M Roghani — Page 2 | PubMed Health

PubMed1987

Benzene and toluene activate protein kinase C.

Protein kinase C plays a pivotal role in the transduction of signals controlling cell activation. A number of tumor promoters including phorbol esters activate the enzyme by substituting for diacylglycerol, the intracellular messenger of physiological ligands. In contrast, chloroform-induced protein kinase C activation does not appear to be mediated through the same mechanism. In vitro studies and experiments on intact platelets have revealed that benzene and toluene are also activators of protein kinase C. The data suggest that these drugs, which do not inhibit [3H]12-O-tetradecanoylphorbol-13-acetate binding to the enzyme, probably act in a chloroform-like manner.

Animals↗

PubMedDate not supplied

Oral administration of pectin-rich plant extract enhances C3 and C4 complement concentration in woman colostrum.

C3 and C4 components of the complement are normally present in human colostrum. These compounds are natural antibacterial agents. Pectin-rich plant extracts have been shown to induce prolactin release and milk synthesis when administered by the oral route in rat. In the present work, extract from a plant rich in pectin, Gossypium herbaceum was given orally to women 2 days after parturition. The extract enhanced concentration of C3 and C4 in colostrum but did not modify the total hemolytic complement activity (TCH50). No change in the concentration of the three compounds was observed in serum of the treated women. Control experiments showed that a treatment by placebo had no effect on colostrum composition. These data suggest that pectin-rich plant extracts favour transfer of C3 and C4 from blood to colostrum by an unknown mechanism. This observation suggests that some plant extracts might be used to reinforce the antibacterial activity of human colostrum.

Adult↗