A synaptic modification algorithm in consideration of the generation of rhythmic oscillation in a ring neural network

In consideration of the generation of bursts of nerve impulses (that is, rhythmic oscillation in impulse density) in the ring neural network, a synaptic modification algorithm is newly proposed. Rhythmic oscillation generally occurs in the regular ring network with feedback inhibition and in fact such signals can be observed in the real nervous system. Since, however, various additional connections can cause a disturbance which easily extinguishes the rhythmic oscillation in the network, some function for maintaining the rhythmic oscillation is to be expected to exist in the synapses if such signals play an important part in the nervous system. Our preliminary investigation into the rhythmic oscillation in the regular ring network has led to the selection of the parameters, that is, the average membrane potential (AMP) and the average impulse density (AID) in the synaptic modification algorithm, where the decrease of synaptic strength is supposed to be essential. This synaptic modification algorithm using AMP and AID enables both the rhythmic oscillation and the non-oscillatory state to be dealt with in the algorithm without distinction. Simulation demonstrates cases in which the algorithm catches and holds the rhythmic oscillation in the disturbed ring network where the rhythmic oscillation was previously extinguished.     

Separation of newly-synthesized RNA by organomercurial agarose affinity chromatography.

Mouse myeloma cells, MOPC-31C, were incubated in the presence of 2-thiouridine and newly-synthesized RNA which appeared to contain 2-thioUMP as a constituent was separated from preexisting RNA by affinity chromatography using organomercurial agarose as a support. Both pH and salt concentration greatly affected the specific adsorption of the newly-synthesized RNA on the column. Under optimal conditions the rate of adsorption of the newly-synthesized RNA on the column was proportional to the logarithmic concentration of 2-thiouridine in the culture medium. Furthermore, at a given concentration of 2-thiouridine in the medium, a shorter incubation period caused a reduction of the rate of RNA adsorption on the column. The molecular size distributions of both total RNA and the adsorbed fraction, synthesized during 30 min in the presence of 2-thiouridine, were similar to that of RNA synthesized in the absence of the drug.     

Purification of immunoglobulin heavy chain messenger RNA by immunoprecipitation from the mouse myeloma tumor, MOPC-31C.

Immunoglobulin heavy chain mRNA was purified from immunoprecipitated polysomes derived from the mouse myeloma tumor, MOPC-31C. The purified mRNA migrated predominantly as a single band upon polyacrylamide gel electrophoresis in 98% formamide and the molecular weight of this mRNA was calculated to be 700,000. This mRNA was as active as the purified light chain mRNA when it was employed as a template in a cell-free protein synthesizing system from wheat germ. The translation product had a molecular weight of 55,000 daltons, and migrated slightly faster than mature heavy chain upon polyacrylamide gel electrophoresis in sodium dodecylsulfate. The protein synthesized by the direction of this mRNA was shown to yield tryptic peptides corresponding to those derived from the mature heavy chain protein except that one missing peptide was replaced by another additional peptide. DNA complementary to the mRNA was synthesized by RNA-dependent DNA polymerase from avian myeloblastosis virus. Hybridization kinetic analysis between the heavy chain mRNA and its complementary DNA indicated that the RNA was essentially homogenous with rabbit globin mRNA as a standard.     

THE EFFECT OF ISCHAEMIA AND RECIRCULATION ON PROTEIN SYNTHESIS IN THE RAT BRAIN

Abstract— Rats were subjected to cerebral compression ischaemia for 15min and were subsequently recirculated with blood for periods up to 3 h. In vivo incorporation of intravenously administered L-[1–¹⁴C]valine into total brain proteins was found to be severely inhibited (about 20% of controls) after 45 min of recirculation. After 3 h, protein synthesis had increased, the specific radioactivity of proteins then being about 40% of controls. The post-ischaemic inhibition of protein synthesis was accompanied by a breakdown in polyribosomes and a concomitant increase in ribosomal subunits. In vitro incorporation of L-[1–¹⁴C]phenylalanine by a postmitochondrial supernatant system derived from animals subjected to 15 min ischaemia and 15 min recirculation was also severely reduced and showed, in contrast to control animals, no response to the addition of a specific inhibitor of polypeptide chain initiation (Poly(I)). Together with the in vivo accumulation of ribosomal subunits this indicates a block in peptide chain initiation during the early stages of recirculation.
Polyribosomes from animals subjected to 15 min ischaemia without recirculation showed a normal rate of in vitro protein synthesis which was inhibited by Poly(I) to a similar extent as polyribosomes from control animals. These results suggest that the post-ischaemic inhibition in chain initiation develops during the early stages of recirculation rather than during the ischaemic period itself.     

Studies of the fine structure of β-d-glucans of barleys extracted at different temperatures

Enzymic analyses of aqueous extracts of barley obtained at 25–100° demonstrated an exponential relationship between β-d-glucan content and temperature. Purified β-d-glucans, in particular those from extracts made at 40° and 100°, were compared by the Smith-degradation method followed by g.l.c. analysis of the methyl and the trimethylsilyl ethers of the products. All extracts yielded qualitatively the same products, including oligosaccharides which were characteristic of sequences of adjacent (1→3)-linkages. The material extracted at 100° contained relatively more of these sequences, and also showed a much higher specific viscosity, than did the material extracted at low temperatures. The structural implications of these findings are discussed.     

A case of renin producing leiomyosarcoma originating in the lung.

A 54-year-old woman was referred to our hospital for the treatment of a tumor of the right chest wall. Clinical examination revealed hypertension, hypokalemia, metabolic alkalosis, hyperaldosteronism and hyperreninemia. Computed tomography and an abdominal echogram indicated a tumor in the right phrenic area and two tumors in the retroperitoneum near the pancreas head. After the surgical resection of these tumors, the primary reninism was diminished. The pathological diagnosis of these tumors was leiomyosarcoma. Plasma active and inactive (trypsin-activated) renin activities (PRA) were 85.7 and 38.9 ng angiotensin I/ml/h, respectively. These PRA did not respond to either postural stimulation or suppression by the volume expansion. Active and inactive renin activities in a right phrenic area tumor were 208 and 32 ng angiotensin I/mg protein /h, respectively. Those of an abdominal tumor were 196 and 30 ng angiotensin I/mg protein/h, respectively. Renin mRNA identical in molecular size to that of the human kidney was identified by northern blot analysis. This is the first case report of renin producing leiomyosarcoma derived from the lung, which is characterized by relatively lower plasma prorenin concentrations.     

Identification and characterization of the cis-elements regulating the rat AMOG (adhesion molecule on glia)/Na,K-ATPase beta 2 subunit gene.

We have identified a positive regulatory cis-acting element of the adhesion molecule on glia (AMOG)/Na,K-ATPase beta 2 subunit gene as GAGGCGGGG at position -87 to -79 by transient transfection assay using B103 cells (rat neuroblastoma cell line). The newly identified AMOG regulatory element (AMRE) enhanced the promoter activity in a mutually compensating manner with the Sp1 element at position -147 to -142. AMRE acts as a positive regulatory element not only in B103 cells but also in 3Y1 (rat embryo cell line) cells to roughly the same extent and in MDCK (canine kidney cell line) cells to a lesser extent. AMRE also enhances other gene promoters, such as myelin basic protein (MBP) and herpes simplex virus (HSV) thymidine kinase (TK) gene promoters. The element is not a typical enhancer element because when it is introduced downstream of the HSV TK promoter, it has no enhancing activity.     

Structural organization and expression of the gene for bovine myosin I heavy chain.

Brush border myosin I heavy chain (MIHC), known previously as the brush border 110-kDa protein, contains an amino-terminal sequence which is highly homologous to the globular head domain of conventional myosin II heavy chain (MIIHC). The carboxyl-terminal sequence of MIHC completely diverges from that of MIIHC and functions as calmodulin-binding and membrane-interaction sites. In this investigation, we determined the structural organization of the bovine MIHC by isolating a set of genomic segments containing the whole MIHC gene. The bovine MIHC gene is 26 kilobase pairs long and consists of 28 exons. At the homologous amino-terminal portion of MIHC, many introns are located at positions equivalent to those of the rat MIIHC gene and the amoeba MIHC gene. At the carboxyl-terminal sequence of MIHC, the putative calmodulin-binding and membrane-interacting domains are specified by discrete sets of exons. These findings support the view that the amino-terminal head portions of MIHC and MIIHC evolved from a common ancestral origin and also that the MIHC protein was generated as a result of fusion of discrete genomic segments encoding different functional and structural protein domains. Analysis of tissue expression of the MIHC mRNA was also extended in this investigation, and the results indicated that this mRNA is expressed in some tissues other than the intestines.