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E Eichhorn

Publications and source records attributed to E Eichhorn.

14 recordsLinked to original sources
PubMed2006

Evaluation of soluble CD30 as an immunologic marker in heart transplant recipients.

CD30 is an immunologic molecule that belongs to the TNF-R superfamily. CD30 serves as a T-cell signal transducing molecule that is expressed by a subset of activated T lymphocytes, CD45RO+ memory T cells. Augmentation of soluble CD30 during kidney transplant rejection has been reported. Our study sought to determine whether the level of sCD30 prior to heart transplant could categorize patients into high versus low immunologic risk for a poor outcome. A significant correlation was observed between high levels of soluble CD30 and a reduced incidence of infection. None of the 35 patients with high pretransplant levels of sCD30 level (>90 U/mL) developed infections posttransplantation. However, 9 of 65 patients who had low levels of sCD30 (<90 U/mL) developed infections posttransplantation (P < .02). No remarkable differences were noted among the other clinical parameters. The results also showed that the high-definition flow-bead (HDB) assay detected both weak and strong class I and class II HLA antibodies, some of which (weak class II HLA Abs) were undetectable by the anti-human globulin cytotoxicity method. In addition, more antibody specificities were detected by HDB. In conclusion, we have observed that high levels of sCD30 prior to heart transplant may be associated with greater immunologic ability and therefore produce a protective effect on the development of infection post heart transplant. We have also shown that the HDB assay is superior to the visual cytotoxicity method to detect HLA antibodies, especially those to class II HLA antigens.

Antigens, CD↗
PubMed2001

Escherichia coli utilizes methanesulfonate and L-cysteate as sole sulfur sources for growth.

Twenty-three Escherichia coli strains were tested for their ability to use taurine, methanesulfonate, L-cysteate and other alkanesulfonates as sole sulfur sources for growth. One strain was unable to use any of the alkanesulfonates offered as sole sulfur sources for growth but grew with sulfate. Seven strains (class I) used alkanesulfonates for this purpose, but not methanesulfonate or L-cysteate. A further seven strains (class II) grew with all compounds tested, except with L-cysteate, and eight strains (class III) utilized all compounds tested as sulfur sources. Sulfur assimilation from methanesulfonate and L-cysteate was absolutely dependent on the ssuEADCB operon that encodes an alkanesulfonate uptake system (SsuABC) and a two-component monooxygenase (SsuDE) involved in the release of sulfite from alkanesulfonates. Long-term exposure of class I strains to methanesulfonate and of class II strains to L-cysteate selected for derivatives that utilized these two sulfur sources as efficiently as sulfate. The nucleotide sequence of the ssuEADCB operon in the methanesulfonate- and L-cysteate-utilizing derivative EC1250Me+ was identical to that in the class I wild-type EC1250. Gain of the ability to utilize methanesulfonate and L-cysteate as sulfur sources thus appears to result from increased expression of ssu genes rather than from a change in the quality of one or several of the Ssu proteins.

Alkanesulfonates↗
PubMed2001

Sulfonate-sulfur metabolism and its regulation in Escherichia coli.

In the absence of sulfate and cysteine, Escherichia coli can use aliphatic sulfonates as a source of sulfur for growth. Starvation for sulfate leads to the expression of the tauABCD and ssuEADCB genes. Each of these gene clusters encodes an ABC-type transport system required for uptake of aliphatic sulfonates and a desulfonation enzyme. The TauD protein is an alpha-ketoglutarate-dependent dioxygenase that preferentially liberates sulfite from taurine (2-aminoethanesulfonic acid). SsuD is a monooxygenase that catalyzes the oxygenolytic desulfonation of a range of aliphatic sulfonates other than taurine. Its cosubstrate is FMNH2, which is provided by SsuE, an NAD(P)H-dependent FMN reductase. In contrast to many other bacteria, E. coli is unable to grow with arylsulfonates or with sulfate esters as sulfur source. The tau and ssu systems thus provide all genes for the utilization of known organosulfur sources by this organism, except the as yet unidentified gene(s) that enable some E. coli strains to grow with methanesulfonate or cysteate as a sulfur source. Expression of the tau and ssu genes requires the LysR-type transcriptional regulatory proteins CysB and Cbl. Synthesis of Cbl itself is under control of the CysB protein, and the CysB protein may therefore be regarded as the master regulator for sulfur assimilation in E. coli, while the Cbl protein functions as an accessory element specific for utilization of sulfur from organosulfur sources.

Alkanesulfonates↗
PubMed2001

Practical recommendations for the use of ACE inhibitors, beta-blockers and spironolactone in heart failure: putting guidelines into practice.

Surveys of prescribing in both hospitals and primary care have shown delays in translating improved survival data from clinical trials into clinical practice thereby denying patients the benefits of proven treatments, such as the angiotensin converting enzyme inhibitors. This may be due to unfamiliarity with clinical guidelines and concerns about adverse events. Recent trials have shown that substantial improvements in survival are associated with spironolactone and beta-blocker therapy. In order to accelerate the uptake of these treatments, and to ensure that all eligible patients should receive the most appropriate medications, a clear and concise set of clinical recommendations has been prepared by a group of clinicians with practical expertise in the management of heart failure. The objective of these recommendations is to provide practical guidance for non-specialists in order to support the implementation of evidenced-based therapy for heart failure. These practical recommendations are meant to supplement rather than replace existing guidelines.

Adrenergic beta-Antagonists↗
PubMed2000

Purification and Partial Characterization of Tryptophan 7-Halogenase (PrnA) from Pseudomonas fluorescens This work was supported by the Deutsche Forschungsgemeinschaft (DFG) through the Graduiertenkolleg "Struktur-Eigenschafts-Beziehungen bei Heterocyclen", the Environment and Climate Research and Technology Development Programme of the European Union, the Sächsische Staatsministerium für Umwelt und Landesentwicklung, the Max-Buchner-Stiftung, and the Fonds der Chemischen Industrie. Samples of P. fluorescens BL915DeltaORF1-4 with pPEH14(prnA) and pPEH14(prnC) were obtained from Dr. J. M. Ligon, Novartis Agribusiness Biotechnology Research, Inc., Research Triangle, NC (USA) and NADH oxidase (from Thermus thermiphilus) from Prof. Helmut Erdmann, Fachhochschule Flensburg (Germany).

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Journal Article↗
PubMed2000

Deletion analysis of the Escherichia coli taurine and alkanesulfonate transport systems.

The Escherichia coli tauABCD and ssuEADCB gene clusters are required for the utilization of taurine and alkanesulfonates as sulfur sources and are expressed only under conditions of sulfate or cysteine starvation. tauD and ssuD encode an alpha-ketoglutarate-dependent taurine dioxygenase and a reduced flavin mononucleotide-dependent alkanesulfonate monooxygenase, respectively. These enzymes are responsible for the desulfonation of taurine and alkanesulfonates. The amino acid sequences of SsuABC and TauABC exhibit similarity to those of components of the ATP-binding cassette transporter superfamily, suggesting that two uptake systems for alkanesulfonates are present in E. coli. Chromosomally located in-frame deletions of the tauABC and ssuABC genes were constructed in E. coli strain EC1250, and the growth properties of the mutants were studied to investigate the requirement for the TauABC and SsuABC proteins for growth on alkanesulfonates as sulfur sources. Complementation analysis of in-frame deletion mutants confirmed that the growth phenotypes obtained were the result of the in-frame deletions constructed. The range of substrates transported by these two uptake systems was largely reflected in the substrate specificities of the TauD and SsuD desulfonation systems. However, certain known substrates of TauD were transported exclusively by the SsuABC system. Mutants in which only formation of hybrid transporters was possible were unable to grow with sulfonates, indicating that the individual components of the two transport systems were not functionally exchangeable. The TauABCD and SsuEADCB systems involved in alkanesulfonate uptake and desulfonation thus are complementary to each other at the levels of both transport and desulfonation.

ATP-Binding Cassette Transporters↗
PubMed1999

Characterization of a two-component alkanesulfonate monooxygenase from Escherichia coli.

The Escherichia coli ssuEADCB gene cluster is required for the utilization of alkanesulfonates as sulfur sources, and is expressed under conditions of sulfate or cysteine starvation. The SsuD and SsuE proteins were overexpressed and characterized. SsuE was purified to homogeneity as an N-terminal histidine-tagged fusion protein. Native SsuE was a homodimeric enzyme of M(r) 58,400, which catalyzed an NAD(P)H-dependent reduction of FMN, but it was also able to reduce FAD or riboflavin. The SsuD protein was purified to >98% purity using cation exchange, anion exchange, and hydrophobic interaction chromatography. The pure enzyme catalyzed the conversion of pentanesulfonic acid to sulfite and pentaldehyde and was able to desulfonate a wide range of sulfonated substrates including C-2 to C-10 unsubstituted linear alkanesulfonates, substituted ethanesulfonic acids and sulfonated buffers. SsuD catalysis was absolutely dependent on FMNH(2) and oxygen, and was maximal for SsuE/SsuD molar ratios of 2.1 to 4.2 in 10 mM Tris-HCl, pH 9.1. Native SsuD was a homotetrameric enzyme of M(r) 181,000. These results demonstrate that SsuD is a broad range FMNH(2)-dependent monooxygenase catalyzing the oxygenolytic conversion of alkanesulfonates to sulfite and the corresponding aldehydes. SsuE is the FMN reducing enzyme providing SsuD with FMNH(2).

Alkanesulfonates↗
PubMed1998

Differences in cellular infiltrates in the adenoid of allergic children compared with age- and gender-matched controls.

BACKGROUND: Allergic sensitization of the airways occurs in the mucosa of the shock organ, or in the lymphatic stations draining these structures. The lymphatic structure closest to the nasal mucosa is the adenoid. OBJECTIVES: The objective of this study was to find evidence for our hypothesis that allergic sensitization can occur in the adenoid. Of special interest, in this context are cell types involved in antigen-allergen presentation (e.g. Langerhans cells) and effector cells of allergic disease. METHODS: In this study cellular infiltrates in adenoids of 16 allergic patients and 16 age- and gender-matched controls were evaluated. The number of cells positive for CD1a, CD4, CD8, CD-68, chymase, tryptase, IgE, MBP and cells positive for interleukin (IL)-4 were determined using immunohistochemical staining techniques. The epithelium, follicles and the interfollicular spaces were evaluated separately. RESULTS: When comparing the two groups a significant increase in cells positive for CD1a was found in interfollicular spaces of the allergic group (P = 0.008). CD1a+ cells in the follicular space and eosinophils in the interfollicular space showed a trend to be more numerous in the allergic group (P = 0.02 and P = 0.05, respectively). The other cell types investigated did not show significant differences between the groups. CONCLUSIONS: The results of this study show for the first time that cells involved in allergic sensitization and allergic disease differ in the adenoid of allergic children compared with controls. These findings support our hypothesis that allergic sensitization takes place in the adenoid. Furthermore, this study confirms that CD1a+ (Langerhans) cells are involved in allergic disease.

Adenoids↗
PubMed1997

Characterization of alpha-ketoglutarate-dependent taurine dioxygenase from Escherichia coli.

The Escherichia coli tauD gene is required for the utilization of taurine (2-aminoethanesulfonic acid) as a sulfur source and is expressed only under conditions of sulfate starvation. The sequence relatedness of the TauD protein to the alpha-ketoglutarate-dependent 2,4-dichlorophenoxyacetate dioxygenase of Alcaligenes eutrophus suggested that TauD is an alpha-ketoglutarate-dependent dioxygenase catalyzing the oxygenolytic release of sulfite from taurine (van der Ploeg, J. R., Weiss, M. A., Saller, E., Nashimoto, H., Saito, N., Kertesz, M. A., and Leisinger, T. (1996) J. Bacteriol. 178, 5438-5446). TauD was overexpressed in E. coli to approximately 70% of the total soluble protein and purified to apparent homogeneity by a simple two-step procedure. The apparent Mr of 81,000 of the native protein and the subunit Mr of 37,400 were consistent with a homodimeric structure. The pure enzyme converted taurine to sulfite and aminoacetaldehyde, which was identified by high pressure liquid chromatography after enzymatic conversion to ethanolamine. The reaction also consumed equimolar amounts of oxygen and alpha-ketoglutarate; ferrous iron was absolutely required for activity; and ascorbate stimulated the reaction. The properties and amino acid sequence of this enzyme thus define it as a new member of the alpha-ketoglutarate-dependent dioxygenase family. The pure enzyme showed maximal activity at pH 6.9 and retained activity on storage at -20 degrees C for several weeks. Taurine (Km = 55 microM) was the preferred substrate, but pentanesulfonic acid, 3-(N-morpholino)propanesulfonic acid, and 1,3-dioxo-2-isoindolineethanesulfonic acid were also desulfonated at significant rates. Among the cosubstrates tested, only alpha-ketoglutarate (Km = 11 microM) supported significant dioxygenase activity.

Amino Acid Sequence↗
PubMed1986

Effects of lithium carbonate on human calcium metabolism.

Serum calcium and immunoreactive parathyroid hormone levels increase within the normal range in 80% of patients during the first four weeks of lithium carbonate administration and may rise above normal in 10% after long-term therapy. Since the lithium ion in vitro makes the parathyroid cell less sensitive to calcium, and since several lithium carbonate-treated patients with parathyroid adenomas have been described, it has been suggested that the lithium ion can stimulate parathyroid growth. The data are inconclusive, however, since the adenomas could be sporadic and there has been no direct proof of increased parathyroid mass or biologic activity. Based on the available studies, we have formulated a reasonable scheme for monitoring calcium metabolism during lithium carbonate treatment. Proper treatment of hypercalcemic lithium carbonate-treated patients remains uncertain, but we have outlined some tentative management guidelines.

Adult↗