Enolase, a cellular glycolytic enzyme, is required for efficient transcription of Sendai virus genome.

Cellular proteins (host factors) may play key roles in transcription of Sendai virus (SeV) genome. We have previously shown that the host factor activity, which stimulates in vitro mRNA synthesis of SeV, from bovine brain comprises at least three complementary factors, and two of them were identified as tubulin and phosphoglycerate kinase (PGK). Here the third host factor activity was further resolved into two complementary factors, and one of them was purified to an almost single polypeptide chain with an apparent M(r) of 52,000 (p52) and was identified as a glycolytic enzyme, enolase. Recombinant human alpha-enolase, as did p52, acted synergistically with other three host factors to stimulate SeV mRNA synthesis. West-Western blot analysis demonstrated that tubulin specifically binds enolase as well as PGK, suggesting that these two glycolytic enzymes regulate SeV transcription through their interactions with tubulin.

Prebeta1-high-density lipoprotein (prebeta1-HDL) concentration can change with low-density lipoprotein-cholesterol (LDL-C) concentration independent of cholesteryl ester transfer protein (CETP).

To clarify whether prebeta1-high-density lipoprotein (prebeta1-HDL) concentration changes with low-density lipoprotein-cholesterol (LDL-C) concentration independent of cholesteryl ester transfer protein (CETP), we determined prebeta1-HDL concentration by native two-dimensional gel electrophoresis in 58 subjects with normal triglyceride and HDL-cholesterol concentrations. We also measured LDL-C and CETP concentrations. In 17 subjects, a second blood sample was taken 1-6 months after the first. We found that prebeta1-HDL concentration was positively correlated with LDL-C concentration (r=0.529, P<0.0001) and with CETP mass (r=0.398, P<0.01). In 17 patients, Deltaprebeta1-HDL was positively correlated with DeltaLDL-C (r=0.635, P<0.01), but not with DeltaCETP mass (r=0.275). In conclusion, prebeta1-HDL concentration changes with LDL-C concentration independent of CETP. These results suggest that prebeta1-HDL concentration may reflect the balance between several regulatory factors, including LDL-C and CETP concentrations.

Serum amyloid A protein generates pre beta 1 high-density lipoprotein from alpha-migrating high-density lipoprotein.

Serum amyloid A protein (SAA), an acute-phase reactant in reactive amyloidosis, has high affinity for high-density lipoprotein (HDL). When SAA is added to HDL, SAA displaces apolipoprotein A-I (apoA-I) and phospholipid from the HDL particles. These dissociated components may form prebeta1-HDL because free apoA-I can associate with phospholipid to become a lipoprotein having prebeta mobility. To determine whether SAA generates prebeta1-HDL from alpha-migrating HDL, we investigated the effects of recombinant SAA on HDL subfraction concentration using nondenaturing two-dimensional gradient gel electrophoresis. When we added SAA (0.5 mg/mL) to plasma, the prebeta1-HDL concentration increased by 164% (from 4.7% +/- 1.3% to 12.4% +/- 3.2% of apoA-I, p < 0.005). The increase in prebeta1-HDL was proportional to the dose of SAA. When we added SAA to a column of Sepharose beads coupled to the isolated HDL (alpha-migrating HDL), prebeta1-HDL was dissociated from the column together with the SAA-associated HDL. In summary, we demonstrate that SAA generates prebeta1-HDL from alpha-migrating HDL. We speculate that SAA-mediated HDL remodeling may take place in inflammation.

Abnormality in plasma catecholamines and myocardial adrenoceptors in cardiomyopathic BIO 53.58 Syrian hamsters and improvement by metoprolol treatment.

The catecholaminergic neuronal activity and the densities of alpha-1 and beta adrenoceptors and angiotensin II receptors were simultaneously determined in BIO 53.58, a model of idiopathic dilated cardiomyopathy, and F1B control hamsters. Further, we examined the effect of repeated p.o. administration of metoprolol on these biochemical parameters. Compared with F1B control hamsters, there was a significant decrease in Bmax of specific binding of both (-)-[125I]iodocyanopindolol and [3H]prazosin with a marked elevation of plasma catecholamine (mainly norepinephrine and epinephrine) concentrations, in BIO 53.58 hamsters at 11 and 18 weeks of age (severe cardiomyopathic stage), but not at 5 weeks of age. On the other hand, the Bmax value of myocardial [125I]angiotensin II binding in BIO 53.58 hamsters was almost identical to that in F1B hamsters. These results suggest a development of down-regulation of myocardial beta and alpha-1 adrenoceptors because of an increased catecholaminergic neuronal activity with aging in BIO 53.58 hamsters. Repeated p.o. administration of a relatively low dose (1 mg/kg/day) of metoprolol for 7 weeks in 11-week-old BIO 53.58 hamsters caused a significant increase of myocardial (-)-[125I]iodocyanopindolol binding sites with a marked reduction in plasma catecholamine levels; this indicated a significant recovery to the F1B levels. The improvement of these biochemical parameters by metoprolol treatment was also accompanied by a significant decrease in the fibrosis in the heart in BIO 53.58 hamsters. These data suggest that catecholaminergic neurons and adrenoceptors play a part in the development of heart failure in idiopathic dilated cardiomyopathy. Consequently, the present study may provide a further pharmacological basis for the use of beta-1 adrenoceptor antagonists in patients with idiopathic dilated cardiomyopathy.