Induction and depression of cytochrome P-450-dependent mixed-function oxidase by a cloned consensus alpha-interferon (IFN-alpha CON1) in the hamster.

A novel analogue of human alpha-interferon (IFN-alpha CON1) was tested for its ability to modify the hepatic cytochrome P-450-dependent mixed-function oxidase system in the hamster. This cloned interferon was derived by selecting the most frequently observed amino acid sequences at each position in the known human alpha-interferon subtypes. IFN-alpha CON1 had a biphasic effect on cytochrome P-450 and related drug biotransformation in the hamster causing an initial increase followed by a significant depression.

The role of three domains in the biological activity of human interferon-alpha.

Earlier studies showed that minor differences in primary structure among the interferon-alpha (IFN-alpha) protein family are reflected in their potency in selected biological assays. These studies have been extended and results from assays of antiviral, growth inhibitory and 2',5'-oligoadenylate (2-5A) synthetase activities indicate that the various novel hybrid and analog species are differentially biologically active. Overall these observations suggest a correlation between predicted secondary structure characteristics, receptor binding affinity, and 2-5A synthetase, antiviral and growth inhibitory activities.

The synthetic human growth hormone fragment (32-38) increases glucose uptake in the conscious dog.

hGH32-38 was tested to determine if the peptide could affect hepatic glucose production in the conscious dog under basal conditions (euglycemia) or if it could enhance glucose uptake when hyperglycemia was induced. hGH32-38 (1.6 nmol.

Structure/function studies on recombinant human gamma interferon.

Structure/function relationships for human gamma interferon (IFN-gamma) were investigated using recombinant DNA-derived homologues produced in E. coli. The various biological effects examined were antiviral, growth inhibitory and 2-5A synthetase activities, as well as receptor binding characteristics.

Cytoskeletal association of human alpha-interferon-receptor complexes in interferon-sensitive and -resistant lymphoblastoid cells.

Human Daudi lymphoblastoid cells, which are highly sensitive to the antiproliferative action of human leukocyte alpha-interferon (IFN-alpha), and IFN-resistant and IFN-sensitive Daudi subclones (Cl2 and Cl1, respectively), contain 2300 (Kd = 20 X 10(-12) M), 3000 (Kd = 45 X 10(-12) M), and 3700 (Kd = 52 X 10(-12) M) IFN-alpha binding sites per cell, respectively. Thus, these IFN-sensitive and IFN-resistant cells have similar numbers of high-affinity IFN-alpha receptors. IFN-receptor complexes that are insoluble in Triton X-100 accumulate in IFN-sensitive but not in IFN-resistant cells.