A decrease in the level of unscheduled DNA synthesis in preparations of irradiated rat hepatocyte nuclei under the effect of polyamines

The results obtained show the possibility of polyamine (spermine and spermidine) utilization to stabilize the nuclear chromatin and to protect it against nuclease degradation in the course of isolation of liver cell nuclei. Besides, the inhibition of the unscheduled DNA synthesis induced by nuclease incision and by gamma- or UV-radiation was demonstrated in the presence of polyamines.     

Interleukin-6 triggers the association of its receptor with a possible signal transducer, gp130

Interleukin-6 mediates pleiotropic functions in various types of cells through its specific receptor (IL-6-R), the cDNA of which has already been cloned. We report here that an 80 kd single polypeptide chain (IL-6-R) is involved in IL-6 binding and that IL-6 triggers the association of this receptor with a non-ligand-binding membrane glycoprotein, gp130. The association takes place at 37 degrees C within 5 min and is stable for at least 40 min in the presence of IL-6, but does not occur at 0 degree C. Human IL-6-R can associate with a murine gp130 homolog and is functional in murine cells. Mutant IL-6-R lacking the intracytoplasmic portion is functional, suggesting that the two polypeptide chains interact to involve their extracellular portion. In fact, a soluble IL-6-R lacking the transmembrane and intracytoplasmic domains can associate with gp130 in the presence of IL-6 and mediate its function. These findings indicate that the complex of IL-6 and IL-6-R can interact with a non-ligand-binding membrane glycoprotein, gp130, extracellularly and can provide the IL-6 signal.     

Antigenic similarity between cytoplasmic tetrodotoxin-sensitive protein and neuronal membrane proteins

Membrane proteins with a molecular weight of 290, 180, and 55 kDa were isolated using immunosorbent attached to sepharose and rabbit antibodies to cytoplasmic tetrodotoxin-sensitive protein from beef brain gray matter. A technique used for research into voltage-dependent sodium channels was applied to reconstruction of these proteins and investigation of toxin-dependent sodium flows through the lipoprotein membrane. Findings are interpreted as evidence of the similarity between cytoplasmic tetrodotoxin-sensitive protein and that of sodium channels at the cell membrane.A. A. Bogomolets Institute of Physiology, Academy of Sciences of the Ukrainian SSR, Kiev; A. V. Palladin Institute of Biochemistry, Academy of Sciences of the Ukrainian SSR, Kiev. Translated from Neirofiziologiya, Vol. 21, No. 4, pp. 485–489, July–August, 1989.     

Spread of fast thermowaves through the cerebral cortex produced by visual stimulation

Thermowaves spreading through the cerebral cortex were observed and investigated during acute experiments on white rats using a new technique — that of thermoencephaloscopy (TES) through the intact skull. These waves were induced by regular visual stimulation (at intervals of 1.5–3 min) or by initiating one of the flashes and spread through the cortex along trajectories of five basic types; amplitude of thermowaves: 0.005–0.1°C; length: 10–15 mm; duration 1.2–11.4 sec; velocity: 1–33 mm/sec; extent of pathway: 2–56 mm. They appeared with a high degree of probability (of 0.92) during the interval between 15 sec before and 26 sec after the flash. Numbers of moving waves declined by the point of stimulus application and rose by 7–8 sec after the flash. Waves arose in 50% of cases in the contralateral visual cortex (areas 17 and 18a), spreading to the midline and crossing to the ipsilateral hemisphere (areas 17, 18a, and 7). Local waves moving along a circular trajectory were also discovered in the contralateral visual cortex. Several types of wave, differing in trajectory, also arose in the ipsilateral visual cortex. Mechanisms and possible significance of this effect are examined.Institute of Higher Nervous Activity and Neurophysiology, Academy of Sciences of the USSR, Moscow. Translated from Neirofiziologiya, Vol. 21, No. 4, pp. 467–475, July–August, 1989.     

Interactions of three sequentially expressed genes control temporal and spatial specificity in Aspergillus development

Aspergillus nidulans brlA, abaA, and wetA form a dependent pathway that regulates asexual reproductive development. The order in which these genes are expressed determines the outcome of development. Expression of brlA in vegetative cells leads to activation of abaA and wetA, cessation of vegetative growth, cellular vacuolization, and spore formation. By contrast, expression of abaA in vegetative cells does not result in conidial differentiation but does lead to activation of brlA and wetA, cessation of vegetative growth, and accentuated cellular vacuolization. brlA, abaA, and wetA act individually and together to regulate their own expression and that of numerous other sporulation-specific genes. We propose that the central pathway controlling development is largely autoregulatory. The timing and extent of expression of the regulatory genes and their targets are determined as development proceeds by intrinsically controlled changes in the relative concentrations of regulatory gene products in the various conidiophore cell types.     

A restricted cytoplasmic region of IL-2 receptor beta chain is essential for growth signal transduction but not for ligand binding and internalization

The functional, high affinity form of interleukin-2 receptor (IL-2R) is composed of two receptor components, the IL-2R alpha (p55) and IL-2R beta (p70-75) chains. Unlike the IL-2R alpha chain, the IL-2R beta chain contains a large cytoplasmic domain that shows no obvious tyrosine kinase motif. In the present study, we report the establishment of a system in which the cDNA-directed human IL-2R beta allows growth signal transduction in a mouse pro-B cell line. This system enabled us to identify a unique region within the cytoplasmic domain of the human IL-2R beta chain essential for ligand-mediated signal transduction. We also demonstrate that certain cytoplasmic deletion mutants in the IL-2R beta chain, although deficient in signal transduction, can still form high affinity IL-2R in conjunction with endogenous mouse IL-2R alpha chain; the mutants are still able to internalize the ligand as well.