Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.16.3.1 (ceruloplasmin)
 5,074 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The Moore's hypothesis concerning a relationship between the metabolism of copper and that of vitamin A led us to consider a possible relationship between this vitamin and ceruloplasmin, the carrier protein for copper. Experiments were carried out on Sprague-Dawley rats. The ceruloplasmin level of control animals and vitamin A - deficient rats was determined An average increase between 22 and 33% was observed in the animals with vitamin A deficiency, the highest levels being observed in the females. These results are in agreement with Peterson's previous work. A second type of experiment was carried out to confirm these results. The rats were raised in a copper-deficient diet and the vitamin A level was regularly determined. In these conditions serum and liver levels of vitamin A are normal and do not vary, ceruloplasmin level is zero; however apoceruloplasmin is still being synthetized : Nevertheless at the ultime state of the deficiency vitamin A level decreases while apoceruloplasmin increases. These results raise the following question. Could the relationship between ceruloplasmin and vitamin A be possibly due to an inflammatory state in vitamin A deficient rats. In this respect a third series of experiments were undertaken and are in progress; the vitamin A and ceruloplasmin levels are regularly determined.
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PMID:[Relation between ceruloplasmin and vitamin A in Sprague-Dawley rats]. 53 78

The subcellular localization in rat liver cells of retinol-binding protein (RBP), prealbumin, ceruloplasmin, albumin, and class I transplantation antigen chains was investigated by radioimmunoassay determinations. The concentration of RBP was high in the rough and smooth endoplasmic reticulum (SER). The relative concentrations of prealbumin, ceruloplasmin and albumin were similar in the endoplasmic reticulum fractions and in the Golgi fraction. Neither of the proteins were found in significant amounts in the post-microsomal supernatant nor in the plasma membrane. The concentrations of the class I transplantation antigen chains were higher in the Golgi fraction than in the endoplasmic reticulum fractions. In the rough endoplasmic reticulum (RER) fraction ceruloplasmin and the class I antigens partially interact with high-molecular weight (MW) components, presumably membrane-bound glycosyltransferases. RBP, prealbumin and albumin seemed to be present in free form within the microsomal lumen. In vitamin A deficiency the RBP and to a lesser extent the prealbumin concentrations in the endoplasmic reticulum fractions were significantly increased, as compared to fractions from normal livers. This suggests that the presence of vitamin A is a prerequisite for the transport of RBP from the endoplasmic reticulum to the Golgi complex. The intracellular concentrations of albumin and ceruloplasmin were not significantly altered by vitamin A deficiency. In contrast, the amounts of the class I antigen heavy chains were found to be increased.
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PMID:Subcellular localization in normal and vitamin A-deficient rat liver of vitamin A serum transport proteins, albumin, ceruloplasmin and class I major histocompatibility antigens. 633 57

The most substantial change in the ratio between glycoprotein fractions distributing in the blood serum of rat under conditions of different vitamin A provision (0.50-0.70 micromol/L) are observed; they are characteristic of gamma-globulin, haptoglobin and alpha 1-acid glycoprotein; the intensity of colouring of their bars decreases on serum electrophoregrammes. At the same time, the decline of intensity of bar coloration of ceruloplasmin fraction takes place under the conditions of middle vitamin A deficiency (0.35-0.50 micromol/L) while that of transferrin takes place at marginal A-deficient state (< 0.35 micromol/L). In latent and logarithmic periods of Guerin's carcinoma growth, regardless of conditions of different vitamin A provision, the intensity of bars colouring, on electrophoregrammes, which correspond to immunoglobulin, haptoglobin, ceruloplasmin alpha2-Macroglobulin, alpha 1-acid glycoprotein and alpha1-antytrypsyn, increases. In a stationary period of tumour growth a decrease of coloration intensity of gamma- and alpha2-globulin fractions is observed.
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PMID:[Peculiarities of fractional composition of serum glycoproteins in Guerin's carcinoma development under condition of different vitamin A provision]. 1987 21