Biomedical subjects

E Korsching

Publications and source records attributed to E Korsching.

6 recordsLinked to original sources

PubMed2003

Molecular cytogenetic investigations of synchronous bilateral breast cancer.

BACKGROUND: Bilaterality in breast cancer is a rare event and together with an early onset of disease points towards inheritance of the disease. However, most cases seem to occur sporadically, either in a synchronous or metachronous manner. METHODS: Thirty two invasive carcinomas and one in situ carcinoma from 16 patients with synchronous, bilateral breast cancer were investigated by means of comparative genomic hybridisation (CGH) and polymerase chain reaction based multiplex microsatellite analysis. The results were analysed conventionally and were also subjected to a biomathematical cluster analysis. RESULTS: On average, bilateral breast cancer cases showed a low number of genetic alterations, a low frequency of genetic amplifications, and a high rate of chromosomal 16q losses. A distinct, characteristic genetic alteration associated with bilateral breast disease could not be found. Although two tumour pairs appeared to be related using biomathematical processing for microsatellite analysis, this result was reproduced by CGH data processing in one patient only. CONCLUSIONS: Most synchronous, bilateral breast cancer cases seem to represent independent tumours rather than metastatic events. Nevertheless, the possibility of a specific susceptibility remains.

Adult↗

PubMed2003

Demystified...tissue microarray technology.

Several "high throughput methods" have been introduced into research and routine laboratories during the past decade. Providing a new approach to the analysis of genomic alterations and RNA or protein expression patterns, these new techniques generate a plethora of new data in a relatively short time, and promise to deliver clues to the diagnosis and treatment of human cancer. Along with these revolutionary developments, new tools for the interpretation of these large sets of data became necessary and are now widely available. Tissue microarray (TMA) technology is one of these new tools. It is based on the idea of applying miniaturisation and a high throughput approach to the analysis of intact tissues. The potential and the scientific value of TMAs in modern research have been demonstrated in a logarithmically increasing number of studies. The spectrum for additional applications is widening rapidly, and comprises quality control in histotechnology, longterm tissue banking, and the continuing education of pathologists. This review covers the basic technical aspects of TMA production and discusses the current and potential future applications of TMA technology.

Animals↗

PubMed2000

Telepathology network: conceptual groundwork and evaluation.

Telepathology uses telecommunication technology to transmit microscopic images for diagnostic or teaching purposes. Basic requirements for a telepathology system are described. Usage scenarios for a telepathology network are presented including applications in intraoperative frozen section diagnosis, scientific collaboration and computer based training. Results of an evaluation of 4 currently available telepathology systems are presented.

Computer Communication Networks↗

PubMed1995

Generation of type VIII collagen-specific antibodies.

We generated a specific polyclonal antibody against the alpha 1 chain of type VIII collagen. The antibody detects type VIII collagen and is definitely free of crossreactivities with the closely related type X collagen. The antibody was generated against a dodecamer peptide chosen to satisfy the following requirements: (a) maximal homology between collagen type VIII molecules from different species; (b) maximal antigenicity as predicted by algorithms from Emini et al. (J. Virol. (1985) 55, 836). Hoop and Woods (Proc. Natl. Acad. Sci. USA (1981) 78, 3824), and Karplus and Schulz (Naturwissenschaften (1985) 72, 212); and (c) maximal specificity, i.e. absence of this sequence in all other proteins known so far. All three requirements were satisfied for a sequence fragment of 12 amino acids (100-111) in the alpha 1(VIII) NC2 domain. This peptide was produced synthetically. Polyclonal antibodies were raised in rabbits and affinity purified on a peptide column. The antibody was tested in a quantitative EIA, immunoblots and in immunocytochemistry and found to be well-suited for all three types of application. The antibody did not crossreact with type X collagen and other extracellular matrix molecules in the EIA. In immunoblots of affinity-purified extracts of the Descemet membrane, a major source of type VIII collagen, the antibody detected several known forms of type VIII collagen. In immunocytochemistry the antibody stained endothelial and astrocytoma cells in monolayer cultures, and cells and extracellular matrix in cryosections of the human Ewing sarcoma, arterial vessels and chicken embryonic heart, whereas the chicken tibiotarsus remained negative. This distribution of immunoreactivity corresponds to the distribution of type VIII but not that of type X collagen. In conclusion this antibody may serve as a highly specific and sensitive tool for investigating the appearance and regulation of type VIII collagen.

Amino Acid Sequence↗

PubMed1990

The primary structure of a triple-helical domain of collagen type VIII from bovine Descemet's membrane.

We have isolated and sequenced a fragment of 469 amino acid residues from bovine type VIII collagen. The sequence was composed of a series of Gly-X-Y repeats which was interrupted 8 times by short imperfections. The number and relative location of these interruptions were similar to those of chicken alpha 1(X) and rabbit alpha 1(VIII) chain triple-helical domains. Comparison to published N-terminal sequences to two triple-helical fragments of bovine type VIII collagen and to the cDNA derived sequence of the rabbit alpha 1(VIII) chain showed that this fragment was the triple-helical domain of a second type VIII collagen chain which we designate alpha 2(VIII).

Amino Acid Sequence↗

PubMed1990

Characteristics and in vivo occurrence of type VIII collagen.

Type VIII collagen was isolated from bovine Descemet's membranes by pepsin treatment and salt fractionation, as described by Kapoor et al. [(1986) Biochemistry 25, 3930-3937]. Contaminating type IV collagen was removed by ion-exchange chromatography. Purified type VIII collagen consisted of two different polypeptide chains and, compared to the fiber forming collagens, showed a higher thermal stability. Corresponding fractions isolated from pepsinized human Ewing's sarcoma and fetal calf aorta reacted immunologically with a protein of similar molecular mass. After extraction of Descemet's membranes with guanidine hydrochloride, a peptide of about 60 kDa was obtained. This seems to be the tissue form of type VIII collagen.

Amino Acids↗