Protein P1, which is a nuclear protein resembling high mobility group prote
ins, has been studied in human breast adenocarcinomas and compared to those
from control tissue. The presence of the protein was confirmed by in vitro
phosphorylation by casein kinase II and immunoblotting, using antibodies r
aised in rabbits against rat liver P1. The protein has been isolated by rev
erse phase HPLC chromatography which provides a more rapid method of purifi
cation requiring smaller amounts of material. The levels of P1 expression w
ere investigated and it was found that there was a three-fold increase in t
he ratio of P1/histone HI in normal breast tissue as compared to the neopla
stic tissue. In two other malignant and non-malignant tissues studied, the
level of P1 was also decreased in the malignant tissues. Thermolytic phosph
opeptides of P1 from normal and malignant human breast tissues exhibited th
e same pattern, though when compared to the phosphopeptide pattern from rat
tissue, differences were observed. (C) 2001 Elsevier Science Inc. All righ
ts reserved.