Biomedical subjects

G Maier

Publications and source records attributed to G Maier.

At least 37 records · Page 2Linked to original sources

PubMed1998

[Patterns of perception of work status: a contribution to innovative capacity of elderly workers].

Current demographic trends indicate an increase in average age within the workforce. The "junior-staff-directed" personnel strategies of companies obviously no longer fit when the number of older workers increase. Based on current research, it is still open in which direction older employees present an obstacle for innovation and which intervention strategies are necessary to promote their ability for innovation. This study particularly indicates the subjective view of older workers regarding various aspects of their current job-situation. Data collection is based on semi-structured interviews with 75 participants (49 men, 26 women, 45 to 55 years old) working in companies of chemical industries in Germany. Results show that older workers have different perceptions of their job situation. One group feels to be "successful and socialintegrated", a second group of older workers "adjusts itself passively to job demands", and a third group is "complaining and not satisfied with the current job situation". Indicators for innovation abilities are "to be able to set goals", "acceptance of challenges" as well as the "acceptance to take over responsibility". In addition aspects of the working conditions and the degree of job-training discriminated between the three groups. The findings point to a close relationship between "innovation capability" of older workers and "stimulating working conditions"; conclusions for personnel strategies can be drawn.

Adaptation, Psychological↗

PubMed1998

Blood flow measurements with [(15)O]H2O and [18F]fluoride ion PET in porcine vertebrae.

A dual positron emission tomography (PET) tracer study with [18F]fluoride and the freely diffusible tracer [(15)O]H2O was performed to measure the capillary transport of [18F]fluoride and to evaluate the potential of [18F]fluoride ion PET to quantitate bone blood flow. Under the condition of a high predictable single-pass extraction fraction (E(F)) for [18F]fluoride, the [18F]fluoride ion influx transport constant (K1F), derived from kinetic [18F]fluoride ion PET measurements, can be used to estimate bone blood flow. Bone blood flow was measured in vertebral bodies by dynamic [(15)O]H2O PET during continuous ventilation with N2O, O2, and Isoflurane (FiO2 = 0.3) in seven adult mini pigs, followed by dynamic [18F]fluoride ion PET. The mean blood flow measured by [(15)O]H2O (FlowH2O) was 0.145 +/- 0.047 ml x minute(-1) x ml(-1) and the mean K1F was 0.118 +/- 0.031 ml x minute(-1) x ml(-1), respectively (mean +/- SD). Regional analysis showed excellent agreement between FlowH2O and K1F at low flow and a significant underestimation of flow by K1F relative to FlowH2O in regions of normal and elevated flow. The observed relationship between parameters followed the Renkin-Crone distribution. The permeability-surface product was determined as 0.25 minute(-1) for vertebral bodies consisting of a mixture of trabecular and cortical bone. We conclude that [18F]fluoride ion PET can be used to estimate bone blood flow in low and normal flow regions, as long as the flow dependency of the E(F) is taken into consideration. Above blood flow values of 0.2 to 0.35 ml x minute(-1) x ml(-1), the magnitude of K1F is increasingly independent on blood flow because diffusion limits tracer transport.

Animals↗

PubMed1998

[Clinical examinations of gilts with puerperal septicemia and toxemia].

In a clinical examination on 78 gilts suffering from feverish puerperal illness the signs were documented. 42 gilts without puerperal disturbances out of the same farms (n = 22) were used as a control. Data for statistics were recorded in minute-books, listing 38 parameters, partly divided in three or four subunits. Within the first 24 hours after parturition 60% of the probands were registered, the other gilts up to the 72nd hour after parturition. 42.3% of the patients beared for the first or second time. Duration of partus averaged more than six hours in 85.9% of patients with consequent puerperal illness, whereas probands of the same age in the control group finished parturition in less than three hours (78.8%; p < or = 0.01). Frequency of obstetrical intervention measured 27% in the group of patients, in the group of probands 9.5% (p < or = 0.05). Gilts with following puerperal illness delivered 1.1 piglets more than healthy individuals (p < or = 0.05) and showed an increased stillbirth rate (p < or = 0.01). Signs of clinical interest in puerperal illness were increase of body temperature (p < or = 0.01), cardiac rate (p < or = 0.01) and respiratory frequency (p < or = 0.01). Approximately 75% of the patients showed anorexia, 66% abnormal faecal consistency. 24.4% of the diseased animals showed exclusively signs of mastitis, in 29.5% there was a combination of mastitis and inflammatory affection of the genital system to be diagnosed, in 46.1% of the cases a solitary infection of the reproductive tract was to be stated. Predominantly E. coli, followed by Staphylococcus spp. and Streptococcus spp. were isolated from the genital tract. The results of this study emphasize the clinical necessity to differentiate between isolated mastitis and puerperal septicaemia respectively toxaemia in cases of feverish puerperal illness. Puerperal septicaemia and toxaemia can, but do not have to be associated with mastitis in gilts.

Animals↗

PubMed1997

Human Supt5h protein, a putative modulator of chromatin structure, is reversibly phosphorylated in mitosis.

The Saccharomyces cerevisiae proteins Spt4p, Spt5p and Spt6p are involved in transcriptional repression by modulating the structure of chromatin. From HeLa cells we have purified a human homologue of Spt5p, Supt5hp, and show here that the protein is reversibly phosphorylated in mitosis. The cloned cDNA predicts a protein of 1087 residues with 31% identity to yeast Spt5p. It includes an acidic N-terminus, a putative nuclear localization signal and a C-terminal region containing two different repeated motifs. One of them, with the consensus sequence P-T/S-P-S-P-Q/A-S/G-Y, is similar to the C-terminal domain in the largest subunit of RNA polymerase II.

Amino Acid Sequence↗

PubMed1997

An automated multidimensional screening approach for rapid method development in high performance liquid chromatography.

Despite enormous advancements in the area of high performance liquid chromatography (HPLC) in recent years, method development remains a major challenge. This is primarily due to the unknown nature of the matrix material which sometimes is difficult to characterize (e.g. biological matrices). To improve the efficiency of method development a multidimensional screening approach was presented. This approach was based on two major steps: (1) a matrix spiked with drug was eluted from a large number of columns, each under different mobile phase compositions, to provide the preliminary selectivity-separation information; (2) this information was then used to compose column switching pairs (each pair consisted of a preparatory column followed by an analytical column) and the elution profile was evaluated to determine the suitable clean up and quantitation conditions. An example was provided using ethyl 3,5-bis(acetylamino)-2,4,6-triiodobenzoate (EEDA), an X-ray enhancement agent, in human plasma. Since the HPLC system was fully automated the data generation time, and consequently the method development time, can be significantly reduced.

Acetonitriles↗

PubMed1997

Identification of monoclonal antibody At5 as a new member of HNK-1 antibody family: the reactivity with myelin-associated glycoprotein and with two brain-specific proteoglycans, phosphacan and neurocan.

Monoclonal antibody At5 was primarily developed against chordin, a notochord-specific antigen of Acipenseridae (sturgeon fishes). In higher vertebrates the antibody reacted mainly with neural tissue antigens. In this study we have shown that the specificity of monoclonal antibody At5 is similar to that of antibodies of HNK-1 family which react with two glycolipids and with several high molecular weight glycoconjugates of neural tissue. We have demonstrated by protein sequencing and immunoblotting that one of At5 target antigens of human brain is dMAG, a derivative of myelin-associated glycoprotein. In the preparations of At5 antigens proteoglycans phosphacan and neurocan were identified by immunoblotting with specific monoclonal antibodies 6B4 and 1G2, respectively. The distribution of At5 and 6B4 immunoreactivity was studied on sections of mixed oligoastrocytoma. Oligodendroglioma area of this tumor was intensely stained with both antibodies, whereas astrocytoma area did not exhibit any At5 or 6B4 immunoreactivity.

Amino Acid Sequence↗

PubMed1997

Gluteal compartment syndrome due to rhabdomyolysis after heroin abuse.

We report a 30-year-old man who developed painful swelling of his right leg and complete sciatic nerve palsy after an i.v. injection of heroin. Excessive elevation of serum creatine phosphokinase indicated the presence of rhabdomyolysis. Fasciotomy of the gluteus maximus led to rapid and complete recovery from sciatic nerve palsy. Nontraumatic rhabdomyolysis may cause a gluteal compartment syndrome that requires immediate fasciotomy.

Adult↗

PubMed1996

Mini-TnhlyAs: a new tool for the construction of secreted fusion proteins.

A simple and efficient procedure for the construction of secreted fusion proteins in Escherichia coli is described that uses a new minitransposon, termed TnhlyAs, carrying the secretion signal (HlyAs) of E. coli hemolysin (HlyA). This transposon permits the generation of random gene fusions encoding proteins that carry the HlyAs at their C-termini. For the construction of model gene fusions we used lacZ, encoding the cytoplasmic beta-galactosidase (beta-Gal), and phoA, encoding the periplasmic alkaline phosphatase, as target genes. Our data suggest that all beta-Gal-HlyAs fusion proteins generated are secreted, albeit with varying efficiencies, by the HlyB/HlyD/TolC hemolysin secretion machinery under Sec-proficient conditions. In contrast, the PhoA-HlyAs fusion proteins are efficiently secreted in a secA mutant strain only under SecA-deficient conditions.

Alkaline Phosphatase↗

PubMed1995

Purification and characterization of subtilisin cleaved actin lacking the segment of residues 43-47 in the DNase I binding loop.

The protease subtilisin has been reported to cleave skeletal muscle G-actin between Met 47 and Gly 48 generating a core fragment of 33 kDa and a small N-terminal peptide, which remains attached to the core fragment [Schwyter, D. Phillips, M., & Reisler, E. (1989) Biochemistry 28, 5889-5895]. However, amino acid sequencing and mass spectroscopy of subtilisin cleaved-actin revealed two cleavage sites, one between Met 47 and Gly 48 and a second between Gly 42 and Val 43, generating an actin core of 37 kDa and a nicked 4.4 kDa N-terminal peptide. Here we describe a procedure for purifying the actin core fragment and the attached N-terminal peptide from the linking pentapeptide comprising amino acid residues 43-47 under native conditions by anion exchange chromatography. After removal of the pentapeptide, the salt-induced polymerization of actin was abolished. However, the purified fragments could be polymerized by addition of salt plus myosin subfragment 1 or salt plus phalloidin as shown by sedimentation and fluorescence increase using N-(1-pyrenyl)iodoacetamide labeled actin. These results confirm earlier reports proposing that cleavage in the DNase I binding loop is affecting the ion induced polymerization of actin [Higashi-Fujime, S., et al. (1992) J. Biochem. (Tokyo) 112, 568-572; and Khaitlina, S., et al. (1993) Eur. J. Biochem. 218, 911-920]. Monomeric and filamentous subactin exhibited reduced abilities to inhibit deoxyribonuclease I (DNase I) and to stimulate the myosin subfragment 1 ATPase activity. Direct binding of subactin to DNase I was verified by gel filtration and to myosin subfragment 1 by affinity chromatography, chemical cross-linking, and electron microscopy.

Actins↗

PubMed1994

Detection of bacteremia by Difco ESP blood culture system.

In a multicenter study, the Difco ESP blood culture system (Difco Laboratories, Detroit, Mich.) was compared with the BACTEC NR660 system (Becton Dickinson Diagnostic Instrument Systems, Sparks, Md.). The ESP system monitors each blood culture bottle every 12 to 24 min to detect changes in oxygen consumption and gas production by microbes. Equal volumes of blood were inoculated into aerobic ESP-80A and BACTEC 6A, 16A, or PEDS Plus broths and anaerobic ESP-80N and BACTEC 7A or 17A broths and were incubated for up to 7 days. ESP bottles contain supplemented tryptic soy broth without antimicrobial agent-adsorbing resins. From 7,532 aerobic compliant sets, the ESP system detected 356 clinically significant positive cultures and the BACTEC NR660 system detected 329. From 6,007 anaerobic cultures, the ESP system detected 234 clinically significant positive cultures and the BACTEC NR660 system detected 198. In aerobic broths, 292 organisms were isolated from both systems and 78 organisms were isolated from the ESP system alone, whereas 54 organisms were isolated from the BACTEC NR660 system alone (P < 0.05). Among individual organisms, pneumococci were isolated significantly more often in ESP aerobic broths. In anaerobic broths, 180 organisms were isolated from both systems and 68 organisms were isolated from the ESP system alone, whereas 35 organisms were isolated from the BACTEC NR660 system alone (P < 0.05). Aerobic gram-positive organisms as a group and Candida spp. were isolated significantly more often in ESP anaerobic broths. Both systems detected 207 clinically significant bacteremic episodes and the ESP system alone detected 63, whereas the BACTEC NR660 system alone detected 32 (P < 0.05). Significantly more episodes of bacteremia caused by Staphylococcus epidermidis and anaerobes were detected by the ESP system. The differences in the numbers of organisms detected >6h earlier in ESP broths compared with BACTNEC NR660 broths were significant, as were earlier times to detection. Although the total number of organisms detected was not significantly different, the ESP system alone detected more organisms in a shorter time than did the BACTEC NR660 system alone. The continuous monitoring capability of the ESP system makes it an attractive alternative to the BACTEC NR660 system.

Adult↗

PubMed1993

[99mTc-MAG3-kidney function scintigraphy without and with captopril in the diagnosis of renovascular hypertension].

In this study, the diagnostic value of renal function scintigraphy performed both without and with ACE inhibition has been evaluated using the new radiopharmaceutical 99mTc-MAG3. In cases of decompensated renal artery stenoses, the typical scan finding with this tubular excreted agent was shown to be a distinct parenchymal nuclide retention in combination with a delayed appearance of the radiotracer in the pelvic system. Using this criterion in 43 patients with suspected renovascular hypertension, sensitivity and specificity were 89 and 88%, respectively. Bilateral positive findings were non-specific; excluding them from the study, specificity increased to 100%. In renal insufficiency, captopril scans seem to be of reduced diagnostic value. Summarising our experiences, renal function scintigraphy using 99mTc-MAG3 without and with captopril was proved to be a reliable non-invasive method to detect or exclude haemodynamically relevant renal artery stenosis.

Captopril↗

PubMed1993

[Evaluation criteria for captopril-kidney function scintigraphy using 99mTc-MAG3].

Renal function scintigraphy under ACE inhibition has gained an important role in the diagnosis of renovascular hypertension. Using the radiopharmaceutical 99mTc-MAG3, 54 kidneys with angiographically verified renal artery status were evaluated with respect to the following scintigraphic parameters: intraparenchymal tracer transport, urine drainage, kidney size, and functional side-to-side ratio. In cases of decompensated renal artery stenosis, the typical scan finding using MAG3 was shown to be a distinct parenchymal nuclide retention in combination with a delayed appearance of the radiotracer in the pelvic system. In our patients, the visual impression of the renal sequential scans was superior to quantitative evaluation methods. Using these criteria in 43 patients with suspected renovascular hypertension, sensitivity and specificity were 89% and 88%, respectively. Bilateral positive findings were nonspecific; when excluding them from the study, specificity increased to 100%.

Adult↗

PubMed1992

Purification and molecular cloning of the APO-1 cell surface antigen, a member of the tumor necrosis factor/nerve growth factor receptor superfamily. Sequence identity with the Fas antigen.

The APO-1 antigen as defined by the mouse monoclonal antibody anti-APO-1 was previously found to be expressed on the cell surface of activated human T and B lymphocytes and a variety of malignant human lymphoid cell lines. Cross-linking of the APO-1 antigen by anti-APO-1 induced programmed cell death, apoptosis, of APO-1 positive cells. To characterize the APO-1 cell surface molecule and to better understand its role in induction of apoptosis, the APO-1 protein was purified to homogeneity from membranes of SKW6.4 B lymphoblastoid cells by solubilization with sodium deoxycholate, affinity chromatography with anti-APO-1 antibody, and reversed phase high performance liquid chromatography. Each purification step was followed by an APO-1-specific solid phase enzyme-linked immunosorbent assay using the monoclonal antibody anti-APO-1. In sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the APO-1 antigen was found to be a membrane glycoprotein of 48-kDa. Endoproteinase-cleaved peptides of the APO-1 protein were subjected to amino acid sequencing, and corresponding oligonucleotides were used to identify a full-length APO-1 cDNA clone from an SKW6.4 cDNA library. The deduced amino acid sequence of APO-1 showed sequence identity with the Fas antigen, a cysteine-rich transmembrane protein of 335 amino acids with significant similarity to the members of the tumor necrosis factor/nerve growth factor receptor superfamily. The APO-1 antigen was expressed upon transfection of APO-1 cDNA into BL60-P7 Burkitt's lymphoma cells and conferred sensitivity towards anti-APO-1-induced apoptosis to the transfectants.

Amino Acid Sequence↗

PubMed1992

Secreted and cellular proteochondroitin sulfates of a human B lymphoblastoid cell line contain different protein cores.

Proteoglycans of the human B lymphoblastoid cell line LICR-LON-HMy2 were metabolically labeled with [35S]sulfate. High-density fractions of 35S-labeled material separated by CsCl gradient ultracentrifugation were further purified by anion exchange chromatography and gel filtration. Two proteoglycans, isolated from cell lysates and culture supernatants, were characterized by gel filtration and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) in combination with enzymatic degradation. Treatment with chondroitinase AC completely degraded the glycosaminoglycan moiety of the proteoglycans. Three to 4 chondroitin sulfate chains (average molecular mass = 26 kDa) were estimated for each of the two proteoglycans. Differences between the proteochondroitin sulfates (CSPG) were observed in the content of N-linked oligosaccharides. After chondroitinase AC treatment the resulting band in SDS-PAGE of the secreted CSPG was sensitive to treatment with endoglycosidase F (Endo F) which further reduced the molecular mass from 30 to 21.5 kDa, whereas the band of the cellular CSPG after chondroitinase AC treatment (molecular mass = 30 kDa) remained resistant to Endo F treatment. The composition of amino acids was different in the protein cores, suggesting differences in the primary structure. Both CSPG contained a high percentage of glycine and serine. For both CSPG a molecular mass of approximately 135 kDa was deduced from the hydrodynamic sizes of the glycosaminoglycan chains obtained after alkaline/borohydride treatment and the migration of the protein/oligosaccharide complexes in SDS-PAGE. 75% of all [35S]sulfate-labeled molecules were found in the culture supernatant and 25% in the cellular fraction. 35S-Labeled material in the culture supernatant consisted exclusively of intact CSPG, whereas 35S-Labeled molecules in the cellular preparation consisted largely of free chondroitin sulfate chains. Only 8.3% of the cellular material, isolated from the microsomal fraction, was intact CSPG. In pulse-chase experiments maximal secretion of CSPG was found after 4 h, comprising approximately 40% of totally synthesized CSPG. From these experiments we tentatively conclude that a small proportion of CSPG synthesized by LICR-LON-HMy2 cells is membrane-associated, a larger portion is secreted, and another portion is intracellularly degraded.

Amino Acids↗

PubMed1990

A 47-kDa human nuclear protein recognized by antikinetochore autoimmune sera is homologous with the protein encoded by RCC1, a gene implicated in onset of chromosome condensation.

Several autoimmune sera from patients with Raynaud phenomenon decorated mammalian kinetochores and bound to a 47-kDa protein on immunoblots of nuclear lysates. Antibody affinity-purified from immunoblots of the 47-kDa band recognized kinetochores, but due to crossreaction with an 18-kDa protein, localization remains elusive. We used one of these sera to purify the antigen from HeLa cells synchronized in mitosis as a noncovalent complex with a 25-kDa protein. The antigen was released from DNA by intercalation with 25 mM chloroquine. Ion-exchange chromatography yielded the pure complex with an apparent molecular size of 68 kDa, which was separated into its components by gel filtration in 6 M guanidinium chloride. Upon two-dimensional gel electrophoresis the 47-kDa protein gave two main spots of pI 6.6 and 6.7, respectively. Posttranslational modification is indicated by additional antigenic spots, by lack of a free alpha-amino group, and by chromatographic behavior of peptides on reversed-phase chromatography. The amino acid sequence for 205 residues of the 47-kDa protein has been established. This sequence is highly homologous with the translated reading frame of RCC1, a gene reportedly involved in regulating onset of mammalian chromosome condensation.

Amino Acid Sequence↗

PubMed1990

[Impulse cytophotometry and irrigation cytology in the diagnosis of bladder cancer].

In a retrospective study in which 273 patients with histologically proven carcinoma of the urinary bladder had been examined by performed cytological and flow cytometric analysis carried out in parallel, the diagnostic yield of flow cytometry was compared with the result of urinary cytology. Urinary cytology and flow cytometry made it possible to detect histologically proven transitional cell carcinoma (TCC) in 60% and 64%, respectively. Combination of the two methods increased the diagnostic yield to 76%. An increase in the diagnostic yield was seen especially for well-differentiated TCC, from 34% to 51%. In spite of this improvement, the combination of flow cytometry with urinary cytology did not mean fewer endoscopic investigations were needed in view of the persisting substantial diagnostic deficit in well-differentiated TCC.

Aneuploidy↗

PubMed1988

[DNA profile, recurrence rate and progression of superficial G2 cancer of the urinary bladder].

In a retrospective study the prognostic value of flow cytometric DNA analysis was studied in 114 newly diagnosed cases with superficial bladder tumours. G1-tumours were generally diploid, G3-tumours almost exclusively aneuploid. G2-tumours exhibited a bimodal distribution with 50% diploid and 50% aneuploid cases respectively. Recurrence and progression correlated systematically with the ploidy level. Furthermore, the degree of aneuploidy is predictive for proneness to progression.

Aged↗

PubMed1987

Cytokeratin domains involved in heterotypic complex formation determined by in-vitro binding assays.

Cytokeratins are constituent proteins of intermediate filaments (IFs) that form heterotypic tetrameric IF subunits containing two polypeptide chains of each of the two cytokeratin subfamilies, i.e. the acidic (type I) and the basic (type II). To locate the molecular domains involved in the formation of these heterotypic complexes, we have developed a binding assay in which total cellular or cytoskeletal polypeptides, or proteolytically prepared cytokeratin fragments, are separated by one-, or two-dimensional gel electrophoresis, blot-transferred on to nitrocellulose paper and probed with radio-iodinated purified cytokeratin polypeptides or fragments thereof, using buffers of various ionic strengths with or without 4 M-urea. Using these polypeptides in the binding assay, specific heterotypic binding was observed between complementary cytokeratin polypeptides of the two subfamilies (but not with other IF proteins) and between the corresponding alpha-helical rod domain fragments. Both rod coils 1 and 2 of the type II cytokeratin 8 bound to the rod (coils 1 and 2) fragment of type I cytokeratins, and this binding occurred at both low and high ionic strengths. The results obtained indicate that: (1) the binding between cytokeratin polypeptides of the complementary type is stronger and more selective than interactions of cytokeratins with other IF and non-IF proteins; (2) both the head and the tail portions of the proteins are not required for heterotypic complex formation; (3) the complementarity information located in the alpha-helical portions of the rod domain, and in short sequences immediately flanking them, is sufficient to discriminate between the two types of cytokeratins and to secure the formation of heterotypic cytokeratin complexes; (4) both coils 1 and 2 of the rod can contribute to this association; and (5) the formation of the heterotypic cytokeratin complex is not critically dependent upon ionic interactions. Our results are further compatible with the concept that the heterotypic binding takes place between cytokeratin homodimer coiled-coils.

Amino Acid Sequence↗