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T Herrmann

Publications and source records attributed to T Herrmann.

At least 127 records · Page 7Linked to original sources
PubMed1990

Spatial behaviour of normal and septal rats on alternate route maze problems.

The behaviour of normal rats and rats with lesions of the septum was compared on a variety of alternate route variations of the three-table problems. In all variations of the task, septal rats were impaired on test trial performance when they displayed stereotypic body turn responses and demonstrated a strong preference for the most direct route between tables both during exploration and testing in all conditions. Normal rats displayed a similar route choice tendency in the simplest situations but shifted route choice behaviour in the most complex configuration, when they chose the inner, but longer, path. The use of the inner path may have allowed delayed-choice, single-point reference orientation, or reduction in the number of available alternatives. It is concluded that normal rats form a cognitive representation that allows them to identify environmental factors likely to facilitate solution, whereas septal rats rely on "taxon"-type strategies that can combine guidances and orientational responses.

Animals↗
PubMed1990

Application of a semi-phenomenological model to experimental data of radiation induced pneumopathy in pigs.

A semi-phenomenological model has been derived, which describes the inactivation effect on individual cells by survival curves. This model is applied to experimental data of pneumopathy in pigs. The corresponding survival curves as well as the relations between cell survival and complication probability are calculated and discussed. Furthermore, dose-response curves for single dose irradiation and different fractionation schemes are derived. The comparison between the response curve for single dose irradiation and similar curves from the literature shows a good agreement.

Animals↗
PubMed1989

The intermediate-affinity interleukin (IL)2 receptor expressed on Theileria annulata-infected cells comprises a single IL 2-binding protein. Partial characterization of bovine IL2 receptors.

Bovine high-, intermediate- and low-affinity interleukin 2 receptors (IL2R) were studied by ligand binding and affinity labeling using 125I-labeled IL2 and homobifunctional chemical cross-linking reagents. High- (Kd = 17 pM) and low-affinity (Kd greater than 6 nM) IL 2R were detected on concanavalin A-activated peripheral blood lymphocytes (PBL). Theileria annulata (TA)-infected autonomously growing PBL (TA-PBL) express predominantly intermediate-affinity IL2R (Kd = 1 nM). Affinity-labeling studies revealed that the high-affinity IL2R comprises a 55-kDa (L chain) and an additional 90-kDa IL 2-binding protein (H chain). TA-PBL express predominantly the H chain. In contrast to the human chain, the bovine form was not separable by sodium dodecyl sulfate-polyacrylamide gel electrophoresis/urea into the two distinct bands H1 and H2 and ran in parallel to the human H2 band. These results suggest (a) that the bovine intermediate-affinity IL2R comprises a single H chain and (b) that the single H chain and the L chain are sufficient to form the functional high-affinity bovine IL2R.

Affinity Labels↗
PubMed1989

Different staphylococcal enterotoxins bind preferentially to distinct major histocompatibility complex class II isotypes.

The stimulation of T cells by staphylococcal enterotoxins (SE) is strictly dependent on major histocompatibility complex (MHC) class II-bearing cells. The interaction between SE and MHC class II molecules was studied on the human B cell lymphoma Raji and its MHC class II-negative variant RJ 2.2.5. Affinity purification with SEA and SEB matrix allowed the isolation of HLA-DR-like molecules from detergent lysates of 125I surface-labeled Raji cells, but not from RJ 2.2.5 cells. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis also revealed preferences in the binding of other SE such as SED, SEE and toxic shock syndrome toxin 1 to DR-like molecules, SEC2 to HLA-DQ-like molecules and SEC3 to DR- and DQ-like molecules. Preadsorption of the different MHC class II MHC isotypes confirmed the preferential binding of SEA to DR and of SEC2 to DQ. The implications of these findings for the understanding of SE-induced T cell activation and the potency of SE as a tool in the study of MHC class II antigens are discussed.

Chromatography, Affinity↗
PubMed1989

[Radiation sequelae of the pancreas].

The pancreas has been considered a radioresistant organ for a long time. This classification originates in absence of clinical symptoms or in the vague position of the organ within the symptom-complex of radiogenic malabsorption after pancreas irradiation. Experiments with animals show considerable alterations after irradiation yet, especially in ultrastructural sphere. These disorders appear to be altered qualitatively after fractionated radioexposure: whereas in high single doses the parenchymatous part is affected more, in severe small single doses in area of small vessels with relatively early fibrotic alteration more severe alterations are described by different investigators. Alterations in parenchymatous structures of pancreas are capable of regression. Nevertheless it is not explained till now, why lasting pancreas-enzyme reduction can develop after a longer period. The great compensatory ability of pancreas results in merely non-essential enzyme alterations in serum as a rule in small-fractionated irradiation of upper abdomen. Unanimously all investigators find a small or no impairment of island cell apparatus after irradiation. Continuation of studies on radiogenic impairment of pancreas seems to be required earnestly, in particular in investigations of different fractionation rhythm too. However it renders more difficult by the problem to mark off clear endpoint-criteria.

Animals↗
PubMed1989

Demonstration of two distinct forms of released low affinity-type rat IL-2 receptors.

The release of IL-2 binding proteins, derived from the 55,000 MW low affinity IL-2R (L chain), has been observed for virtually all L chain-bearing cells in either humans, the mouse or the rat. Based on the characterization of the released human L chain as a molecule 10,000 MW smaller than the cell surface receptor, either proteolytic cleavage or differential splicing of the L chain encoding mRNA have been suggested as mechanisms underlying the receptor release. Combining affinity labelling of the L chain with [125I]IL-2 and immunoprecipitation with L chain-specific monoclonal antibody (mAb) applied for the detection of soluble rat IL-2R revealed the existence of two classes of soluble receptors, one being of the same size as cell surface-expressed L chain, the other of 40,000 apparent molecular mass. These findings raise the possibility of other mechanisms of receptor release than those discussed for human L chain.

Affinity Labels↗
PubMed1988

Determination of picogram amounts of lipoxin A4 and lipoxin B4 by high-performance liquid chromatography with electrochemical detection.

A new method for the determination of lipoxins with electrochemical detection after high-performance liquid chromatography is described. The half-wave potentials of lipoxin A4 and lipoxin B4 at a glassy carbon electrode and a mobile phase of methanol-water (65:35 v/v) and 1 mM trifluoroacetic acid was found to be +1.14 V versus an Ag/AgCl reference electrode. The use of trifluoroacetic acid instead of sulphuric acid and lithium perchlorate led to a background current of 6-8 nA at +1.20 V. The detection limits for both lipoxins, based on a signal-to-noise ratio of 3:1 were found to be 5-10 pg (15-30 fmol). The new method was applied to an extract of human polymorphonuclear granulocytes, preincubated with 15-hydroxyeicosatetraenoic acid and stimulated with Ca2+ ionophore A23187.

Chemical Phenomena↗
PubMed1988

[Primary extranodular non-Hodgkin's lymphomas--observations on etiopathogenesis, histology and prognosis].

The total non-Hodgkin's lymphoma-population treated between 1978 and 1986 by means of radiotherapy or combined chemo/radiotherapy was analysed as to primary extranodular manifestation. 39 cases, 16 women and 23 men, were observed (stage IE 12, stage IIE 22 and stage IIIE 5). Immunoblastic (10), lymphoblastic (9) and centroblastic (6) lymphomas are the most frequent with respect to histology. Gastroenteron (16) and otorhinolaryngological region (13) are in the lead with regard to localisation. 5-year-survival-rates are determined in dependence on clinical stage: IE 65.8%, IIE 39.2% (low, connected with the proportion of high-malignant histology) and IIIE 25.0%. The 5-year-survival-rate of primary gastrointestinal manifestation amounted to 51.5%. With respect to aetiopathogenesis of primary extranodular lymphomas gut-, mucosa- and bronchial-associated lymphoid tissue, aberrant lymph-nodes and the influence of viral- and immunologic factors seem to be important.

Adult↗
PubMed1988

The human intermediate-affinity interleukin 2 receptor consists of two distinct, partially homologous glycoproteins.

In this report we demonstrate that the human intermediate-affinity-type interleukin (IL) 2 receptor (IL 2R) consists of two distinct glycoproteins designated H1 and H2, whereas the high-affinity IL 2R consists of three chains, H1, H2 and the light chain (L), the Tac antigen. They are neither linked by disulfide bridges to each other nor to the L chain. Similar to the L chain, H1 and H2 apparently carry intramolecular disulfide bonds. From affinity-labeled IL 2 intermediate-affinity receptor complexes, we deduced an apparent mol. mass of 70 kDa for H1 and of 75 kDa for H2 in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and of 55 kDa for H1 and of 85 kDa for H2 in SDS-PAGE/urea. As demonstrated by limiting proteolysis, both glycoproteins display high homologies or even identity proximal to the IL 2-binding sites. The areas which are responsible for the striking differences between H1 and H2 in SDS-PAGE/urea are located distally to the IL2-binding site and, in contrast to the L chain, are protected from the action of exogenous proteases by the plasma membrane.

Cross-Linking Reagents↗
PubMed1988

Demonstration of two distinct forms of released low-affinity type interleukin 2 receptors.

The release of interleukin 2 (IL2)-binding proteins, derived from the 55-kDa low-affinity IL2 receptor (IL2R; L chain), has been observed for virtually all L chain-bearing cells in either humans, the mouse or the rat. Based on the characterization of the released human L chain as a molecule 10 kDa smaller than the cell surface receptor, either proteolytic cleavage or differential splicing of the L chain-encoding mRNA have been suggested as mechanisms underlying the receptor release. Combining affinity labeling of the L chain with 125I-labeled IL2 and immunoprecipitation with L chain-specific monoclonal antibodies applied for the detection of soluble mouse IL2R revealed the existence of two classes of soluble receptors, one being of the same size as cell surface expressed L chain, the other of 45-kDa apparent molecular mass. These findings raise the possibility of mechanisms of receptor release other than those discussed for human L chain.

Animals↗
PubMed1988

The high affinity interleukin 2 receptor: evidence for three distinct polypeptide chains comprising the high affinity interleukin 2 receptor.

Low and high affinity receptors for interleukin 2 were investigated on interleukin 2 (IL-2) receptor bearing cells by chemical cross-linking of 125I-labelled IL-2 to its receptor, or membrane proteins associated with the IL-2 binding sites. SDS-PAGE analysis of the cross-linked complexes of the murine CTLL 16 cells and human T-blasts, which bear high and low affinity IL-2 receptors, showed three distinct bands. The fastest of those three bands ran in parallel to the single band of 65-70 kDa found on the only low affinity receptor bearing mouse T-lymphoma Eb, which is thought to be one beta-chain (55 kDa IL-2 binding protein) and one IL-2. Both upper bands ran in parallel with those produced by the 2C8 clone of the NK-like cell line YT which lacks the 55 kDa binding protein and bears only a single class of receptors with an intermediate affinity. Internalisation studies using CTLL 16 cells revealed that all three bands disappeared under conditions allowing receptor internalisation. Low and high affinity binding sites of CTLL 16 cells were destroyed by trypsinisation and the IL-2 binding properties of the cells were regenerated in parallel with the reappearance of all bands. These results show in addition to the beta-chain (55 kDa binding protein) and the alpha-chain 75 kDa binding protein, an IL-2 membrane protein complex with an apparent mol. wt of 115 kDa in CTLL 16 cells. They are the first direct indication of a putative gamma-chain of the high affinity IL-2 receptor.

Animals↗