Ekkehard Kallee

Bennhold's analbuminemia: A follow-up study of the first two cases (1953–1992)

A pair of siblings with analbuminemia were followed for 38 years. The female patient received replacement therapy with human serum albumin. Extreme lipodystrophy developed in this patient by the fourth decade of life. She had juvenile osteoporosis, which normalized under albumin replacement. She died from a granulosa cell cancer at age 69. Her brother never received albumin, even though his serum contained only 60 micrograms/ml of an albumin-like protein. He suffered from severe osteoporosis with gibbus formation, and he died from a colon carcinoma at age 59. Despite high cholesterol values and high levels of several blood clotting factors, neither of the patients had severe atherosclerosis or thrombotic events. Laboratory findings before and after infusion of large amounts of albumin into the sister point to a mechanism whereby albumin-bound substances can be passively transported from the bloodstream into the extravascular space and vice versa.

Inhibitory and disruptive effects of some antirheumatics on antigen-antibody complexes

Purified antibodies to human serum albumin or to human gamma-globulin were used to study the direct influence of some antirheumatic drugs on the formation and disruption of immunoprecipitates. 125I-labelled human serum albumin and 125I-labelled human IgG served as indicators. The effects of the following drugs were described: diclofenac, monophenylbutazone, diphenylbutazone, ibuprofen, and metamizol. At approximately therapeutic concentrations, the antirheumatics inhibited the formation of complexes of homologous antibodies with human serum albumin and, surprisingly, with human IgG. When the antigens were precipitated with antibodies, subsequent addition of the antirheumatics to the preformed immunoprecipitates caused disruption of [125I]human serum albumin-anti-human serum albumin precipitates but practically no disruption of human [125I]IgG-anti-human IgG precipitates. These new findings may be of relevance for clinical diagnosis and therapy as well as for research in immunochemistry. It is conceivable that, in patients, antirheumatic or other drugs might interfere with immunological determinations of clinico-chemical quantities. Interference of drugs with antigen-antibody reactions might also help to explain some beneficial effects or undesirable side effects of certain drugs.

Einfluß verschiedener Medikamente auf die Bindung von Schilddrüsenhormonen an Lebermitochondrien / Influence of Various Drugs on the Adsorption of Thyroid Hormones to Liver Mitochondria

Abstract 1. [131I] ʟ-thyroxine (T4) or [131I] ʟ-triiodothyronine (T3) was added in 50 pᴍ - 25 nᴍ and 26 pᴍ -132 nᴍ concentrations to suspensions of rat liver mitochondria. In distribution equilibria between soluble proteins and mitochondria the adsorption of the thyroid hormones to the mito chondria followed an approximately linear function when the radioactive hormones were added within the range of physiological concentrations. At identical protein concentrations T3 was adsorbed to the mitochondria one tenth more strongly than T4 when neither serum proteins nor cell sap had been added. The adsorption of both T3 and T4 to mitochondria and soluble proteins is reversible. The distribution of the thyroid hormones between organelles and soluble proteins depends on the ratio of the protein concentration in the sedimented mitochondria to the protein concentration in the supernate after centrifugation. The desorption of T3 and T4 from the mito chondria by soluble proteins, however, represents no linear function. 2. The distribution equilibria of simultaneously added 131I -T4 and 125I -T3 can be shifted by certain drugs. Chlorpromazin and dinitrophenol displaced the thyroid hormones from their binding to soluble proteins onto the mitochondria. Vice versa, phenylbutazone, phenytoin, brom-sulfalein and silymarin displaced the hormones from the mitochondria more strongly than from soluble proteins. Sodium oleate displaced the hormones in both directions. Minor shifting effects or none at all could be detected when several other drugs were used. The described procedure apparently yields new information on some effects of drug action

131J-Serumproteine und Schilddrüse

As shown in experiments on the half life of radioiodinated serum in rabbits, trace-iodinated serum proteins are not directly desiodinated by the organism in the presence of excessive diiodotyrosine. iodide, or thyroxine. The half life of 131I-Serum proteins depends on the hormonal action of the thyroid rather than on a direct desiodination of 131I-proteins.