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cryoglobulinemia/carbohydrate

Krækjan er vistuð á klemmuspjaldið
GreinarKlínískar rannsóknirEinkaleyfi
11 niðurstöður

Nature of cryoglobulinaemia.

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Cryoimmunoglobulins seem to differ from non-cryoimmunoglobulins in not having carbohydrate groups, most probably sialic acid residues. It is proposed that cryoimmunoglobulinaemia is a physiological event and that desialylated immunoglobulins are a normal byproduct of the immune system. The rise in

Chemical analysis of cryoglobulins observed in a case of essential IgG-IgA cryoglobulinaemia.

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In a case of essential mixed (IgG-IgA) cryoglobulinaemia the carbohydrate and aminoacid composition of cryoglobulins was chemically analyzed. A normal aminoacid and sialic acid composition was observed, whereas the glucide percentage was augmented with respect to the normal range for the two classes

Cryoglobulinemia in a patient with Sjögren's syndrome, and factors of cryoprecipitation.

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The IgGK cryoglobulin in a patient with Sjögren's syndrome showed deviations from normal IgG involvine its amino acid composition as well as its carbohydrate components. The heavy chains showed abnormal numbers of arginine, threonine, valine and isoleucine residues, and there was an impressive

Fibronectin, Cryoglobulinemia and Immune Complexes in Sjogren's Syndrome Patients.

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The problem of proper diagnosis, patient's status and disease progression is very actual for autoimmune diseases. Still the diagnosis of Sjogren's syndrome is more state of art than of science. Our preliminary investigations showed that serum fibronectin of elevated molecular weight may be probably

Dermic peripheral microangiopathy in plasmo-proliferative disorders.

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Skin biopsy specimens from 12 patients with plasmo-proliferative disease (myeloma and macrogobulinemia) were histopathologically and histochemically examined. In all the cases studied (by a biopsy obtained from the hand) there were alterations in the dermal microvasculature characterized by

Preexisting human anti-murine immunoglobulin reactivity due to polyclonal rheumatoid factors.

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We report that sera from healthy controls, patients with ovarian or lung cancer, and patients with rheumatoid arthritis all contain IgM polyclonal rheumatoid factors which recognize antigenic determinants on murine and to a greater extent human immunoglobulin IgG. The major part of this reactivity
The perfusion of polymeric or secretory IgA-Concanavalin A complexes into the aorta of rats led to a mannose-dependent binding of both IgA and lectin to the glomerular capillary wall, as shown by double immunolocalization experiments, by quantitative analysis of the amount of radiolabelled complexes
A 75-year-old man with no known previous liver disease was admitted to our institution because of right pleural effusion, backache, and pain in the upper right quadrant. Physical and laboratory work-up revealed decompensated liver cirrhosis. Spiral computed tomography (CT) showed a 6-cm tumour in

Inhibtion of cold insolubility of serum cryoglobulin by epsilon aminocaproic acid.

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Cold-induced insolubility of serum cryoglobulins can be inhibited by various carbohydrates and aminocarboxylic acids. Among the inhibitors, Epsilon amino caproic acid (EACA) was found to be effective at therapeutic levels in a patient who had mixed-type cryoglobulinemia. In vivo administration of

Importance of the IgG isotype, not the state of glycosylation, in determining human rheumatoid factor binding.

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We investigated the influence of carbohydrate on the binding of human rheumatoid factors (RF) to the Fc fragment of IgG. The monoclonal RF studied were derived from the serum of patients with mixed cryoglobulinemia or from hybridomas generated from patients with rheumatoid arthritis (RA) and

Cryoglobulins and pyroglobulins: an overview.

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Cryoglobulins are serum proteins with heterogeneous etiopathogenetic and immunochemical properties. What they have in common is temperature-dependent insolubility, in that at temperatures below 37 degrees C (often around 4 degrees C) they precipitate, and then redissolve at 37 degrees C. When the
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