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Biomedical subjects

M Jacob

Publications and source records attributed to M Jacob.

At least 217 records · Page 12Linked to original sources
PubMed1981

The nuclear 5S RNAs from chicken, rat and man. U5 RNAs are encoded by multiple genes.

Preparations of chicken, rat and human nuclear 5S RNA contain two sets of molecules. The set with the lowest electrophoretic mobility (5Sa) contains RNAs identical or closely related to ribosomal 5S RNA from the corresponding animal species. In HeLa cells and rat brain, we only detected an RNA identical to the ribosomal 5S RNA. In hen brain and liver, we found other species differing by a limited number of substitutions. The results suggest that mutated 5S genes may be expressed differently according to the cell type. The set with the highest mobility corresponds to U5 RNA. In both rat brain and HeLa cells, U5 RNA was found to be composed of 4 and 5 different molecules respectively (U5A, U5B1-4) differing by a small number of substitutions or insertions. In hen brain, no U5B was detected but U5A' differing from U5A by the absence of the 3'-terminal adenosine. All the U5 RNAs contain the same set of modified nucleotides. They also have the same secondary structure which consists of two hairpins joined together by a 17 nucleotide long single-stranded region. The 3' half of the molecule has a compact conformation. Together, the results suggest that U5 RNAs are transcribed from a multigene family and that mutated genes may be expressed as far as secondary structure is conserved. The conformation of U5 RNA is likely to be related to its function and it is of interest to mention that several similarities of structure are found between U5 and U1A RNA.

Animals↗
PubMed1981

The conformation of chicken, rat and human U1A RNAs in solution.

Chicken, rat and human U1A RNAs in solution, were examined for secondary structure, using several methods including hydrolysis by various nucleases, hybridization to DNA oligomers and analysis of fragment interactions. The experimental results showed that the three U1A RNAs have the same structure, stable over a wide range of pH and ionic conditions. They allowed the selection of one out of several possible models constructed from the data of primary structure. This model is characterized by 4 hairpins and two single-stranded regions, the two hairpins from the 3' part of the molecule bearing very stable stems. In addition, the experimental results showed that in contrast to the 5' half of the molecule, the 3' half has a compact conformation probably stabilized by tertiary interactions. The 5' end of U1A RNA is accessible and free of base-pairing so that it might base-pair with regions of other RNA molecules, for instance, with the extremities of introns as has been recently proposed in a model of splicing.

Animals↗
PubMed1981

The status of small nuclear RNA in the ribonucleoprotein fibrils containing heterogeneous nuclear RNA.

hnRNP are made of two classes of unit, monoparticles and heterogeneous complexes. The monoparticles are much more easily dissociated by salt than the heterogeneous complexes. We made use of this differential salt sensitivity to determine the localization of snRNA in hnRNP. 1, About 50% of the snRNA were released by NaCl under the conditions of dissociation of monoparticles, U1 RNA which was enriched in monoparticles was preferentially released. 2, When the proteins resistant to salt dissociation were digested with proteinase K, an additional small proportion of snRNA was released, in particular a species designated 5 Sa RNA. Therefore, 5 Sa RNA seems to be preferentially associated with the proteins of heterogeneous complexes. 3, 40% of the snRNA remained associated with the hnRNA in the absence of any detectable protein. U1 and U2 RNA were the major RNAs in this fraction. The same RNA pattern was obtained for phenol-extracted RNA. The results indicate that all snRNA species are associated with the proteins of monoparticles, with those of heterogeneous complexes and with hnRNA. The existence of these pools of snRNA may reflect different functional states.

Animals↗
PubMed1981

Parkinsonism provoked by alcoholism.

Seven chronic alcoholics, aged 53 to 70, demonstrated transient signs of parkinsonism provoked by alcohol withdrawal or chronic severe intoxication. All showed improvement or recovery when they abstained or decreased their alcohol intake for several days to weeks. Animal studies have demonstrated impaired striatal dopaminergic function during severe ethanol intoxication or withdrawal. Chronic alcoholism apparently can exacerbate or uncover latent central dopaminergic deficiency.

Aged↗
PubMed1980

Nucleotide sequences of nuclear U1A RNAs from chicken, rat and man.

The methods of enzymatic and chemical treatment of end-labeled RNA were applied to the determination of the nucleotide sequence of chicken and man U1A RNA and to the reexamination of that of rat U1A RNA. The chemical method allowed the easy demonstration of the cap structure. All three RNA were 165 nucleotide long. Two hitherto non described modified pyrimidines were detected close to the 5' end. Only 9 base substitutions were observed from chicken to man indicating high degree of conservation of U1A RNA through evolution.

Animals↗
PubMed1980

Characterization of glycine-rich proteins from the ribonucleoproteins containing heterogeneous nuclear ribonucleic acid.

The salt-soluble 28 000-38 000-dalton proteins were isolated from ribonucleoproteins containing heterogeneous nuclear RNA and partially purified. They were glycine-rich proteins (22-26 mol/100) and contained a small amount of NG-dimethylarginine. Their N-terminal amino acid was blocked. Their pI was basic, extending from 6.95 to 9.20. Some 40 different polypeptides were demonstrated by combining molecular weight and pI determinations. Comparison of peptidic maps and of peptide size after trypsin and thermolysin digestion indicated the presence of only four proteins. The pattern of distribution of pI showing series of discrete major and minor bands common to two or three polypeptides of different apparent molecular weight was also compatible with the existence of four proteins and in addition supported the idea that the multiplicity of polypeptides was due to extensive posttranslational modifications.

Arginine↗
PubMed1980

Comparison of the nuclear ribonucleoproteins containing the transcripts of adenovirus-2 and HeLa cell dna.

A method as devised allowing the preparation of hnRNA-containing ribonucleproteins (hnRNP) frm HeLa cells infected with adenovirus type 2 under conditions where the extraction of viral replication complexes as minimal. Approximately 60% of the RNA from such hnRNP hybridized with adenovirus DNA. The hnRNP from infected cells had the same general characteristics as those from uninfected cells. Their size was heterogeneous (30-260 S) and depended upon that of their RNA. Their CsCl densities were identical (1.39-1.40 g/ml), indicating the same protein:RNA ratio. Their proteins were found in the same molecular weight range, between 25 000 and 200 000. The major proteins of hnRNP from HeLa cells were present in hnRNP from adenovirus-infected cells. As 60% of the cellular RNA was replaced by adenovirus RNA in hnRNP, this in dicated that there was not stringent specificity in the RNA-protein interactions. The relative proportions of the proteins were identifical in both cases, suggesting that the hnRNP assembly was independent of nucleotide sequences at least for the major proteins. The hnRNP from infected and uninfected cells differed by the size of their RNA, which was larger after infection, and by the presence of six additional minor polypeptides after infection. However, it cannot be excluded that the presence of these polypeptides in hnRNP resulted from non-specific adsorption.

Adenoviruses, Human↗
PubMed1980

[Skeletal lesions in chronic antero-medical instability of the knee (author's transl)].

The authors have operated on 110 cases of chronic antero-medial instability of the knee. In 33 cases there were femoral and tibial lesions. The medial tibial plateau was eroded at its posterior border with, at times, microfractures at this level or at the level of the posterior and axial part of the medial femoral condyle. This can be explained by abnormal movements of lateral rotation and translation of the posterior border of the medial tibial plateau which becomes subluxated under the femoral condyle. In 14 cases, periosteal elevation of the posterior capsule from the posterior border of the medial tibial plateau was found. The authors consider that this type of lesion may explain secondary degenerative lesions of the patella.

Adolescent↗
PubMed1979

Differentiating abilities of avian somatopleural mesoderm.

Quail-to-chick grafting experiments were performed on 2-day embryos in order to test the differentiating abilities of the somatopleure. After orthotopic and heterotopic transplatations of different parts of quail somatopleural mesoderm into chick embryos it is demonstrated that avian somatopleural cells differentiate into skeletal elements, smooth muscles, tendons and connective tissues. However, skeletal muscle fibres do not originate from somatopleural cells.

Animals↗
PubMed1979

Fractionation of constituents of ribonucleoproteins containing heterogeneous nuclear ribonucleic acid.

A method of fractionation of hnRNP constituents adaptable to large-scale preparation is presented. It is based on differential resistance to salt dissociation of the two classes of units of hnRNP, the 30--50S monoparticles and the heterogeneous complexes. The monoparticle proteins were released from hnRNP by 0.4 M NaCl. They were separated from the salt-resistant RNP corresponding to the heterogeneous complexes in three steps: chromatography on DEAE-cellulose, high-speed centrifugation, and Bio-Gel chromatography. The latter chromatography permitted a first fractionation of monoparticle proteins according to molecular weight. Such fractions may serve for purification of individual proteins of molecular weight below 80 000. After the two first steps, two fractions of salt-resistant RNP were obtained. In addition to heterogeneous RNA up to 30 S, small nuclear RNAs were detected which represented 6% of total RNA. The protein pattern was complex, and no clear-cut segregation of groups of proteins could be observed between the two fractions. They were both highly enriched in phosphoproteins as compared to nomoparticle proteins. In another fraction corresponding to the void volume of Bio-Gel chromatography, one-third of the RNA was small nuclear RNA. It is suggested that this fraction contains snRNP in addition to free proteins of molecular weight above 80 000 and to salt-resistant RNP similar to those described above but of small size.

Animals↗