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1.
Ultraschall Med ; 21(2): 47-58, 2000 Apr.
Article in German | MEDLINE | ID: mdl-10838704

ABSTRACT

Endosonography is an imaging method whereby a high frequency ultrasound probe is inserted into a body cavity with or without under endoscopic control. Examination of the gastrointestinal tract is performed using special echo-endoscopes or trans-endoscopic mini-probes. The gastrointestinal wall, mediastinum, pancreas, bile ducts, retroperitoneum, and other structures surrounding the gastrointestinal tract are target organs for endosonography. A detailed image of pathological processes can thus be obtained. The method can be used both for primary diagnosis of lesions and in follow-up of gastrointestinal diseases. It is accurate in local staging of cancer and in detecting small lesions. There are some limitations for optimal examination like stenoses or other factors prohibiting a precise positioning of the ultrasound transducer. The clinical importance of endo-sonographic examinations must be continuously evaluated on the basis of new technical modalities and changes in therapeutic procedures.


Subject(s)
Endosonography , Gastrointestinal Diseases/diagnostic imaging , Humans
3.
Stud Health Technol Inform ; 39: 246-53, 1997.
Article in English | MEDLINE | ID: mdl-10173061

ABSTRACT

This paper describes a method for the acquisition and integrative processing of laparoscopic and endoluminal ultrasound images. We used a stepping motor attached to a stabilizing rig, interfaced to the laparoscope, or the ultrasound probe. 360 degrees laparoscopic scenes were constructed during minimally invasive surgery, and three-dimensional reconstructions were made of related ultrasound data. Integration of 360 degrees panoramas with geometric ultrasound models could be displayed as interactive scenes. This resulted in a better demonstration of the surgical field and topographic anatomy. In conclusion, this type of visualizations may be used in virtual reality simulations for documentation, education and in operative planning.


Subject(s)
Endosonography/methods , Image Processing, Computer-Assisted/methods , Laparoscopy/methods , User-Computer Interface , Computer Simulation , Humans , In Vitro Techniques , Software Design
4.
J Histochem Cytochem ; 33(4): 367-74, 1985 Apr.
Article in English | MEDLINE | ID: mdl-3884707

ABSTRACT

The localization of the alpha and beta subunits of S-100 protein was studied in normal tissue where the identification of three subclasses of S-100 containing cells was derived: i) cells that contain both alpha and beta subunits; ii) cells that contain only the alpha subunit; and iii) cells that contain only the beta subunit. In this study monospecific antibodies against the S-100 alpha and beta subunits were used to characterize the S-100-like immunoreactivity in the rat kidney: Certain cells in the distal nephron, i.e., the connecting piece, collecting ducts, and the thin limb of Henle's loop, contained S-100 alpha immunoreactivity. Proximal tubules, the thick ascending limb of Henle's loop, the distal tubules, and the juxtaglomerular apparatus were negative. No S-100 beta immunoreactivity was found in kidney tubules. However, Schwann cells of renal pelvic nerves contained S-100 beta immunoreactivity. The presence of S-100 alpha antigen in certain cells of the kidney gives further support to the assumption that the alpha subunit of S-100a is related to cells that are highly involved in pH, electrolyte, and water regulation.


Subject(s)
Biomarkers , Kidney Tubules/analysis , S100 Proteins/analysis , Animals , Humans , Immunoenzyme Techniques , In Vitro Techniques , Kidney Cortex/analysis , Male , Nerve Growth Factors , Rats , Rats, Inbred Strains , S100 Calcium Binding Protein beta Subunit , Sublingual Gland/analysis
5.
J Histochem Cytochem ; 32(8): 805-14, 1984 Aug.
Article in English | MEDLINE | ID: mdl-6747272

ABSTRACT

In the rat, the S-100 antigens in the submandibular gland were found to be immunochemically identical with those in the brain (glial cells) when compared using crossed immunoelectrophoresis. Specific antibodies against the S-100a non-beta and against the S-100 beta subunit were prepared from antibodies against crude S-100 protein and from S-100 components (S-100a and b) by affinity chromatography. In the rat salivary glands a differential distribution of subunit immunoreactivity was clearly evidenced using indirect immunofluorescence. Certain intercalated duct cells of the submandibular gland as well as Schwann cells contained the S-100 beta subunit immunoreactivity exclusively, while other duct cells in parotid, submandibular, and sublingual glands contained S-100a non-beta subunit immunoreactivity. Both subunits were present in astrocytes and ependymal cells. The immunocytochemical localization of alpha and beta subunits is a promising technique for the classification of various types of S-100-containing cells.


Subject(s)
Biomarkers , Brain Chemistry , S100 Proteins/analysis , Salivary Proteins and Peptides/analysis , Animals , Male , Nerve Growth Factors , Rats , Rats, Inbred Strains , S100 Calcium Binding Protein beta Subunit
6.
J Neurosci Res ; 11(1): 1-11, 1984.
Article in English | MEDLINE | ID: mdl-6368851

ABSTRACT

The time course of tissue content and evoked release of endogenous amino acids was analyzed in the partially deafferented dentate gyrus of the rat hippocampus 2-24 days following unilateral lesion of the perforant path. Amino acids in tissue extracts and perfusates were determined after precolumn derivatization and hplc separation. The astrocytic glial cell reaction was monitored with immunohistochemistry of S-100. The tissue content of glutamate decreased significantly on the lesioned side, whereas only a moderate reduction in taurine, aspartate, and alanine occurred. Glutamine was significantly elevated at 7 days. The evoked efflux of glutamate was reduced at 2 and 7 days, whereas no change was seen at longer survival periods. The evoked release of GABA and aspartate increased on the denervated side after 12 and 24 days. The rate of carbon utilization into amino acid pools was followed with 14C-glucose and 14C-acetate. The incorporation of acetate showed a peak 2-9 days following lesion, which paralleled in time the hypertrophic glial cells. The incorporation of glucose decreased during this period. The metabolic events are discussed in relation to the morphological changes in synapses and glial cells.


Subject(s)
Amino Acids/metabolism , Hippocampus/metabolism , Neuroglia/metabolism , Acetates/metabolism , Amino Acids/analysis , Animals , Carbon Radioisotopes , Fluorescent Antibody Technique , Glucose/metabolism , Hippocampus/analysis , Hippocampus/cytology , Histocytochemistry , Male , Neurons/analysis , Potassium Chloride/pharmacology , Rats , S100 Proteins/analysis
9.
Infect Immun ; 23(3): 743-50, 1979 Mar.
Article in English | MEDLINE | ID: mdl-457257

ABSTRACT

Methods for light and electron microscopic identification and characterization of intestinal cholera antitoxin-containing cells (ACC) using peroxidase-labeled immunoreagent are described and used to study the ACC response in mice after immunizations with cholera toxin. Specific ACC appeared in significant numbers after two oral immunizations and increased six- to eightfold with two additional oral boosters, whereas further oral immunizations caused no additional stimulation. Intravenous immunizations had to be repeated seven times before ACC could be detected. After two oral immunizations, most of the ACC were found in the proximal part of the small intestine and no ACC were seen in the colon. This uneven distribution of ACC within the small intestine was eliminated after four oral immunizations, when ACC could also be detected in the colon. The ACC response after four oral immunizations demonstrated a peak at 4 days with far fewer cells present at 2 and 7 days. Electron microscopic studies showed that the ACC were mature plasma cells with the staining localized to the endoplasmic reticulum. Regression analysis of the relationship between the number of ACC and the magnitude of protective immunity against intestinal challenge with cholera toxin indicates a highly significant correlation (r = 0.91, P less than 0.001).


Subject(s)
Antitoxins , Cholera Toxin/immunology , Immunity , Intestinal Mucosa/immunology , Animals , Female , Immunization , Immunization Schedule , Intestinal Mucosa/cytology , Intestinal Mucosa/ultrastructure , Intestine, Small/immunology , Jejunum/immunology , Male , Mice , Plasma Cells/immunology
10.
J Histochem Cytochem ; 26(12): 1053-6, 1978 Dec.
Article in English | MEDLINE | ID: mdl-32212

ABSTRACT

Horseradish peroxidase was reacted with glutaraldehyde under various reaction conditions. The reaction product was, in a second step, bound covalently to aminohexyl groups attached to Sepharose particles. The influence of pH, time and the concentration ratio of enzyme:glutaraldehyde on the reaction was evaluated. A first step reaction with 100-fold molar excess of glutaraldehyde to horseradish peroxidase at pH 9.5 for 2 hr at room temperature results in a high yield of conjugated enzyme with well preserved enzymatic activity.


Subject(s)
Aldehydes/metabolism , Glutaral/metabolism , Histocytochemistry , Horseradish Peroxidase/metabolism , Peroxidases/metabolism , Hydrogen-Ion Concentration , Temperature
11.
J Histochem Cytochem ; 26(5): 412-4, 1978 May.
Article in English | MEDLINE | ID: mdl-96177

ABSTRACT

A new method for the study of glutaraldehyde reactions with proteins is presented. Glutaraldehyde-reacted protein is in a first step isolated and then in a second step reacted with aminohexyl groups bound to Sepharose particles. This reaction is linear at low protein concentrations and proceeds rapidly when proteins are reacted with 100-fold and 1000-fold molar excess of glutaraldehyde. This method enables the study of glutaraldehyde-induced crosslinking properties of the modified proteins as an isolated property with high reliability.


Subject(s)
Aldehydes , Amino Acids , Glutaral , Proteins , Amines , Chemical Phenomena , Chemistry , Horseradish Peroxidase , Proteins/isolation & purification , Sepharose/analogs & derivatives
13.
J Neurol Sci ; 35(2-3): 381-90, 1978 Feb.
Article in English | MEDLINE | ID: mdl-632841

ABSTRACT

The distribution of the 14-3-2 protein in rat brain was investigated by immuno-electron microscopy using antiserum to the protein conjugated with peroxidase. 14-3-2 was demonstrated in the nuclear membrane, the endoplasmic reticular membranes and in the plasma membrane of nerve cells. The protein was also localized to the presynaptic densities and to the pre- and postsynaptic membranes. It could not be demonstrated in the membranes of the Golgi complex, inner membrane of mitochondria or in the nucleoplasm of neurons. No 14-3-2 protein was found in astrocytes, oligodendrocytes or in non-neuroectodermal tissue elements.


Subject(s)
Brain Chemistry , Nerve Tissue Proteins/analysis , Animals , Cell Membrane/analysis , Endoplasmic Reticulum/analysis , Male , Neurons/analysis , Nuclear Envelope/analysis , Rats , Synaptic Membranes/analysis
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