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Biomedical subjects

B Brenig

Publications and source records attributed to B Brenig.

At least 109 records · Page 6Linked to original sources
PubMed1997

[Maternal transmission or bovine spongiform encephalopathy in the case of "Cindy" disproved].

On December 27th, 1996 a Galloway cattle named "Cindy" died of bovine spongiform encephalopathy (BSE) in Höxter. So far all cases of BSE reported in Germany have been imported from the UK. However, the identity and origin of "Cindy" was not clear. DNA sequence analysis of the mitochondrial D-loop region and DNA typing of micro-satellite sites finally revealed that "Cindy" was imported from the UK as well.

Animals↗
PubMed1996

Regulation of tissue-specific expression of the skeletal muscle ryanodine receptor gene.

The ryanodine receptors (RYR) are a family of calcium release channels that are expressed in a variety of tissues. Three genes, i. e. ryr1, ryr2, and ryr3, have been identified coding for a skeletal muscle, cardiac muscle, and brain isoform, respectively. Although, the skeletal muscle isoform (RYR1) was shown to be expressed predominantly in skeletal muscle, expression was also detected in the esophagus and brain. To analyze the transcriptional regulation of the RYR1 gene, we have constructed chimeric genes composed of the upstream region of the RYR1 gene and the bacterial chloramphenicol acetyltransferase (CAT) gene and transiently transfected them into primary cultured porcine myoblasts, myotubes, and fibroblasts. A 443-base pair region upstream from the transcription start site was sufficient to direct CAT activity without tissue specificity. Deletion of a 61-base pair fragment from the 5'-end of the promoter resulted in a marked reduction of CAT activity in all three tissue types. A similar reduction of expression was observed when using a construct with the first intron in antisense orientation upstream from the promoter. In contrast, the first intron in sense orientation enhanced expression only in myotubes, while expression was repressed in fibroblasts and myoblasts. Gel retardation analyses showed DNA binding activity in nuclear extracts for two upstream DNA sequence elements. Our data suggest that (i) RYR1 gene expression is regulated by at least two novel transcription factors (designated RYREF-1 and RYREF-2), and (ii) tissue specificity results from a transcriptional repression in nonmuscle cells mediated by the first intron.

Amino Acid Sequence↗
PubMed1996

Mapping of the porcine urate oxidase and transforming growth factor beta 2 genes by fluorescence in situ hybridization.

We have mapped two genes from human chromosome 1, urate oxidase (UOX) and transforming growth factor beta 2 (TGFB2), by fluorescence in situ hybridization (FISH) in the pig genome. Porcine-specific polymerase chain reaction (PCR) primers for both genes were designed from the porcine cDNA sequence. With the help of these primers yeast artificial chromosome (YAC) clones for UOX and TGFB2 were isolated from a pig YAC library. These DNA probes were used for FISH analysis. TGFB2 was localized to SSC 10p16. With the YAC probe for UOX two porcine chromosome regions 6q26 and 6q32, revealed specific signals. These results, help to refine the comparative mapping data between human and pig.

Animals↗
PubMed1996

The porcine gene TBP10 encodes a protein homologous to the human tat-binding protein/26S protease subunit family.

We have cloned a porcine gene, designated TBP1O, that belongs to the Tat-binding protein/26S protease subunit family. The genomic structure of the porcine TBP1O gene was analyzed after isolation of three overlapping genomic phage lambda clones. The TBP10 gene harbors 12 exons spanning 4.5 kb of chromosomal DNA. The TBP1O gene was assigned to Chromosome (Chr) 12 by fluorescence in situ hybridization (FISH) on metaphase chromosomes. The chromosomal location was confirmed by PCR analysis of a porcine-rodent hybrid cell panel. The TBP1O protein is encoded by a 1221 nucleotide cDNA and has a molecular mass of 45.6 kDa. The predicted amino acid sequence has highest similarity to the human and bovine p45 subunit of the 26S protease and the human transcription factor TRIP1. Further similarities were detected to the slime mold protein DdTBP1O and the Schizosaccharomyces pombe and Saccharomyces cerevisiae protein SUG1. Like DdTBP1O and other members of the protein family, the porcine TBP1O harbors a leucine zipper motif in the N-terminal region and a domain characteristics of ATP-dependent proteases in the C-terminal region.

ATPases Associated with Diverse Cellular Activitie↗
PubMed1996

The porcine skeletal muscle ryanodine receptor gene structure coding region 1 to 10614 harbouring 71 exons.

The skeletal muscle ryanodine receptor (RYR1) belongs to a family of calcium release channels that are expressed in different tissues. The RYR1 gene is one of the largest genes characterized, so far, containing a 15253 nucleotide ORF in swine. To study the genomic organization of the porcine skeletal muscle ryanodine receptor gene we have isolated seven genomic fragments spanning 72.7 kb of chromosomal DNA of chromosome 6q12. This region harbours exons 1 to 71 coding for 3538 amino acids (69.6%) of the ryanodine receptor 1.

Amino Acid Sequence↗
PubMed1996

Mapping of type I loci from human chromosome 7 reveals segments of conserved synteny on pig chromosomes 3, 9, and 18.

We have mapped in the pig (Sus scrofa) the genes for zona pellucida glycoprotein 3 (ZP3), erythropoietin (EPO), and malate dehydrogenase 2 (MDH2) by somatic cell hybrid analysis in the pig genome. Previously, the gene for the T-cell receptor beta cluster (TCRB) was assigned to SSC 18 and that for interleukin 6 (IL6) to SSC 9. However, statistical analysis of mapping data for ZP3, EPO, and MDH2 did not discriminate between SSC 9 and SSC 3. Porcine-specific PCR primers for ZP3 and IL6 were used to isolate probes from porcine YAC libraries. These two genes were mapped by FISH to porcine chromosome regions 3pter --> p15 (ZP3) and 9q14 --> q15 (IL6). Comparative mapping considerations permit the tentative assignment of porcine EPO and MDH2 to 3pter --> p15.

Animals↗
PubMed1996

[225 years of the Veterinary Institute--modern research in historic buildings].

The institute of Veterinary Medicine is the oldest veterinary school of Germany and nowadays it is part of the agricultural faculty of the Georg-August-University of Goettingen. Because of shifts in the emphasis of research in veterinary science in the area of animal production and hygiene several structural changes have been made over the last few years. In this brief introduction latest developments at the institute of Veterinary Medicine are reviewed.

Animals↗
PubMed1996

[Structure and expression of the porcine skeletal muscle ryanodine receptor gene].

The ryanodine receptors (RYR) are a family of intracellular Ca2+ release channels that were first identified in the terminal cistenae of the sarcoplasmic reticulum of the skeletal and cardiac muscle. Mutations within the skeletal muscle isoform were shown to cause malignant hyperthermia in swine and man. We have analysed the genomic structure of the porcine skeletal muscle ryanodine receptor and its expression using chimeric reporter gene constructs consisting of the RYR1 gene promoter and the chloramphenicol acetyltransferase gene after transfection in muscle and non-muscle cells.

Animals↗
PubMed1996

[Proacrosin and acrosin--retrospect of a multifunctional complex].

Proacrosin is a molecule that is located under the acrosomal cap and that acts as a secondary ligand after acrosome reaction. Proacrosin is thought to bind to ZP2 (zona pellucida receptor 2). The high affinity is based on the interaction of the zona pellucida glycoprotein's acidic sulphate groups with basic, positively charged amino acids of the proacrosin molecule. Proacrosin is a serine protease and is capable to lyse the zona pellucida locally. Our structural analysis of proacrosin shows, that the catalytic centre is surrounded by loops containing positively charged amino acids which create the binding domain. This review is intended to describe the results that lead to the elucidation of the biochemistry of proacrosin.

Acrosin↗