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Biomedical subjects

A Schweiger

Publications and source records attributed to A Schweiger.

At least 55 records · Page 3Linked to original sources
PubMed1989

Right hemisphere contribution to lexical access in an aphasic with deep dyslexia.

Three hemifield tachistoscopic studies of a right-handed patient with acquired Broca's aphasia and deep dyslexia, but with intact visual fields, are presented to support the hypothesis of right hemisphere (RH) participation in deep dyslexic reading. A systematic comparison of this deep dyslexic with the disconnected RHs of two patients with complete cerebral commissurotomy disclosed a similar, but not identical, pattern of abilities. The results demonstrate partial reliance on the RH for accessing the meaning of single words, but not for phonological encoding in this patient.

Adult↗
PubMed1986

Ultraviolet light-induced crosslinking of two major phosphoproteins and poly(A)+RNA from free polyribosomes; changes in phosphorylation by inhibitors of transcription and translation.

Polyribosomes were isolated without the use of detergents, irradiated with ultraviolet light and labelled in the presence of (gamma-32P) adenosine 5'-triphosphate. Poly(A)+RNA-protein structures separated by chromatography on oligo (dT)-cellulose contained up to 1o crosslinked proteins as shown by SDS-polyacrylamide gel electrophoresis. These included a 71 kDa poly(A)-bound species and two major phosphoproteins of 66 and 13o kDa. Pretreatment of rats with inhibitors of transcription and translation caused different and significant alterations in the labelling of the two phosphoproteins, suggesting that phosphorylation of proteins closely associated with mRNA may be involved in the regulation of the stability of this RNA or its binding to structural elements in the cell.

Amanitins↗
PubMed1985

Phosphoproteins crosslinked to poly(A) + heterogeneous nuclear RNA after irradiation with ultraviolet light.

Isolated liver nuclei or whole lymph node lymphocytes stimulated with concanavalin A in culture were irradiated with ultraviolet light. The crosslinked structures of poly(A)+ heterogeneous nuclear RNA and protein were purified on oligo(dT)-cellulose after labelling irradiated nuclei in the presence of adenosine 5'-[gamma-32P]triphosphate and analysed by SDS-polyacrylamide gel electrophoresis. The liver and lymphocyte nuclear proteins included about 17-19 species of 35-150 kDa and were shown to produce quite similar electrophoretic band patterns. Two proteins of 110-120 and 40-42 kDa were phosphorylated. Using partial proteolytic digestion the large-size crosslinked phosphoprotein has been identified as the 110 kDa component described previously (Schweiger, A. and Kostka, G. (1984) Biochim. Biophys. Acta 782, 262-268). The 40-42 kDa band was presumably related to the group C species of main proteins associated with heterogeneous nuclear RNA. In crosslinked nuclear structures from rats treated with low doses of alpha-amanitin for 1 h the relative amount of the 110-120 kDa phosphoprotein was reduced while the labelling with [32P]ATP was almost abolished.

Animals↗
PubMed1985

Biphasic increase in the in vivo phosphorylation of nuclear 110-kDa protein during early lymphocyte transformation.

A major 110-kDa phosphoprotein in rat liver and hepatoma (P 110) was identified in nuclear 0.2 M HCl extracts from rat lymph node cells. Stimulation with concanavalin A altered both the amount of P110 and, more strikingly, its in vivo phosphorylation in a typical biphasic manner with an initial maximum after 10-14 h. RNA synthesis showed a similar biphasic increase. Inhibition of hnRNA synthesis (5,6 dichlorobenzimidazoleriboside), but not of DNA synthesis (hydroxyurea), depressed both the amount of P110 and its phosphorylation markedly.

Animals↗
PubMed1985

Behavioural and electrodermal measures of lateralization for music perception in musicians and nonmusicians.

Two groups of students, musicians and nonmusicians were tested on a dichotic listening forced choice recognition task with concurrent recording of bilateral electrodermal activity. Stimuli were excerpts of Bach 4-part chorales; probes were the soprano, bass, harmony or the chorale excerpt, with or without changed notes. Laterality effects in recognition and the GSR were obtained only in musicians as a function of the complexity of the task. It was concluded that styles of information processing assumed by the hemispheres are the consequence of an interaction between the stimulus and the state of the organism at the moment, such that the direction of laterality can change within a subject performing the same task depending upon its perceptual demand.

Auditory Perception↗
PubMed1984

Concentration of particular high molecular mass phosphoproteins in rat liver nuclei and nuclear matrix decreases following inhibition of RNA synthesis by alpha-amanitin.

Purified liver nuclei were isolated from rats treated with non-lethal doses of alpha-amanitin, actinomycin D, galactosamine or cycloheximide. The nuclei were incubated in the presence of adenosine 5'-[gamma-32P]triphosphate, and digested with DNAase or DNAase plus high salt concentrations to prepare nuclear residual structures. Using SDS-polyacrylamide gel electrophoresis followed by autoradiography, samples from untreated rats were shown to contain major phosphoproteins in the range 76-260 kDa, with a prominent triplet of bands with 110, 117 and 128 kDa. Treatment of animals with alpha-amanitin or high doses of actinomycin D and galactosamine caused a significant decrease in the concentration of a few phosphorylated species, including the 110 kDa protein in whole nuclei, and their disappearance from the nuclear matrix or residual ribonucleoprotein structures after 1-3 h. The changes were reversible, complete recovery being observed after 5 h in the case of alpha-amanitin. No similar results were obtained with nuclei from rats treated with the translation inhibitor cycloheximide. The data are discussed in view of a possible effect of certain high molecular mass phosphoproteins on reactions of the heterogeneous nuclear RNA/mRNA pathway in the cell.

Amanitins↗
PubMed1984

Synthesis of 2',5'-oligoadenylate by rat liver nuclear matrix protein.

Nuclear matrix was prepared from unstimulated rat liver by treatment of nuclei with DNAse and 0.4 M NaCl and was further extracted with 2.0 M NaCl. Proteins were bound to poly(rI):(rC)-agarose, incubated with (alpha-32P) adenosine 5'-triphosphate and 2',5'-linked oligoadenylate was isolated from the supernatant. The substance inhibited amino acid incorporation in a reticulocyte translation system and was identified after enzymatic treatment followed by thin-layer chromatography on PEI-cellulose. The possible function of 2',5'-oligo(A) synthetase in the maturation of pre-mRNA associated with nuclear matrix is discussed.

Adenine Nucleotides↗
PubMed1983

High molecular mass phosphoproteins in the rat liver nuclear matrix identification of a prominent 110,000 Dalton species.

Purified rat liver nuclei were labelled in vitro in the presence of (32P) ATP and submitted to sequential extraction with DNAse, 0.4 or 2.0 M NaCl and Triton X-100. The residual or matrix structures contained 8-10 phosphoproteins between 76 and 260 kd including a triplet of major bands with 110, 117 and 128 kd. The 110 kd species was purified by chromatography on oligo(dT)-cellulose. It was shown to be identical with the 110 kd phosphoprotein of rat liver or Morris hepatoma free polyribosomes using the technique of limited digestion with S. aureus protease V 8.

Animals↗
PubMed1983

Nicotine gum in smoking cessation: a placebo-controlled, double-blind trial.

Sixty subjects were run in a study comparing the use of nicotine gum with placebo gum during cessation from smoking. Subjects were given clinic support and chewed the gum ad libitum. A survival analysis showed the two groups differed significantly in successful abstinence over time (p less than .03). Differences between groups appeared early (within weeks) and, at six months, a 28% superiority of nicotine over placebo gum was demonstrated with mean success rates of 48% and 20%, respectively. Between six months and one year, relapse in the nicotine group accounted for the 30% vs. 20% success rates for nicotine and placebo observed at one year. In a pilot study ("dispensary") testing the efficacy of the two gums when intervention was minimal, subjects in both groups resumed smoking within the first two weeks. The enhanced short-term success rates with nicotine gum in the clinic study are attributed to an effective interaction between use of the active preparation and clinic support. Long-term cessation may require extended maintenance procedures and/or an identification of optimal gum use.

Administration, Oral↗
PubMed1982

ADP-ribosylation of proteins associated with heterogeneous nuclear RNA in rat liver nuclei.

Purified rat liver nuclei were incubated in vitro in the presence of [adenylate-32P]nicotinamide adenine dinucleotide. The label was rapidly incorporated into trichloroacetic acid-insoluble material and also detected in particles carrying heterogeneous nuclear RNA. The particles were isolated by density gradient centrifugation, and their size determined to be 30-40 S from parallel experiments using nuclei labelled with [3H]uridine 5'-triphosphate under similar conditions. Treatment of the 30-40 S-particles with enzymes of different specificities showed that the label was tightly bound to proteins, not incorporated into nuclei acids and not utilized in phosphorylation of proteins. The label was detached by phosphodiesterase I from snake venom and identified as ADP-ribose and adenosine 5'-phosphate present at a ratio of 7.5 to 1 using thin layer chromatography on poly(ethyleneimine)-cellulose. Radioactively labelled (ADP-ribosylated) proteins were visualized by autoradiography following SDS-polyacrylamide gel electrophoresis. They included several major species of the ribonucleoprotein with molecular weights of 36000, 39000 and 42000, and a limited number of high molecular weight polypeptides.

Adenosine Diphosphate↗
PubMed1981

Properties of a 110000 molecular weight protein in rat liver hnRNP particles.

Particles carrying heterogeneous nuclear RNA (30--40 S-particles) were isolated from rat liver nuclei and the particle proteins separated by sodium dodecylsulfate gel electrophoresis. Some properties of a 110000 molecular weight component (P 110/103) were studied in detail: (i) P 110/103 was labeled to a 4-5 times higher specific activity than the major particle proteins in the presence of [14C]-amino acids in vivo. (ii) In nuclei incubated with [3H]- or [32P]-nicotinamide adenine dinucleotide P 110/103 was labeled presumably by ADP-ribosylation. (iii) A protein with the same molecular weight as P 110/103 and isolated from the nuclear extract by affinity chromatography was phosphorylated in vitro.

Amino Acids↗
PubMed1980

Composition of hnRNA-associated proteins in rat liver is specifically altered after cycloheximide treatment.

Rats were treated with non-lethal doses of alpha-amanitin or cycloheximide. Nuclei were prepared and the particles carrying heterogeneous nuclear RNA (30--40 S-particles) isolated by density gradient centrifugation. In the case of alpha-amanitin the yield of particles was reduced to about 45%. Cycloheximide affected the composition of proteins associated with the nuclear RNA. In particular, the concentration of a 110 000 molecular weight protein as determined by sodium dodecylsulfate gel electrophoresis was reduced to 20--30% after 2 h and then increased to 150--180% of the control before it approached the normal level after 30 h. Possible mechanisms underlying these changes are discussed.

Amanitins↗
PubMed1977

Preparation in undenatured form of the main protein bound to heterogeneous nuclear RNA in liver and hepatoma cells.

Particles carrying heterogeneous nuclear RNA (30 S-particles) were prepared from rat liver and Zajdela hepatoma ascites cell nuclei after ultrasonic disruption. The ribonucleoprotein structures were disintegrated in the presence of 100mM spermidine. Using chromatography on Sepharose-polyadenylate a protein component has been obtained which possessed high affinity for heterogeneous nuclear RNA, polyuridylate and polyadenylate, and double-stranded DNA. This protein was the main species of the ribonucleoprotein studied; it showed bands with molcular weights of 37000 and 40000 respectively in SDS gel electrophoresis. The RNA-binding proteins isolated from liver and hepatoma had identical molecular weights and the same affinity for Sepharose-polyadenylate used in the isolation.

Animals↗