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Biomedical subjects

J R Moor

Publications and source records attributed to J R Moor.

8 recordsLinked to original sources
PubMed1981

Ceruloplasmin assays in diagnosis and treatment of human lung, breast, and gastrointestinal cancers.

Ceruloplasmin was assayed as enzyme activity, as antigen, and as total copper in serum samples from 150 male lung cancer patients and comparable numbers of male controls. By all three assays, ceruloplasmin was significantly increased above the normal before treatment, and the degree of elevation was related to TNM stage [i.e., the International Union Against Cancer classification system based on extent of primary tumor (T), condition of lymph nodes (N), and absence of presence of metastases (M)]. Surgery had no immediate effects, but in patients who evidence of disease for longer periods, ceruloplasmin returned to nearly normal values. High levels of ceruloplasmin was elevated in 6 of 9 patients before tumor recurrence; 2 of 3 smokers (in the first panel of sera) with elevated ceruloplasmin levels subsequently developed lung cancer. The relative merits of the three assays were compared. Some sex- and age-related differences among normal controls were apparent. The results of pilot studies on men with gastrointestinal cancer and women with breast cancer are presented. It is concluded that only in limited situations will assays of ceruloplasmin aid in diagnosis, prognosis, and long-term monitoring of cancer patients.

Adult↗
PubMed1979

Copper regulation of ceruloplasmin in copper-deficient rats.

In copper-deficient rats, oral intubation of copper increases the rate of ceruloplasmin synthesis without affecting general synthesis of plasma or liver proteins. It also restores the enzyme from half to full activity. Copper given by injection at doses commonly employed has additional nonspecific effects on protein synthesis and in some strains of rats produces severe hemolysis. In contrast to deficient rats, in normal rats copper does not elevate plasma ceruloplasmin unless hemolysis also occurs. Thus, at least in deficiency, copper availability controls the rate of synthesis, acitvation, and plasma concentration of ceruloplasmin.

Animals↗
PubMed1977

Plasma ceruloplasmin. Evidence for its presence in and uptake by heart and other organs of the rat.

Evidence for the presence of the plasma protein, ceruloplasmin, in heart and other tissues of the rat was sought using various techniques. With p-phenylenediamine, ceruloplasmin-like oxidase activity was detected in heart post-mitochondrial and 100 000 X g supernatants in amounts far exceeding those that could be accounted for by residual blood. Much lower levels were detected in kidney, brain and liver. Oxidase activity of heart purified on DEAE-cellulose in the same way as rat plasma ceruloplasmin and behaved identically also in disc gel electrophoresis. The presence of ceruloplasmin in heart extracts was confirmed immunologically by Ouchterlony diffusion, using rabbit antibody raised against pure rat ceruloplasmin. When pure [3H]leucine-labeled ceruloplasmin was infused intravenously into a copper-deficient rat, radioactivity was concentrated in the heart and brain within 2 h; radioactive counts per g attained 11 and 3 times those of plasma in the two organs, respectively. A lesser concentration occurred in the liver. the results suggest that circulating ceruloplasmin (made by the liver) finds its way into the cells of some organs, especially the heart, a phenomenon which may be related to the function of ceruloplasmin to provide copper to the cytochrome oxidase of various tissues.

Animals↗
PubMed1975

Structural differences in ferritins from normal and malignant rat tissues.

Ferritins purified from several normal and malignant rat tissues were examined for amino acid composition, content of tryptic peptides, available sulfhydryl groups and subunit sizes and proportion. Ferritin extracted from adult kidney, neonatal liver and hepatic and renal tumors differed from the ferritin of adult rat liver in migration on electrophoretic gels and in antibody affinity, but did not differ among themselves. Nevertheless, they showed distinctive differences in amino acid composition and tryptic peptide content. All of them and also adult liver ferritin contained two major species of subunits differing in molecular weight. The proportions of subunits, and the available sulfhydryl groups of the intact ferritin molecules, differed among these tissue ferritins. On the basis of amino acid and peptide content, the ferritins of hepatomas and the renal tumor analyzed showec the greatest similarity but not identity. The ferritin of neonatal liver was next most similar. Kidney ferritin differed considerably in composition from tumor and neonatal ferritins, while adult liver ferritin was the most extremely divergent of the series examined. A similar progressive difference was found on examining the proportions of subunits and sulfhydryl groups in these ferritins. However, changes in subunit proportion cannot explain the amino acid and peptide compositional changes.

Amino Acids↗
PubMed1972

Prenatal and postnatal changes in the content and species of ferritin in rat liver.

The iron and ferritin content of rat liver and the species of ferritin present were examined from 4 days before to 3 weeks after birth. 1. Total iron and ferritin iron accumulated rapidly during the last days of gestation and from the second postnatal day underwent a steady depletion. 2. The amount of iron deposited before birth in the liver of each pup varied inversely with litter size and could be increased moderately by injection of iron into the mother before mating. 3. Intraperitoneal injection of iron 1 day after birth doubled the concentration of total iron, ferritin iron and ferritin protein in the liver over the next 24h, but at 3 weeks after birth it raised the very low concentrations of iron and ferritin severalfold. 4. As shown by electrophoretic migration, ferritin and dissociated ferritin subunits prepared from the livers of rats from 4 days before to 3 weeks after birth differed from those of adult liver ferritin and were indistinguishable from those of adult kidney and spleen ferritin. Treatment with iron at 3 weeks of age induced formation of a ferritin with electrophoretic properties resembling those of adult liver. It is concluded that iron given at this stage of development may activate the genetic cistron for adult liver ferritin.

Age Factors↗