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Biomedical subjects

H Busch

Publications and source records attributed to H Busch.

At least 109 records · Page 6Linked to original sources
PubMed1988

Pharmacotherapy of alcohol-withdrawal syndrome in hospitalised patients. Clinical and methodological aspects.

Because of the unreliability of the alcoholic, these suggestions are only intended for inpatients. Effective agents are presented first, and then the often very different pharmacological concepts are critically reviewed. Physicians use target symptoms as checkpoints for the effective pharmacological treatment of the alcohol-withdrawal syndrome. Clomethiazole and benzodiazepines are regarded as proven monotherapeutics against delirium. However, their somatic side effects and above all the problems of drug dependence make it necessary to look for a lower-risk medication. In every case, physicians must look more closely into the possibility of treating the individual alcohol-withdrawal syndrome with an agent less liable to cause addiction. Attractive, adequately tested alternatives are now becoming available for the large number of withdrawal syndromes which are below the level of delirium in terms of severity. This paper discusses the significance of substances without dependence potential, e.g. carbamazepine. This aspect is of special interest for the psychiatrist, whose task it is to guarantee the patient's abstinence after detoxification. We also look at other possible advantages of these substances when given in combination with drugs of the alcohol-barbiturate group against severe alcohol-withdrawal syndromes. Following a discussion of priority questions for further research, we draw attention to methodological deficiencies in earlier evaluation studies, and make suggestions for improved designs of drug trials.

Alcoholism↗
PubMed1987

Identification and partial characterization of a Mr 105,000 nucleolar antigen associated with cell proliferation.

This study reports the identification and partial characterization of a novel Mr 105,000 nucleolar antigen (P105) identified by a monoclonal antibody. This monoclonal antibody was obtained when a nucleolar protein extract separated from the immunodominant protein C23 was used as the immunogen. Nucleolar antigen P105 was not detected in normal (resting) human liver, kidney, or peripheral blood lymphocytes but was present in a variety of human malignant cells and tissues. Lymphocyte nucleoli also exhibited specific P105 staining after 72 h of phytohemagglutinin stimulation. Nucleolar antigen P105 was detected in growing and dividing HL 60 cells but was not detected in retinoic acid-induced differentiated HL 60 cells. When HeLa cells were made quiescent by 48 h of serum starvation, the P105 antigen was not detected, but after refeeding with serum-containing medium, the antigen P105 was detected in the HeLa nucleoli within 2 h. These results indicate that nucleolar antigen P105 is a proliferating cell nuclear and nucleolar antigen-like molecule which appears early in the G1-S phase of the cell cycle.

Animals↗
PubMed1987

Novel cell cycle-related nuclear proteins found in rat and human cells with monoclonal antibodies.

Monoclonal antibodies which react specifically with the nuclei of interphase cells recognized three nuclear antigens with molecular weights of 110,000 (p110), 85,000 (p85), and 18,000 (p18). p110 and p85 were found in eight tumor cell lines but were not found in resting lymphocytes. p18 was found in resting lymphocytes as well as the tumor cell lines. Protein p85 appeared in phytohemagglutinin-stimulated lymphocytes in the G1 phase and protein p110 appeared in the S phase. p110 and p85 were localized to the extranucleolar chromatin while p18 was distributed throughout the nucleus and was determined by microscopic and DNase digestion studies to be DNA associated. The anti-p110 antibody recognized a component of the DNA polymerase alpha 2 complex. Three novel nuclear proteins were identified using monoclonal antibodies. Two of these proteins (p110 and p85) are proliferating cell nuclear and nucleolar antigen-like while the third (p18) is not cell cycle dependent.

Animals↗
PubMed1987

Human U3 small nucleolar RNA genes are localized to the nucleoplasm.

U3 RNA, an abundant, conserved, capped, small RNA localized to the nucleolar compartment of eukaryotic cells, its implicated in the processing of pre-ribosomal RNA. The genes for U1 and U2 snRNAs (small nuclear RNAs) are clustered and present in the nucleoplasmic DNA; however, the localization of U3 snRNA genes is not known. DNAs, isolated from HeLa cell nuclei and nucleoli, were hybridized with labeled probes corresponding to the 5'-flanking and the coding regions of the human U3 snRNA gene. The intensity of signals obtained with both the probes were 5-6 fold greater in nuclear DNA, compared to nucleolar DNA. With ribosomal gene probe, the nucleolar DNA had sixfold more intense signal than nuclear DNA. These results indicate that genes for U3 snRNA are in the nucleoplasm. Therefore, U3 snRNA, like 5S ribosomal RNA, appears to be synthesized in the nucleoplasm and transported to the nucleolus.

Cell Compartmentation↗
PubMed1987

Identification and partial characterization of a Mr 40,000 nucleolar antigen associated with cell proliferation.

The present study reports the identification and partial characterization of a novel Mr 40,000 nucleolar antigen (P40) by monoclonal antibodies. Monoclonal antibodies to this protein were obtained when a nucleolar protein extract separated from the immunodominant protein C23 was used to immunize BALB/c mice; 12 hybridoma clones produced antibodies to this protein. P40 was not detected in normal human kidney, liver, and leukocytes but was readily demonstrable in a variety of human malignant tissues. This newly identified P40 antigen differs in its specific nucleolar localization from cyclin (proliferating cell nuclear antigen), a Mr 35,000 antigen which is largely in the nucleoplasm. In addition, cyclin appears in the nucleolus in S-phase; P40 appears in the nucleolus 6 h after refeeding serum-starved HeLa cells.

Animals↗
PubMed1987

Effect of differentiation on the expression of a nucleolar antigen with a molecular weight of 145,000 in HL-60 cells.

Mr 145,000 nucleolar protein antigen (p145) is associated with growing cells (R. L. Ochs et al., J. Cell Biol., 101: 211a, 1985) and has been found in a broad range of human cancers (J. W. Freeman et al., Cancer Res., 46: 3593-3598, 1986). In this study the presence of nucleolar antigen p145 was examined in the human promyelocytic tumor cell line HL-60 which was induced to differentiate by retinoic acid. Differentiation was monitored by morphological changes, [3H]thymidine accumulation, the ability of cells to reduce nitroblue tetrazolium, and cell number. The monoclonal antibody to nucleolar antigen p145 produced bright immunofluorescence in all cycling interphase HL-60 cells; during mitosis only diffuse staining was detected. Nucleolar antigen p145 in HL-60 cells was undetectable after 132 h of treatment with retinoic acid. The absence of nucleolar antigen p145 was associated with an 81% decline in thymidine accumulation and apparent inactivation of ribosomal and nonribosomal DNA transcription as observed by electron microscopy. The loss in expression of the antigen also correlated with increased nitroblue tetrazolium-positive cells, appearance of morphologically distinct myeloid cells, and termination of cell proliferation. These data indicate that the expression of nucleolar antigen p145 occurred in cycling HL-60 cells but not in terminally differentiated noncycling HL-60 cells.

Antibodies, Monoclonal↗
PubMed1987

Monoclonal autoantibody from a (New Zealand black x New Zealand white)F1 mouse and some human scleroderma sera target an Mr 34,000 nucleolar protein of the U3 RNP particle.

A monoclonal IgG2a antinucleolar autoantibody (72B9) was obtained by fusion of spleen cells from a (New Zealand black x New Zealand white)F1 mouse with myeloma cells (P3x63Ag8.653). Antibody 72B9 recognized a highly conserved nucleolar antigen present in both animal and plant cells. The staining pattern produced by antibody 72B9 in different cell substrates was identical with those obtained by scleroderma antibodies reactive with a basic (pI 8.5) nucleolar protein of Mr 34,000, which is associated with the U3 RNP particle. Western blotting further confirmed its reactivity with this scleroderma-related U3 RNP protein.

Animals↗
PubMed1987

Studies on satellite nucleoli in rat hepatocytes and Novikoff hepatoma cells.

The present study was undertaken to provide information on the presence and frequency of satellite nucleoli in cells with increased nucleolar biosynthetic activity. The number of hepatocytes containing satellite nucleoli was analyzed in rat liver, regenerating liver 18 h after partial hepatectomy and in Novikoff hepatoma ascites cells. In comparison with hepatocytes of normal liver, the number of both stimulated hepatocytes and malignant hepatoma cells containing satellite nucleoli was significantly reduced. The results also indicated that whereas most satellite nucleoli contain protein C23, a smaller percentage contain protein B23.

Animals↗
PubMed1987

Novel nucleolar antigens in autoimmune disease.

Antinucleolar antibodies are of interest in 2 important areas, namely, autoimmune diseases and specific products involved in the "mitogenic cascade." The former have delineated a series of novel nuclear and nucleolar elements including the recently described proliferating cell nuclear antigens (PCNA), some of which are present in the nucleolus only at specific times in the G1-S phase of the cell cycle. Important new proteins such as "fibrillarin" (34 kD/pI 8.5) and a 125 kD nucleotide containing protein have been identified with antinucleolar antibodies. Protein p145 is a nucleolar PCNA that is present in growing and dividing cells but not in normal resting tissues. Antinucleolar antibodies offer powerful tools, not only for identification of specific nucleolar proteins important in the cell cycle, but also for purification of their genes and analysis of mechanisms of gene control that operate the "time windows" of the cell cycle.

Amino Acid Sequence↗
PubMed1986

Amino acid sequence of a specific antigenic peptide of protein B23.

A specific antigenic peptide was obtained from protein B23 (Mr/pI = 37,000/5.1) after 30 min of digestion with staphylococcal V8 protease (10 micrograms/ml/mg protein B23). The antigenic peptide was purified by DEAE-cellulose chromatography and high pressure liquid chromatography on a reverse-phase C18 column. The antigenic peptide contains 14.7 and 18.7 mol% of glutamic acid and lysine, respectively. Amino acid sequence analysis showed that the peptide has 68 amino acids and is located on the carboxyl-terminal sequence of protein B23. The sequence is Ser-Phe-Lys-Lys-Gln-Glu-Lys-Thr-Pro-Lys-Thr-Pro- Lys-Gly-Pro-Ser-Ser-Val-Glu-Asp-Ile-Lys-Ala-Lys-Met-Gln-Ala-Ser-Ile-Glu- Lys-Gly- Gly-Ser-Leu-Pro-Lys-Val-Glu-Ala-Lys-Phe-Ile-Asn-Tyr-Val-Lys-Asn-Cys-Phe- Arg-Met- Thr-Asp-Gln-Glu-Ala-Ile-Gln-Asp-Leu-Trp-Gln-Trp-Arg-Lys-Ser-Leu-Cooh. Extensive digestion of the antigenic peptide with V8 protease, trypsin, or chymotrypsin results in loss of the antigenic activity. Three cloned cDNAs (hpB1, hpB2, and hpB7) which code for the 82 amino acids at the COOH terminus of protein B23 and the 3' non-translating sequence were identified and characterized. All three clones have identical nucleotide sequences coding for the antigenic portion of the protein (68 amino acids at the COOH terminus), the stop codon, and the 3' non-translated region. However, mutation of 6 nucleotide bases of one clone (hpB2) caused changes in 4 amino acids in the sequence just preceding the immunoreactive region. The result suggests the presence of at least 2 immunologically similar but distinct proteins which are both recognized by the anti-B23 antibody.

Amino Acid Sequence↗
PubMed1986

A 10S particle released from deoxyribonuclease-sensitive regions of HeLa cell nuclei contains the 86-kilodalton-70-kilodalton protein complex.

Digestion of HeLa cell nuclei with micrococcal nuclease or deoxyribonuclease I (DNase I) released the 86-kilodalton-70-kilodalton (kDa) protein complex in particles sedimenting at approximately 10 S in sucrose density gradients. Immunoaffinity-purified 32P-labeled complexes contained 86- and 70-kDa polypeptides with phosphorylated serine residues and DNA fragments, of which the largest was 110 base pairs long. Digestion of nick-translated nuclei with micrococcal nuclease released 32P-labeled 10S particles that were immunoaffinity-purified; they contained labeled 110-base-pair DNA fragments. The micrococcal nuclease digests were analyzed by two-dimensional electrophoresis, which separated nucleosomes in the first dimension and the associated proteins in the second. Western blots of the separated proteins showed that the 86-kDa-70-kDa complex was associated with the mono-, di-, and trinucleosomes. A more extensive electrophoretic separation revealed that the 10S particle from nick-translated nuclei migrated with a subfraction of the mononucleosomes that lacked H1 histones. These results suggest that the 10S particle which contains the 86-kDa-70-kDa complex is associated with an unfolded nucleosome that is present in DNase I sensitive regions.

Cell Nucleus↗
PubMed1986

Some gene variants for 5 S RNA are dispersed in the rat genome.

In the course of studies on genes for small nuclear RNAs, seven lambda phage clones containing sequences homologous to 5 S RNA were plaque purified from a rat genomic library. The seven clones were found to be from six different genomic loci. When the 5 S RNA hybridized to these clones was digested by T1 RNase, only clone 5S-2 protected the RNA completely. Moreover, clone 5S-2 which has five nucleotide substitutions in the internal control region was transcribed 10 times more efficiently than a bonafide Chinese hamster 5S gene. The other clones were less efficiently transcribed than a bonafide 5S gene or not transcribed at all. The number of gene variants for 5 S RNA in the rat genome was approximately 3000. In contrast to the clustering of 5S genes and gene variants found in Xenopus, Drosophila, hamster, mouse, and human cells, the 5S gene variants in the rat genome are dispersed and most contained conserved 3'-flanking sequences. These naturally occurring 5S gene variants may be useful in binding transcription factors that affect 5S genes.

Animals↗
PubMed1986

Multiple sequences in the Drosophila melanogaster U3 RNA gene are homologous to vertebrate U3 RNA.

We have cloned and sequenced a DNA fragment from the genome of Drosophila melanogaster which is homologous to Novikoff hepatoma (rat) small nucleolar U3 RNA. DNA sequence analysis shows that the regions of homology between the cloned DNA and rat U3 RNA are distributed over the entire length of the molecule and the total homology of linear sequence is 53%. The present finding supports the generalization that U3 RNA has been evolutionally conserved but diverges between mammals and invertebrates. This clone contains the upstream and downstream sequences required for the efficient and correct transcription of small nuclear RNAs. The secondary structure proposed for the U3 RNA sequence deduced from the cloned DNA is similar in general topography to that reported for rat U3 RNA (Bernstein et al., ref. 23).

Animals↗
PubMed1986

Isolation and characterization of two putative full-length Drosophila U4 small nuclear RNA genes.

U4 RNA is one of the abundant small nuclear RNAs implicated in the processing of the 3' -ends of premessenger RNAs (Berget, S. (1984) Nature 309, 179-182). Two potential U4 RNA genes were isolated from a Drosophila genomic DNA library and characterized. These genes, which were from different loci, had transcription and processing signals common to Drosophila U1 and U2 small nuclear RNA genes. One U4 gene locus also contained a downstream 5'-truncated U4 pseudogene. This is the first report in which putative full-length genes for U4 small nuclear RNA were isolated and characterized.

Animals↗
PubMed1986

Isolation and characterization of a human U3 small nucleolar RNA gene.

U3 RNA is an abundant, capped, small nucleolar RNA, implicated in the processing of preribosomal RNA. In this study, a DNA clone coding for U3 RNA (clone U3-1) was isolated from a human genomic library and characterized. The DNA sequence was identical to that of human U3 RNA isolated from HeLa cells. The flanking regions showed homology to the enhancer, promoter, and 3'-processing signal found in U1 and U2 snRNA genes. Further, the recently identified "U3 box" (GATTGGCTGCN10TATGTTAATTATGG) of rat U3 genes (Stroke and Weiner, (1985) J. Mol. Biol. 184, 183-193), was also found in the human U3 gene. This gene was transcribed in Xenopus oocytes; it is the first cloned true human U3 gene.

Base Sequence↗
PubMed1986

Amino acid sequence of protein B23 phosphorylation site.

A major phosphopeptide labeled in vivo, was identified in nucleolar protein B23 (Mr/pI = 37,000/5.1) after tryptic digestion. This peptide was purified by high performance liquid chromatography using reverse-phase (C8 and C18) columns. The phosphopeptide contains 20 amino acids including 1 phosphoserine, 7 glutamic acids, and 4 aspartic acids. The amino acid sequence is: His-Leu-Val-Ala-Val-Glu-Glu-Asp-Ala-Glu-Ser(P)-Glu-Asp-Glu-Asp- Glu-Glu-Asp-Val-Lys. This amino acid sequence is similar to that of nucleolar phosphoprotein C23 (8 consecutive amino acids were identical), and to the regulatory subunit (RII) of cAMP-dependent protein kinase (7 consecutive amino acids were identical, which is phosphorylated by casein kinase II (Carmichael, D.F., Geahlen, R.L., Allen, S.M., and Krebs, E.G. (1982) J. Biol. Chem 257, 10440-10445). The regions near these phosphorylation sites are enriched with glutamic and aspartic acids, suggesting that this acidic amino acid cluster may be essential for kinase recognition.

Amino Acid Sequence↗