Search PubMed⌕ Search

Biomedical subjects

G Reimer

Publications and source records attributed to G Reimer.

52 records · Page 3Linked to original sources
PubMed1978

Presence of two typical DNA-binding nonhistone proteins in psoriatic scales contrary to normal human dermis, epidermis and horny layer.

The composition of DNA-binding proteins (DBP) was shown to be tissue-specific and to vary at different stages of gene expression. As the accelerated epidermopoesis in psoriasis indicates changed gene activities, DBP of psoriatic scales were compared with those of normal human epidermis, dermis and horny layer. Each skin fraction is characterized by its own DBP pattern, indicating different cell species. 1. The DBP of normal human epidermis shows only a small accordance with the DBP of human dermis and implies their difference in origin, function and cell types. 2. Psoriatic scale DBP and epidermal DPB contain more corresponding proteins which can be deduced from the scale's origin from epidermis. However, the composition of all proteins differs to a great extent. This either occurred during parakeratotic keratinization or reflects differences of normal to psoriatic epidermis. Imposing for psoriatic scale DBP are two protein bands with molecular weights of 84,000 and 90,000 daltons. Evidently both are not present in the DBP of other skin layers. 3. The horny layer contains a very small amount of DBP which might represent DNases to a major part. The small DBP content in horny layer confirms the previous supposition of psoriatic scales, to be mostly derived from the preserved nuclei of the parakeratotic scale layer.

Chromosomal Proteins, Non-Histone↗
PubMed1978

DNA-binding proteins of psoriatic scales III. Biochemical characterisation as non-histone-proteins.

Histone and non-histone-proteins (NHP) are proteins with a specific affinity to DNA; each group is involved in the regulation of gene expression in its own way. To investigate molecular biologic processes at psoriasis, DNA-binding proteins (DBP) were isolated from psoriatic scales. During this work the proportions of histone and NHP of the DBP fractions were examined. Using two different methods (Bio Rex 70-chromatography and isoelectrofocussing), it was found that the isolated DBP contain only acidic proteins. Likewise, the composition of amino acids is comparable with those of acidic, nuclear proteins of other tissues. Thus the isolated DBP represent to its greatest extent acidic, chromosomal NHP, which obviously are derived from the preserved nuclei of the parakeratotic scale layer.

Amino Acids↗
PubMed1978

Presence of two typical DNA-binding nonhistone proteins in psoriatic scales contrary to normal human dermis, epidermis and horny layer.

The composition of DNA-binding proteins (DBP) was shown to be tissue-specific and to vary at different stages of gene expression. As the accelerated epidermopoesis in psoriasis indicates changed gene activities, DBP of psoriatic scales were compared with those of normal human epidermis, dermis and horny layer. Each skin fraction is characterized by its own DBP pattern, indicating different cell species. 1. The DBP of normal human epidermis shows only a small accordance with the DBP of human dermis and implies their difference in origin, function and cell types. 2. Psoriatic scale DBP and epidermal DPB contain more corresponding proteins which can be deduced from the scale's origin from epidermis. However, the composition of all proteins differs to a great extent. This either occured during parakeratotic keratinization or reflects differences of normal to psoriatic epidermis. Imposing for psoriatic scale DBP are two protein bands with molecular weights of 84,000 and 90,000 daltons. Evidently both are not present in the DBP of other skin layers. 3. The horny layer contains a very small amount of DBP which might represent DNases to a major part. The small DBP content in horny layer confirms the previous supposition of psoriatic scales, to be mostly derived from the preserved nuclei of the parakerototic scale layer.

Chromatography, DEAE-Cellulose↗
PubMed1977

DNA-binding proteins of psoriatic scales. I. Isolation by affinity chromatography and characterisation by SDS slab gel electrophoresis.

DNA binding proteins (DBP) are shown to be engaged in the regulatory functions of the genome. Since the accelerated epidermopoesis in psoriasis indicates changed gene activities, the examination of DBP possible could help to clarify the pathological processes. Psoriatic scales were used to elaborate the method. DBP was isolated from a protein extract by affinity chromatography with DNA-cellulose according to Alberts et al. About 3-5% of postribosomal crude protein (PCP) extract had an affinity to DNA. The separation of DBP on SDS polyacrylamide slab gels showed a characteristic spectrum of proteins with molecular weights from 12.7 to 150 X 10(3) daltons. The protein band spectrum of the concentrated DBP fraction was different from that of the crude extract. These observations show the isolated DBP to represent an own group of water soluble proteins with DNA binding abilities.

Chromatography, Affinity↗
PubMed1977

DNA-binding proteins of psoriatic scales. II. DNA-Affinity of the three characteristic proteins increased in the water soluble extract of psoriatic scales.

The disc-electrophoretic pattern of a water soluble protein extract of psoriatic scales contains three characteristic proteins. They appear in higher amounts in psoriatic scales compared to normal human stratum corneum. Assuming that these proteins have any functional implication at DNA, their possible correlation to DNA-binding proteins (DBP) of psoriatic scales was examined. The disc-electrophoretic spectrum of DBP was compared with the protein profile of crude extract. However, no protein of DBP fraction correlated with one of the three characteristic proteins present in a water soluble extract. This signifies these proteins to be more a metabolically enriched product than proteins of chromosomal origin.

DNA Helicases↗
PubMed1976

Electromyographic temporal analysis of gait: normal human locomotion.

The telemetered electromyographic (EMG) activity of pretibial muscles (tibialis anterior), triceps surae (lateral gastrocnemius), medial hamstring group and quadriceps (vastus lateralis) of 20 normal subjects was examined during locomotion. The ages of the subjects ranged from 8 to 72 years (mean, 37 years). A microswitch shoe was used to correlate the EMG activity with eight specific components of the gait cycle. Tibialis anterior showed two peaks of activity, the first at the swing-stance transition, the second at the stance-swing transition. Gastrocnemius showed a single peak of activity recorded during push-off. The medial hamstring showed its greatest activity during deceleration in the swing phase. Vastus lateralis demonstrated peak activity at the transition from swing to stance. The mean cadence was 106 steps per minute. Swing phase occupied 39.6% and stance phase 60.4% of the gait cycle.

Adolescent↗
PubMedDate not supplied

An antigenic region of topoisomerase I in DNA polymerase chain reaction-generated fragments recognized by autoantibodies of scleroderma patients.

Topoisomerase cDNA and various fragments thereof generated by the DNA polymerase chain reaction were cloned into plasmid expression vectors (pET series) and the expressed polypeptides were probed with scleroderma sera from seven different patients immunoreactive with topoisomerase I. All sera reacted selectively with a region between amino acid residues 405 and 484 of human topoisomerase I. This conclusion is based on loss of reactivity when this region was omitted from larger pieces. Other portions of topoisomerase I were not reactive with these autoantibodies. At least two different epitopes appear to be recognized within this region by different sera based on differences in immunoreactivity of the 405-484 region when expressed as C-terminal, N-terminal or internally within a peptide.

Autoantigens↗
PubMedDate not supplied

A liquid chromatographic procedure for the analysis of yohimbine in equine serum and urine.

A standardbred mare was dosed with 40 mg yohimbine intravenously. Serum and urine samples were collected and analyzed for yohimbine using solvent extraction and reversed-phase high-performance liquid chromatography (HPLC) with fluorescence detection. Maximum yohimbine concentrations of 45 and 18 ng/mL were observed in serum and urine samples, respectively. Elimination was rapid, with half-lives of approximately 20 and 53 min observed for serum and urine, respectively. The presence of yohimbine in these samples was confirmed by liquid chromatography/mass spectroscopy (LC/MS/MS).

Animals↗
PubMedDate not supplied

[Chromosomal structures of Pseudomonas testosteroni. I. Isolation and characterization of the chromosomal complexes. (author's transl)].

After lysis of Pseydomonas testosteroni with lysozyme and non-ionic detergents different DNA-protein complexes can be separated in 5-25% (w/v) neutral sucrose gradient. The protein to DNA ratio of these complexes varies between 0.5-4.5 to 1, whereby the faster sedimenting forms contain more protein than the slower sedimenting ones. Different initial rates of DNase digestion may indicate various degrees of DNA packing in these complexes. The chromosomal complexes of Pseudomonas testosteroni are relatively stable towards pronase. Treatment with RNase or sodium dodecylsulphate is accompanied by a dramatic increase in viscosity and decrease in relative density. It suggests that DNA in these complexes is maintained in its supercoiled form by RNA molecule(s) in a similar way as in isolated chromosome of E. coli.

Chromosomes, Bacterial↗
PubMedDate not supplied

[Chromosomal structure of Pseudomonas testosteroni. II. Activity of the endogenous RNA-polymerase (author's transl)].

After careful lysis the nucleoid of Pseudomonas testosteroni can be isolated in three different forms with compact and unfolded DNA structures. The released nucleoids contain endogenous DNA-dependent RNA-polymerase activity using the chromosomal DNA as a template. RNA synthesis is proportional to duration of RNA-polymerase reaction and amount of DNA-protein-complexes. The sensitivity towards ionic strength and rifampicin indicates that a part of RNA-polymerase activity is tightly bound to the chromosomal DNA.

Chromosomes↗
PubMedDate not supplied

[Chromosomal structures of Pseudomonas testosteroni. IV. Effect of testosterone on RNA-synthesis (author's transl)].

Testosterone degrading enzymes are synthesized de novo by bacterium P. testosteroni to utilize testosterone-like steroids as the only source of carbon. RNA-synthesis of the whole lysate of testosterone-induced bacteria was found to be 15% reduced compared to the control, suggesting a cytoplasmatic factor which modulates chromatin associated RNA-polymerase activity.

Chromosomes, Bacterial↗
PubMedDate not supplied

Autoantibodies in scleroderma.

In scleroderma a profusion of circulating autoantibodies have now been defined. They include autoantibodies to Scl-70 or DNA topoisomerase 1, and to centromere/kinetochore proteins of 17.80 and 140 kilodaltons. In addition, there are several antigens which are resident primarily in the nucleolus and they are RNA polymerase 1, PM-Scl, fibrillarin and 7-2 ribonucleoprotein. Antibody to Scl-70 has been found primarily in the diffuse form of scleroderma and antibody to the centromere/kinetochore proteins in the CREST (calcinosis, Raynaud's phenomenon, esophageal dysmotility, sclerodactyly and telangiectasia) subset of scleroderma. Autoantibodies to the nucleolar antigens RNA polymerase 1, PM-Scl, fibrillarin and 7-2 RNP have been detected in at least 10% of all patients with scleroderma. For several reasons which are discussed, it appears that the autoantibody response in scleroderma is antigen-driven and further that the autoantigens involved in this disease are present at some time in the nucleolus. These observations may be providing clues to some of the basic mechanisms initiating autoimmunity.

Autoantibodies↗