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Biomedical subjects

R P Linke

Publications and source records attributed to R P Linke.

At least 145 records · Page 8Linked to original sources

Antigenic difference between serum amyloid protein SSA and its low molecular weight derivative SAAL revealed by an anti-amyloid A antiserum at different temperatures.

Serum amyloid protein SAA and its low molecular weight derivate SAAL have been compared in immunodiffusion with an antiserum to amyloid A at different temperatures. At room temperature or at 37 degree C SAAL and SAA did precipitate with anti-AA forming a line of identity. At 4 degrees C, however, only SAAL did react with anti AA. Experiments are described which show that the SAA-derivative SAAL has AA-related antigenic determinants exposed whereas these determinants are hidden in the parent SAA and are only exhibited as result of an unknown temperature-dependent process. Therefore, SAAL can also be distinguished from SAA by the availability of AA-related antigenic determinants for anti-AA antibodies at 4 degrees C.

Amyloid↗

[Hairy cell leukemia. Characterization of the leukemic cell: surface immunoglobulins, Fc-receptors and stimulation by mitogens (author's transl)].

In four patients with hairy cell leukemia the expression of surface immunoglobulins and Fc-receptors on the leukemic cells as well as the stimulation of the leukemic cells by various T- and B-cell mitogens was studied. Using a combined cytochemical radioautographic method the tartrate resistant isoenzyme of the acid phosphatase and immunological markers could be demonstrated simultaneously on single cells. Surface immunoglobulins were detected by 125I-labelled (Fab')2-fragments of monospecific anti-heavy-chain-antibodies. In two patients only mu- and delta-determinants were found on the isoenzyme-positive hairy cells; in one patient 86% and in the other 44% of these cells carried both heavy chains on the same cell. Another patient showed both gamma- and delta-chains on the isoenzyme-positive cells and the fourth patient gamma-chains only. When the hairy cells of one patient were cultured in vitro in human serum-free medium for 14 days, mu- and delta-determinants were found just as on freshly isolated cells suggesting that hairy cells synthesize immunoglobulins. By indirect immunofluorescence the surface-Ig on hairy cells was shown to be capped very rapidly at room temperature. The concentrated surface-Ig was found over that cytoplasmic area where most of the ingested latex particles were located. In addition, using 125I-labelled aggregated human IgG (M.W. 5-15 X 10(6)), Fc-receptors were found on virtually all of the isoenzyme-containing hairy cells in all four patients. Furthermore, a distinct, low-degree stimulation of the isoenzyme-positive hairy cells could be demonstrated when the cells were cultured in the presence of pokeweed mitogen or Lima-bean lectin (B- and T-cell-mitogens), whereas no stimulation was observed by phytohemagglutinin and concanavalin A (T-cell-mitogens). In three patients studied, isoenzyme-positive hairy cells were negative with regard to rosette formation with sheep erythrocytes.

Acid Phosphatase↗

[Fc receptors and surface immunoglobulins in cells of hairy cell leukemia].

Using 125I-labelled aggregated IgG in a quantitative assay a strong expression of Fc-receptors was found on the leukemic cells of a patient with hairy cell leukemia. The Fc-receptor activity on these cells was much higher than that on monocytes and B-lymphocytes from normal blood. Surface immunoglobulins were detected by radioautography using radioactively labelled (Fab')2-fragments of monospecific antibodies directed against immunoglobulin heavy chains. Prior to radioautography the cells were stained for the tartrate resistant acid phosphatase. It was found that all cells containing this enzyme bore sigma-chains on their surface. On more than 90% of these cells a simultaneous expression of mu-chains was detected. gamma-Chains could only be demonstrated on cells which were negative for the tartrate resistant acid phosphatase; part of these cells, however, were hairy cells by morphological criteria.

Acid Phosphatase↗

Isolation of a low-molecular-weight serum component antigenically related to an amyloid fibril protein of unknown origin.

An amyloid fibril protein of unknown origin from a patient with systemic amyloidosis has been purified to homogeneous charge and size by gel filtration and two step isoelectric focusing. From crude antisera to the initial heterogeneous fibril protein, monospecific antibodies have been obtained by immunoabsorption with the immobilized purified amyloid protein. These antibodies have been used to identify an antigenically related serum component in whole sera of patients with and without amyloidosis. Chromatography on Sephadex G-200 in phosphate buffered saline of a patient's whole serum yields a component with an apparent molecular weight of approximately 200,000. Guanidine denaturation of this high-molecular-weight serum component followed by Sephadex G-100 column chromatography in 5 M guanidine affords an antigenically reactive protein with an apparent molecular weight of about 12,500. The antigenic similarity and molecular weight of the latter protein indicates that it could act as the smallest serum precursor of the tissue fibril protein in this group of cases of amyloidosis.

Amyloid↗

Immunoglobulin D myeloma and amyloidosis: immunochemical and structural studies of Bence Jones and amyloid fibrillar proteins.

Urinary Bence Jones protein and amyloid fibril protein isolated from the subcutaneous tissue of a patient with IgD myeloma and associated amyloidosis were subjected to physicochemical and immunochemical identification. Peptide maps and amino-terminal tetrapeptide composition obtained from the two proteins were comparable. Immunochemical cross-reactivity between the two proteins, with other lambda-type amyloid and Bence Jones proteins, and with a serum component was demonstrated. The results suggest that the source of the amyloid fibril protein is an intact circulating light polypeptide chain as well as smaller amino-terminal fragments.

Aged↗

Transthyretin Leu 68 in a form of cardiac amyloidosis.

A form of transthyretin (TTR)-related cardiac amyloidosis was previously described in a German patient. Electrophoretic analysis of plasma TTR showed the presence of an electrically neutral variant. We have now characterized the variant transthyretin by comparative peptide mapping, aminoacid and DNA sequencing procedures. A new mutation in TTR with a substitution of leucine for isoleucine at position 68 of the monomer is described.

Amino Acid Sequence↗