosphoprotein phosphatase activity associated with estrogen-induced protein in rat uterus.

Estrogen-induced protein was purified from rat uteri and assayed for several enzymatic activities involved in the metabolism and action of cyclic nucleotides. No adenylate and guanylate cyclase (EC 4.6.1.1 and 4.6.1.2, respectively), protein kinase (EC 2.7.1.33), and cyclic nucleotide binding activities could be demonstrated in three independent preparations of the protein. However, all three preparations exhibited significant phosphoprotein phosphatase activity (EC 3.1.3.16) on phosphorylated protamine and histones F1. This activity is optimal at neutral pH, inhibited by Zn(++), and unaffected by cyclic AMP or cyclic GMP.

Adenylyl Cyclases↗