R. Foncea et al., CHANGES IN PROTEIN-KINASE-C ACTIVITY, SUBCELLULAR-DISTRIBUTION AND PROTEIN-PHOSPHORYLATION DURING THE LACTOGENIC CYCLE IN THE RAT MAMMARY TISSUE, Research communications in molecular pathology and pharmacology, 87(3), 1995, pp. 253-268
Direct and indirect evidence emphasizes the participation of classical
protein kinase C (cPKC) in the development and function of the mammar
y gland. This work shows that there are changes not only in total cPKC
activity during the lactogenic cycle, but also in the relative amount
s of the soluble and particulate cPKC activities and that the time-cou
rse of these two events are not the same. The time-course of transloca
tion from the cytoplasm to the plasma membrane suggests that the solub
le and particulate forms of the enzyme may be associated with growth a
nd differentiation of the tissue, respectively. Phosphorylation patter
ns also show characteristic and significant differences throughout the
development of the gland. These results suggest that both total mamma
ry cPKC activity and its subcellular forms change in accordance with t
he proliferative and differentiative stages of the mammary gland, and
that the enzyme translocation occurs during the transition from pregna
ncy to lactation.