Biomedical subjects

C Gauss

Publications and source records attributed to C Gauss.

8 recordsLinked to original sources

PubMed2004

Factors affecting the seroprevalence of Toxoplasma gondii infection in wild rabbits (Oryctolagus cuniculus) from Spain.

Sera from 456 wild rabbits (Oryctolagus cuniculus) collected between 1992 and 2003 from five geographical regions of Spain were examined for antibodies to Toxoplasma gondii by the modified agglutination test. Antibodies to T. gondii were found in 65 (14.2%) wild rabbits. Prevalence of infection was significantly higher in samples collected from wild rabbits from Catalonia, northeast Spain (53.8%), where rabbits lived in forest, compared to other areas (Huelva and Cádiz, Andalucía, south Spain; Toledo, Castilla-La Mancha, central Spain; and Zaragoza, Aragón, northeast Spain) with more dry conditions, where prevalence ranged from 6.1 to 14.6%. No differences were observed on prevalence and age (young animals <7 months of age compared to older animals), sex, date of samples collection or season of samples collection. The results indicate that prevalence of T. gondii in some areas of Spain is high, and this finding could have environmental and/or public health implications if wild rabbits are to be used as a source of food.

Age Factors↗

PubMed2004

Revascularization procedures in internal carotid artery pseudo-occlusion.

BACKGROUND: Surgical treatment of patients with suspected internal carotid artery (ICA) pseudo-occlusion and reduced cerebrovascular reactivity (CVR) is still uncertain regarding the diagnostic procedures, the risks and the optimal timing as well as performance of revascularization. METHOD: From 1983-2001, 781 patients with symptomatic ICA stenosis were treated surgically. In 53 patients, a final diagnosis of extracranial ICA pseudo-occlusion was established by repeating Digital Subtraction Angiography (DSA). Angiographical findings were anterograde "string-like" filling of ICA beyond the carotid bifurcation or retrograde filling of the proximal, so called "occluded" extracranial ICA, extending up to the skull base. The CVR was reduced. All patients underwent direct surgery of extracranial carotid artery. Diagnostic parameters, peri-operative risks and postoperative course of these patients were evaluated. FINDINGS: In 40 patients (75.5%) a successful revascularization of ICA was possible. ICA pseudo-occlusion was in all cases of atheromatous origin, moreover in 8 patients combined with a floating thrombus, distal to the stenosis. Thrombectomy was done by means of Fogarty catheter. In 13 patients (24.5%), a surgical re-opening of the ICA lumen was not possible. Five of these patients showed in DSA an anterograde "string sign", eight presented retrograde filling of ICA reaching the skull base. Peri-operative mortality was 1.9%, peri-operative morbidity was 7.5%. After a 4 years (mean) follow-up, 95% of the reopened ICA remained patent. CONCLUSION: In patients with explicit carotid artery occlusion signs, careful selective DSA should be compulsory with a late series to detect ICA pseudo-occlusion. There is a chance for extracranial reopening ICA, even with compromised CVR, if anterograde "string like" or retrograde filling of proximal so called "occluded" ICA as far as the skull base is angiographically identified.

Adult↗

PubMed2001

The huntingtin interacting protein HIP1 is a clathrin and alpha-adaptin-binding protein involved in receptor-mediated endocytosis.

The huntingtin interacting protein (HIP1) is enriched in membrane-containing cell fractions and has been implicated in vesicle trafficking. It is a multidomain protein containing an N-terminal ENTH domain, a central coiled-coil forming region and a C-terminal actin-binding domain. In the present study we have identified three HIP1 associated proteins, clathrin heavy chain and alpha-adaptin A and C. In vitro binding studies revealed that the central coiled-coil domain is required for the interaction of HIP1 with clathrin, whereas DPF-like motifs located upstream to this domain are important for the binding of HIP1 to the C-terminal 'appendage' domain of alpha-adaptin A and C. Expression of full length HIP1 in mammalian cells resulted in a punctate cytoplasmic immunostaining characteristic of clathrin-coated vesicles. In contrast, when a truncated HIP1 protein containing both the DPF-like motifs and the coiled-coil domain was overexpressed, large perinuclear vesicle-like structures containing HIP1, huntingtin, clathrin and endocytosed transferrin were observed, indicating that HIP1 is an endocytic protein, the structural integrity of which is crucial for maintenance of normal vesicle size in vivo.

Adaptor Protein Complex alpha Subunits↗

PubMed2001

Predictive value of chromatin decondensation in vitro on fertilization rate after intracytoplasmic sperm injection (ICSI).

This study was undertaken to identify the relationship between sperm chromatin decondensation after incubation with sodium dodecyl sulphate (SDS) and ethylene diamine tetra acetic acid (EDTA), or heparin at various points of time. Likewise, this study will determine chromatin stability within definite time intervals, chromatin decondensation after intracytoplasmic sperm injection (ICSI), and whether chromatin decondensation in vitro could be used as a predictive test for fertilization capability after ICSI. Sixty-five infertile couples undergoing ICSI therapy were included in this prospective study. Male factor infertility was the main indication for inclusion. One millilitre from each semen sample after washing was mixed with SDS-EDTA (group 1) or SDS/heparin (group 2) and incubated for 120 min. Many smears were made within 10 min of mixing the spermatozoa with detergent and the reducing agents and at the following points of time 30, 60 and 120 min and after 24 h. Chromatin decondensation was evaluated after staining with acridine orange (AO). The mean percentage of uncondensed chromatin of spermatozoa in the semen sample in the first group before addition of SDS/EDTA was 26.1 +/- 19.0 and 22.3 +/- 18.9% in the second one. After incubation of spermatozoa for 30, 60 and 120 min and 24 h, the chromatin decondensation increased in the first group to 64.0 +/- 28.6, 83.0 +/- 21.1, 87.9 +/- 14.6, 92.1 +/- 16.2 and 98.0 +/- 6.75%, respectively. The corresponding values in the second group were 69.5 +/- 29.9, 78.6 +/- 22.4, 86.9 +/- 17.1, 95.13 +/- 6.5 and 98.3 +/- 5.6%. On the other hand, no correlations were found between the chromatin decondensation or chromatin decondensation rate in vitro and the fertilization rates in all investigated groups. In conclusion, neither the chromatin decondensation ability in vitro nor the rate of chromatin decondensation between various points of time after using SDS/EDTA, SDS/heparin could predict the chromatin decondensation of spermatozoa (fertilization capability) after ICSI.

Adult↗

PubMed1999

Analysis of the mouse proteome. (I) Brain proteins: separation by two-dimensional electrophoresis and identification by mass spectrometry and genetic variation.

The total protein of the mouse brain was fractionated into three fractions, supernatant, pellet extract and rest pellet suspension, by a procedure that avoids any loss of groups or classes of proteins. The supernatant proteins were resolved to a maximum by large-gel two-dimensional electrophoresis. Two-dimensional patterns from ten individual mice of the commonly used inbred strain C57BL/6 (species: Mus musculus) were prepared. The master pattern was subjected to densitometry, computer-assisted image analysis and treatment with our spot detection program. The resulting two-dimensional pattern, a standard pattern for mouse brain supernatant proteins, was divided into 40 squares, calibrated, and specified by providing each spot with a number. The complete pattern and each of the 40 squares are shown in our homepage (http://www.charite.de/ humangenetik). The standard pattern comprises 8767 protein spots. To identify the proteins known so far in the brain fraction investigated, a first set of 200 spots was analyzed by matrix-assisted laser desorption/ionization - mass spectrometry (MALDI-MS) after in-gel digestion. By screening protein databases 115 spots were identified; by extending the analysis to selected, genetically variant protein spots, 166 spots (including some spot series) were identified in total. This number was increased to 331 by adding protein spots identified indirectly by a genetic approach. By comparing the two-dimensional patterns from C57BL/6 mice with those of another mouse species (Mus spretus), more than 1000 genetically variant spots were detected. The genetic analysis allowed us to recognize spot families, i.e., protein spots that represent the same protein but that are post-translationally modified. If some members of the family were identified, the whole family was considered as being identified. Spot families were investigated in more detail, and interpreted as the result of protein modification or degradation. Genetic analysis led to the interesting finding that the size of spot families, i.e., the extent of modification or degradation of a protein, can be genetically determined. The investigation presented is a first step towards a systematic analysis of the proteome of the mouse. Proteome analysis was shown to become more efficient, and, at the same time, linked to the genome, by combining protein analytical and genetic methods.

Animals↗

PubMed1997

Cystic craniopharyngioma: long-term results after intracavitary irradiation with stereotactically applied colloidal beta-emitting radioactive sources.

OBJECTIVE: Long-term follow-up data were analyzed to assess the value of intracavitary irradiation with stereotactically applied beta-emitting radioisotopes for the treatment of craniopharyngioma cysts. METHODS: Sixty-two of 70 consecutive patients with predominantly cystic craniopharyngiomas were selected for retrospective analysis. Beta-Emitting isotopes were injected intracystically using a computed tomography-guided and computer-assisted three-dimensional stereotactic treatment planning and application system (cumulative dose to the inner surface of the cyst wall, 200 Gy). RESULTS: The tumor response rate gained with yttrium-90-labeled silicate (66 of 78 cysts) or phosphorous-32-labeled chromic phosphate (8 of 78 cysts) was 79.5%. Four cysts treated with rhenium-186-labeled sulfate did not respond. Mean survival after intracavitary irradiation was 9.0 +/- 0.9 years (median follow-up, 11.9 yr). In patients with solitary cysts, the mean survival was 12.5 +/- 1.4 years (actuarial 5- and 10-yr survival rates, 80 and 64%, respectively). Six months postoperatively, visual deficits (38 of 62 patients) had improved in 23 patients and were stable in 15 patients. The side effects that occurred 6 to 12 months after treatment with yttrium-90 were complete blindness (three patients), worsening of visual field cuts (one patient), third nerve palsy (one patient), and diabetes insipidus and/or panhypopituitarism (three patients). CONCLUSIONS: Intracavitary irradiation using yttrium-90 or phosphorous-32 is highly effective in the treatment of cystic craniopharyngiomas. If applied as initial treatment in patients with solitary cysts, it is the only required therapy over a long period.

Adolescent↗

PubMed1990

Mass spectrometric peptide mapping analysis and structural characterization of dihydrodiol dehydrogenase isoenzymes.

The direct molecular weight determination and structural analysis of polypeptides and peptide mixtures have become amenable by the recent development of fast atom bombardment (FABMS) and 252Cf-plasma desorption (PDMS) mass spectrometry. FABMS and PDMS peptide mapping, i.e., the direct analysis of peptide mixtures resulting from proteolytic digestion, have been developed as powerful methods for the structural characterization of epoxide-metabolizing isoenzymes. The major advantage of this approach is provided by the selectivity of the endoproteolytic cleavage, combined with the specific and accurate molecular weight determination of complex digest mixtures containing peptides up to several thousands daltons in size. Furthermore, the mass spectrometric peptide mapping analysis can be combined with a range of protein-chemical modification reactions and with sequential degradation such as by carboxypeptidases. Both FABMS and PDMS peptide mapping have already been successfully applied to the structural differentiation of glutathione transferase and epoxide hydrolase isoenzymes in cases where references sequence data for at least one isoenzyme form was available. In the application described here, for a series of dihydrodiol dehydrogenase (DDH) isoenzymes with hitherto undetermined primary structures, a direct correlation between the structural differentiation from peptide mapping data and differences in their substrate specificities could be demonstrated. The mass spectrometric peptide mapping analysis of isoenzymes proved to be an efficient basis for the elucidation of the structure of one major DDH isoenzyme form; partial sequence data for this protein are reported.

Alcohol Oxidoreductases↗

PubMedDate not supplied

Technology development at the interface of proteome research and genomics: mapping nonpolymorphic proteins on the physical map of mouse chromosomes.

Data obtained from protein spots by peptide mass fingerprinting are used to identify the corresponding genes in sequence databases. The relevant cDNAs are obtained as clones from the Integrated Molecular Analysis of Genome Expression (I.M.A.G.E.) consortium. Mapping of I.M.A.G.E. clones is performed in two steps: first, cDNA clones are hybridized against a 10-hit genomic mouse bacterial artificial chromosome (BAC) library. Second, interspersed repetitive sequence polymerase chain reaction (IRS-PCR) using a single primer directed against the mouse B1 repeat element is performed on BACs. As each cDNA detects several BACs, and each individual BAC has a 50% chance to recover an IRS-PCR fragment, the majority of cDNAs produce at least a single IRS-PCR fragment. Individual IRS fragments are hybridized against high-density spotted filter grids containing the three-dimensional permutated pools of yeast artificial chromosome (YAC) library resources that are currently being used to construct a physical map of the mouse genome. IRS fragments that hybridize to YAC clones already placed into contigs immediately provide highly precise map positions. This technology therefore is able to draw links between proteins detected by 2-D gel electrophoresis and the corresponding gene loci in the mouse genome.

Animals↗