HnRNP CBP35.CBP67 interaction during stress response and ageing.
Previous studies have demonstrated the existence of nuclear carbohydrate binding proteins in a variety of mammalian cells with molecular masses of 35,000, 67,000, and 70,000 (CBP35, CBP67, and CBP70), which are associated with nuclear ribonucleoprotein (RNP) complexes. CBP35 consists of two domains, an amino-terminal portion that is homologous to certain regions of proteins of the heterogeneous nuclear RNP complex, and a carboxyl-terminal portion homologous to beta-galactoside-specific lectins. CBP35 it has been proposed, like the glucose-specific lectin, CBP67, to guide RNP complexes through the nuclear pore. Here we show that the exposure of mature rats to stress induces an increase in nuclear CBP35 bound to CBP67 and retained on immobilized glucose. Nuclear extracts from the livers of old rats displayed no detectable stress response. This CBP35.CBP67 association detected in rat liver is considered with respect to the CBP35.CBP70 association recently observed in HL60 cell nuclear extracts.
Lauc
G
G
Institut für Physiologische Chemie, Abteilung für Angewandte Molekularbiologie, Mainz, Germany.
Seve
A P
AP
Hubert
J
J
Flögel-Mrsic
M
M
Müller
W E
WE
Schröder
H C
HC
D000375:Aging / Q000378:metabolism*; D000818:Animals; D000943:Antigens, Differentiation / Q000378:metabolism*; D037502:Galectin 3; D006801:Humans; D037102:Lectins / Q000378:metabolism*; D008297:Male; D008970:Molecular Weight; D009687:Nuclear Proteins / Q000378:metabolism*; D051381:Rats; D017208:Rats, Wistar; D012261:Ribonucleoproteins / Q000378:metabolism*; D013312:Stress, Physiological / Q000378:metabolism*
D000943:Antigens, Differentiation; D037502:Galectin 3; D037102:Lectins; D009687:Nuclear Proteins; D012261:Ribonucleoproteins