Modification of protein kinase pattern in human placentae during gestation.

The cAMP-dependent and cAMP-independent histone kinases have been studied in the two subcellular compartments (cytosol and particulate fraction) from placentae of different gestational age. The total protein kinase activity, as well as its distribution between the two compartments, changes during the period of gestation. The total activity is significantly increased in full-term placentae. The increase is much greater for the cAMP-dependent (400 per cent), than for the cAMP-independent (270 per cent) protein kinases. It is much higher (400 per cent) in the cytosol than in the particulate fraction (170 per cent); consequently, the particulate fraction of term placentae shows a relatively lower proportion of protein kinase activity (26 per cent of the total activity) than the corresponding fraction of young placentae (37 per cent). DEAE-cellulose chromatography revealed the presence of two cAMP-dependent protein kinase peaks which correspond to Type I and Type II isoenzymes described in many mammalian tissues (Corbin, Keely and Park, 1975). The Type II isoenzyme is predominant in both first- and third-trimester placentae. The increase in protein kinase activity in term placentae is due to the selective activation of the Type II kinase only. The activity of the Type I isoenzyme remained unchanged throughout the period of gestation. The third peak eluted from the DEAE-cellulose column corresponds to a cAMP-independent sucrose-gradient ultracentrifugation into two distinct peaks similar to those already observed in several rat tissues (Toru-Delbauffe, Ohayon and Pavlovic-Hournac, 1983). The protein kinase patterns of both young and term placentae remain stable during the incubation of the tissues 'in vitro' for three hours.