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Biomedical subjects

K Kühn

Publications and source records attributed to K Kühn.

At least 127 records · Page 7Linked to original sources
PubMed1982

[Malignant hyperthermia. Current aspects of dantrolene treatment of 2 cases of hyperthermia maligna incipiens].

During induction with volatile anaesthetic agents and succinylcholine (suxamethonium) both children showed a singular clinical symptom: trismus. In the first case(1) narcosis had been interrupted followed by clinically controlled recovery. One week later, after treatment with oral dantrolen (Dantamacrin), anaesthesia with triggerfree agents was performed without complications. In the second case (2) anaesthesia has been continued by using triggerfree agents. Both children showed significant increases of Creatin-Kinase-activities over 5000 U/l after the interrupted narcosis (1) and postoperatively as being typical biochemical parameters for incipient hyperthermia maligna. All other parameters were normal. A review is given on the use of dantrolene-sodium, its development and its use in our department as lifesaving agent in malignant hyperthermia.

Child↗
PubMed1982

[Possible patient overheating by OP-table heating equipment].

The technical equipment used in the operation theatre must be safe and foolproof. We observed a complication of near overheating a patient using the thermomaquet heating pads. The conclusion of our observation is that such heating pads must have a high-temperature cut-off device.

Burns↗
PubMed1981

A network model for the organization of type IV collagen molecules in basement membranes.

Type IV collagen was solubilized from a tumor basement membrane either by acid extraction or by limited digestion with pepsin. The two forms were similar in composition and the size of the constituent chains but differed when examined by electron microscopy and in the fragment pattern produced by bacterial collagenase. The acid-soluble form showed after rotary shadowing strands mainly of a length of 320 nm which terminated in a globule, or two strands connected by a similar globule. The globule was identified as a non-collagenous domain (NC1) which under dissociating conditions could be separated into two peptides showing a monomer-dimer relationship. Higher aggregates of NC1 were visualized under non-dissociating conditions. Some of the acid-extracted molecules have retained the previously 7-S collagen domain. The pepsin-solubilized form lacked domain NC1 and consisted mainly of four triple-helical strands (length 356 nm) joined together at the 7-S domain (length 30 nm). Common to both forms of type IV collagen was a small collagenase-resistant domain NC2 which was composed of collagenous and non-collagenous elements and located between the 7-S domain and the major triple helix. These data indicate that the collagenous matrix of basement membranes consists of a regular network of type IV collagen molecules which is generated by two different interacting sites located at opposite ends of each molecule. The 7-S collagen domain connects four molecules while the NC1 domain connects two molecules. The maximal distance between identical cross-linking sites (7-S or NC1) was estimated to be about 800 nm comprising the length of two molecules.

Animals↗
PubMed1981

Glomerular basement membrane and mesangial matrix: a comparative study in different vertebrates.

Perfusion fixation of the rat kidneys with aldehydes and alcian blue demonstrates within the glomerular mesangium various components displaying anionic binding sites. These are the surface coat of the mesangial cells, numerous mesangial microfibrils (probably glycoproteins), and polygonal particles (Presumably proteoglycans). These particles lie close to the mesangial cells and form assemblies of various extension within the mesangial matrix as well. In addition, a discontinuous basement membrane can be recognized which surrounds the mesangial cells. In the hagfish glomeruli (fixed without cationic dye), a prominent layer of microfibrils is interposed between mesangial and endothelial cells. Both these cells show incomplete basement membranes.

Animals↗
PubMed1981

Glomerular permeability for proteins of high molecular weight entrapped in liposomes.

The glomerular filtration barrier is known to be negatively charged. Previous experiments have shown the importance of the electrical charge for permeability. We looked for permeability characteristics of proteins entrapped in liposomes with negative and positive charge detecting that the positive charge enables the protein to pass the glomerular filtration barrier.

Animals↗
PubMed1981

Glomerular podocyte cell junctions in nephrotic syndrome. I. Freeze-fracture studies in rat aminonucleoside nephrosis.

Aminonucleoside nephrosis was induced in rats after a single i.p. injection of puromycin aminonucleoside (PAN). Freeze-fracture studies of the glomeruli were done, three, six and ten days after PAN injection. The epithelial filtration slits disappeared six days after PAN injection. On the split plasma membrane of the podocytes three types of cell junctions which apparently were newly formed were seen: 1) single strands (occluding junctions of leaky type); 2) networks of limited extent, composed of strands and particles (maculae occludentes); 3) assemblies of particles or pits (maculae communicantes) connected by single strands. The cell junctions of podocytes were comparable with those found in human nephrotic syndrome. (Kühn et al., 1981).

Animals↗
PubMed1981

Glomerular podocyte cell junctions in nephrotic syndrome. II. Freeze-fracture studies in human nephrotic syndrome.

In six patients with nephrotic syndrome and in two control subjects freeze-fracture studies of isolated glomeruli obtained by needle biopsies were performed. In the nephrotic patients replicas of freeze-fractured podocytes showed an increased number of cell junctions. These were represented by incomplete occluding junctions and communicating junctions (gap junctions). There was morphologically a similarity between the glomerular podocyte cell junctions in human and experimental nephrotic syndrome (Kühn et al., 1981).

Adolescent↗
PubMed1979

Amino acid sequence of the aminoterminal segment of dermatosparactic calf-skin procollagen type I.

The N-terminal procollagen peptide of the pN alpha 1(I) chain from dermatosparactic calf skin contains 139 amino acid residues. For the determination of the amino acid sequence the procollagen peptide was treated with pyroglutamate aminopeptidase, protease from Staphylococcus aureus V8 and trypsin. The fragments obtained were separated by molecular sieve and ion-exchange chromatography and submitted to automated Edman degradation. The procollagen peptide consists of three segments, an N-terminal globular domain which contains all the cysteine residues and most of the hydrophobic residues present in the entire peptide, a triple helical part with a relatively high content of proline and hydroxyproline, and a short nonhelical region which forms the connection to the nonhelical region of the alpha 1(I) chain and which contains the proline-glutamine bond specifically split by the N-terminal procollagen peptidase during conversion of procollagen to collagen.

Amino Acid Sequence↗