[CBP35-CBP67 interaction in stress response and aging].

Abstract

Three carbohydrate-binding proteins with relative molecular masses of 35, 67, and 70 kDa (CBP35, CBP67, and CBP70) have been described to be present in nuclei of mammalian cells, where they are associated with nuclear ribonucleoprotein (RNP) complexes. CBP35 consists of two domains, an N-terminal domain that is homologous to certain regions of proteins of the heterogeneous nuclear RNP complex, and a C-terminal domain that is homologous to beta-galactoside-specific lectins. CBP35 has been proposed, like the glucose-specific lectin, CBP67, to guide RNP complexes through the nuclear pore. Here, we show that exposition of mature rats (6-8 months old) to stress results in binding of nuclear CBP35 to CBP67 which is retained on a column containing immobilized glucose. In contrast to mature animals, nuclear extracts from the livers of old rats (22-24 months old) displayed no detectable stress response.