Zinc deficiency alters barrier function of cultured porcine endothelial cells

Article Abstract:

The role of zinc in biological membrane function is studied in in vitro culture of porcine pulmonary epithelial cells. Porcine pulmonary vascular epithelia upon exposure to a zinc deficient medium show a dose-dependent decrease in this function with no evidence of morphological derangements. The mineral also prevents endothelial injury caused by fatty acids by binding to lipid and protein fractions of the cell membrane. Hence, zinc is an essential mineral for the maintenance of endothelial cell membrane barrier function and is a vital component in membrane transport systems for enzymes dependent on the mineral.

Research, Angiotensin converting enzyme, Vascular endothelium, Zinc deficiency diseases

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Hepatic metallothionein gene expression in toxic milk mice

Article Abstract:

Hepatic copper toxicity due to toxic milk mutation in mice was investigated in terms of gene expression of metallothionein following ingestion of copper and zinc. In toxic fetal and neonatal mice, the mRNA concentration was the same as normal mice. and increased mRNA coding of metallothionein in the hepatocytes is induced in mutant neonatal mice after copper uptake. Gene expression is more active in adult mice with the toxic milk mutation. Hence, the increased metallothione gene expression in mice is primarily due to accumulation of excess copper, and not as a direct effect of the disease itself.

Genetic aspects, Mice, mutant strains, Mutant mice, Copper, Metallothionein, Milk, Food testing

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Zinc deficiency alters the protein composition of the membrane skeleton but not the extractability or oligomeric form of spectrin in rat erythrocyte membranes

Article Abstract:

The effect of zinc deficiency on the membrane skeleton of red blood cells from rats was examined through composition analysis and extractability evaluation of spectrin from rats kept on a zinc-deficient diet. Results showed that zinc deficiency did not modify spectrin oligomeric form and extractability. It did, however, reduce protein R5 composition of spectrin. This alteration in the composition of the membrane skeleton suggests a structural or compositional modification not indicated by spectrin extractability and oligomeric analysis.

Analysis, Cytoskeleton

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