Jürgen Roth

Physikalisch-Technische Bundesanstalt

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Margit Pavelka

Medical University of Vienna

Rodney J. Scott

University of Newcastle Australia

Zuzana Dobbie

Roche (Switzerland)

X. Llopart

European Organization for Nuclear Research

R. Behrens

Physikalisch-Technische Bundesanstalt

O. Hupe

Physikalisch-Technische Bundesanstalt

Dennis Haag

Friedrich-Alexander-Universität Erlangen-Nürnberg

R Ammann

University College London

Christian Fuhg

Physikalisch-Technische Bundesanstalt

P. Hufschmidt

Friedrich-Alexander-Universität Erlangen-Nürnberg

Cooperative Institutions

University of Zurich

University Hospital of Zurich

University of Basel

Friedrich-Alexander-Universität Erlangen-Nürnberg

Kantonsspital Baselland

University Hospital of Basel

European Organization for Nuclear Research

Friedrich Schiller University Jena

Physikalisch-Technische Bundesanstalt

University of Geneva

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Applications of immunocolloids in light microscopy. II. Demonstration of lectin-binding sites in paraffin sections by the use of lectin-gold or glycoprotein-gold complexes.

Journal of Histochemistry & Cytochemistry (1983)

Jürgen Roth

A new procedure is presented for the light microscopic demonstration of specific sugar sequences of oligosaccharides in glycoconjugates by lectins combined with the colloidal gold marker system. Tissue sections from aldehyde-fixed and paraffin embedded rat kidney were stained either in a one-step method with lectin directly bound to particles of colloidal gold or in a two-step method using non-labeled lectin and glycoprotein labeled with colloidal gold. In both methods the presence of lectin-binding sites in the tissue sections is revealed by the appearance of a red coloration that is due to the accumulation of gold particles. The high specificity of the technique is combined with a good sensitivity and resolution as demonstrated by a differential plasma membrane staining in renal epithelial cells. The lectin-gold or glycoprotein-gold complexes remain stable for months and produce a permanent nonbleaching staining.

Glycoconjugate

10.1177/31.4.6186737

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Citations (47)

VITAMIN-D-DEPENDENT CALCIUM BINDING PROTEIN CONTENT IS REDUCED IN KIDNEYS OF JUVENILE-ONSET DIABETICS

The Lancet (1982)

Lelio Orci Dennis Brown Jürgen Roth A. W. Norman

10.1016/s0140-6736(82)91723-8

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Citations (9)

Nerve Tissue and Disorders

Functional Ultrastructure (2015)

Margit Pavelka Jürgen Roth

Providing the base for the most sophisticated functions and tasks of the body, including memory and creativity, the tissue of the nervous system has attracted the greatest attention from the earliest days of microscopy to the present. The complex functional processes in the central and peripheral parts of the nervous system are continuously topics in the life sciences and medical research. The identification and characterization of neural stem cells within certain areas of the adult brain has revolutionized our knowledge and understanding of adult neurogenesis, and has increased hopes for possible treatment and repair of damage resulting from injuries or degenerative diseases.

10.1007/978-3-7091-1830-6_29

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Epithelium of the Respiratory Tract

Functional Ultrastructure (2015)

Margit Pavelka Jürgen Roth

The upper part of the respiratory tract functions as an air-conducting system. Here, warming and moistening of the inhaled air and removal of inhaled particles occurs. It is lined by the pseudostratified respiratory epithelium, which consists of four cell types: (1) columnar ciliated cells, which possess cilia that project from their apical plasma membrane and function in the autonomous, coordinated movement of luminal content; (2) goblet cells (MC in a), unicellular glands synthesizing and secreting mucus, forming part of the mucus blanket, which functions as a lubricant and a protective layer; (3) a small number of neuroendocrine cells (also referred to as Kultschinsky cells), dispersed in the epithelium; and (4) basal cells, which function as stem cells for the regeneration of the respiratory epithelium.

Respiratory tract

10.1007/978-3-7091-1830-6_18

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Immunohistochemical localization of polysialic acid in tissue sections: differential binding to polynucleotides and DNA of a murine IgG and a human IgM monoclonal antibody.

Journal of Histochemistry & Cytochemistry (1990)

Matthias Husmann Jürgen Roth Elvin A. Kabat C. Weisgerber Matthias Frosch

For immunolocalization of alpha(2-8)-linked polysialic acid, which forms part of the neural cell adhesion molecule (N-CAM), two monoclonal antibodies, MAb735 and IgMNOV, were employed. Both antibodies have previously been shown to bind the extremely low immunogenic capsular polysaccharide of group B meningococci, which also consists of alpha(2-8) polysialic acid, but not to other, even closely related forms of polysialic acid. Despite the identical polysaccharide specificity of these two MAb, we observed marked differences of the staining pattern in tissue sections. We showed that these differences in immunostaining were due to the crossreactivity of IgMNOV with polynucleotides and DNA. MAb735, however, was shown to react exclusively with alpha(2-8) polysialic acid. Moreover, the specificity of MAb735 proved to be unique among eleven other MAb directed against various bacterial polysaccharides, as it was the only one unreactive with polynucleotides. Thus, MAb735, the only IgG type mouse monoclonal antibody to polysialic acid thus far reported, can be considered a specific probe for the unambiguous detection of alpha(2-8) polysialic acid in tissue sections, and should therefore help to further elucidate the role of polysialic acid in developmental processes.

Polysialic acid

Immunostaining

Polynucleotide

10.1177/38.2.1688896

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Citations (28)

Invited commentary

Diseases of the Colon & Rectum (2001)

James M. Church Irene Guldenschuh R Hürlimann Andreas Müller R Ammann

Church, James M. M.D.; Guldenschuh, Irene M.D.; Hurlimann, Rainer M.D.; Muller, Andreas M.D.; Ammann, Rudolf M.D.; Mullhaupt, Beat M.D.; Zala, Gian-Franco M.D.; Flury, Renata M.D.; Seelentag, Walter M.D.; Roth, Jurgen M.D.; Meyenberger, Christa M.D.; Fried, Michael M.D.; Hoppeler, Thomas M.D.; Dobbie, Zuzana Ph.D.; Spigelman, Allan D. M.B., B.S., M.D. F.R.C.S., F.R.A.C.S.; Scott, Rodney J. B.Sc.(Hons), Ph.D., P.D. Author Information

Colorectal Surgery

Surgical oncology

10.1007/bf02234628

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Analytical study of fabry's disease

Virchows Archiv A Pathological Anatomy and Histology (1974)

Jürgen Roth E. Schulze G Raabe G. Waldmann

10.1007/bf00432808

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Citations (8)

Mott cells are plasma cells defective in immunoglobulin secretion

European Journal of Immunology (1985)

A. Alanen Ulla Pira Olli Lassila Jürgen Roth Richard M. Franklin

Plasma cells containing intracellular inclusions of immunoglobulin (Russell bodies) are known as Mott cells, and are found in large numbers in lymphoid organs in autoimmune mice. Hybridoma technique was used to produce cell lines of this phenotype by fusing spleen cells from a NZB mouse with a nonproducing hybridoma cell line (Sp2/0-Ag14), allowing us to carry out studies of this cell type at the biochemical level. Ultrastructurally the inclusions were distended cisternae of rough endoplasmic reticulum, suggesting a block in the secretory pathway of the cells. Biosynthetic labeling studies confirmed that these cell lines have either a complete or partial block of secretion of immunoglobulin, possibly due to an abnormal light chain.

10.1002/eji.1830150306

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Citations (65)

Post‐embedding cytochemistry with gold‐labelled reagents: a review

Journal of Microscopy (1986)

Jürgen Roth

SUMMARY The detection of antigens and glycoconjugates with the protein A–gold and the lectin–gold techniques, respectively, is reviewed. Special attention is directed to the necessary conditions for fixation and embedding as well as to the staining procedures of tissue sections for light and electron microscopy.

Cytochemistry

Glycoconjugate

10.1111/j.1365-2818.1986.tb02771.x

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Citations (134)

Cystinosis

Functional Ultrastructure (2010)

Margit Pavelka Jürgen Roth

This is an autosomal recessively inherited, rare disorder of lysosomal membrane transport. The defect lies in the carrier-mediated transport of cystine across the lysosomal membrane. The cystinosis gene, CNTS, is located on chromosome 17pl3, transcribes a 2.6 kb mRNA that codes for the 367 amino acid long cystinosin, which is a polytope membrane protein. Most cystinosis patients from northern Europe are homozygous for a 57 kb deletion extending from exon 10 upstream. The disease is characterised by the accumulation of free cystine in lysosomes (10 to 100 times the normal lysosomal amount), which then forms crystals (asterisks in panel B). These crystals, which can be observed in the lyso-somes of many tissues, lead to a progressive damage of lysosomes. Rectangular cystine crystals are birefringent. The disease manifests mainly in the kidney and causes the renal tubular Fanconi syndrome and glomerular damage requiring dialysis or transplantation. An elevated cystine content in leukocytes of peripheral blood is diagnostic.

Cystinosis

Fanconi syndrome

Lysosomal storage disease

10.1007/978-3-211-99390-3_64

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