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Biomedical subjects

F Liszt

Publications and source records attributed to F Liszt.

8 recordsLinked to original sources
PubMed2001

[Plasma electrolytes in multiple myeloma].

The plasma cell myeloma (multiple myeloma, myelomatosis) is a progressive disease, characterized by bone marrow plasmacytomas and the presence of monoclonal antibodies (IgG, IgA, IgD, IgE), or free kappa or lambda immunoglobulin side chains. The monoclonal antibodies or Bence-Jones protein may precipitate in the tubuli and impair kidney function. In addition, the plasma protein concentration may increase at the expense of plasma water level causing unrealistically low electrolyte levels. Since the isoelectric points of immunoglobulins are higher than those of most other plasma proteins, the net charge of plasma proteins may change causing new electrolyte balance. In addition, some monoclonal antibodies are more hydrated than others, and their high concentration may cause not only increased plasma viscosity but further electrolyte imbalance. In the present work the relationship between plasma protein and electrolyte levels is studied in samples of 100 multiple myeloma patients.

Blood Proteins↗
PubMed1992

Study of circulating immune complexes in atopic dermatitis.

The authors examined sera from 92 patients (78 adults, 14 children) with atopic dermatitis (AD), for the presence of circulating immune complexes (CIC). Using the PEG precipitation technique they found an increase in CIC total protein. In the quantity of precipitated proteins, elevated IgA and IgG levels and decreased C3 in CIC were measured. Neither the acute nor the subacute stage of the disease, nor skin involvement, correlated with CIC. In increased content of CIC was found in patients who had AD with associated disease recurrent infections, recurrent conjunctivitis, asthma, allergic rhinitis) and especially with pustulosis varicelliformis Kaposi, i.e. eczema herpeticatum. The T lymphocytes, together with other surface complement receptor-positive cells, are able to induce CIC production and keep them in solution.

Adult↗
PubMed1991

Composition of proteoglycan fragments from hyaline cartilage produced by granulocytes in a model of frustrated phagocytosis.

An in vitro model of frustrated phagocytosis was developed in which granulocytes interact with well-defined slices of hyaline cartilage. The composition of the purified proteoglycan fragments released from the cartilage slices by N-formyl-methionyl-leucyl-phenylalanine-stimulated granulocytes was studied after 30, 60 and 90 min incubation time. It was shown that the proteoglycan fragments do not change their composition during incubation. The only change observed during incubation was an increase in the quantity of the fragments. The protein content of the proteoglycan fragments is 7.0-8.6%, corresponding to a peptide chain of 24-28 amino acids, and the relative molecular mass of the total fragment is Mr = 37,600-39,200. On average, each proteoglycan fragment contains two chondroitin sulphate chains (Mr = 22,000-22,400), every fourth fragment contains a keratan sulphate chain (Mr = 7000-7200) and every seventh to eighth contains an O-glycosidic oligosaccharide, whereas no N-glycosidic oligosaccharide could be detected. The results of the disaccharide analysis show that the galactosaminoglycan chains contain 76.2-83.6% chondroitin 4-sulphate, 12.9-19.4% chondroitin 6-sulphate, 3.5-3.8% chondroitin and no dermatan sulphate. Since composition and relative molecular mass of the chondroitin sulphate and keratan sulphate chains from the proteoglycan fragments resemble those of native proteoglycans, the conclusion may be drawn that the degeneration of the proteoglycans occurs by proteases that attack preferably the chondroitin sulphate-rich region of the core protein. This is the first inflammation model of joint destruction, which demonstrates the elution of soluble specific proteoglycan degradation products of defined size.

Amino Acids↗
PubMed1990

Analysis of the proteolytic degradation products of hyaline cartilage proteoglycans.

The proteolytic degradation products of nasal hyaline cartilage proteoglycans produced by polymorphonuclear leukocyte lysosomal enzymes were investigated. The protein content of the degradation products is 7.0-8.6% corresponding to a peptide chain of 24-28 amino acids and the relative molecular mass of the total fragment is M(r) = 37,600-39,200. On an average, each proteoglycan fragment contains two chondroitin-sulphate chains (M(r) = 22,000-22,400), every fourth fragment contains a keratan sulphate chain (M(r) = 7000-7200) and every seventh to eighth contains an O-glycosidic oligosaccharide. The results of the disaccharide analysis show that the galactosaminoglycan chains contain 76.2-83.6% chondroitin-4-sulphate, 12.9-19.4% chondroitin-6-sulphate, 3.5-3.8% chondroitin and no dermatan sulphate. Since composition and relative molecular mass of the chondroitin sulphate and keratan sulphate chains from the degradation products resemble those from native proteoglycans, it is suggested that the degradation of the proteoglycans occurs by proteinases that attack preferably the chondroitin sulphate region of the core protein.

Amino Acids↗
PubMed1989

Luminol dependent chemiluminescence of quartz and zymosan stimulated neutrophils.

The effect of the opsonization by zymosan and quartz particles on the chemiluminescence was investigated on human neutrophil granulocytes. Opsonization of zymosan enhanced the chemiluminescence response, while opsonized quartz inhibited the chemiluminescence reaction. Calcium ionophore A 23187 treatment did not influence the chemiluminescence of quartz but the light signal in the presence of quartz decreased rapidly. In parallel experiments the protein pattern of zymosan treated neutrophils was investigated by high resolution two-dimensional polyacrylamide gel electrophoresis.

Blood Proteins↗