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Biomedical subjects

B Agostini

Publications and source records attributed to B Agostini.

At least 37 records · Page 2Linked to original sources

Effect of 1,25-dihydroxycholecalciferol on impaired calcium transport by the sarcoplasmic reticulum in experimental uremia.

In the fragmented sarcoplasmic reticulum from skeletal muscle of rabbits with experimental uremia, defective calcium ion transport is found. An impairment of all parameters is observed (initial rate of uptake, storing capacity with and without oxalate, and concentrating ability). In vivo administration of 1,25-dihydroxycholecalciferol (1,25-(OH)2-vitamin D3)(2 X 27 ng X kg of body wt-1 X day-1 and 6 X 27 ng X kg-1 X day-1, respectively) improved the kinetic parameters. The low dose improved storing capacity, and the higher dose, in addition to the storing capacity, also corrected concentrating ability and the initial rate of uptake. It is concluded that active calcium transport in the sarcoplasmic reticulum is impaired by uremia and that this defect is responsive to the administration of 1,25-(OH)2-vitamin D3.

Animals↗

Cytochemical studies on sarcoplasmic reticulum of heart and skeletal muscle.

Ultrastructural aspects and cytochemical localization of Ca uptake and of -SH groups involved in the calcium transport of vesicular fragments of sarcoplasmic reticulum (SR) from rabbit skeletal muscle and from dog myocardium were studied by positive and various negatively-staining techniques. Size, shape, and membrane structure as well as proportion of calcium-containing vesicles vary a great deal depending on the method applied. On negatively stained material sarcoplasmic reticulum derivatives are identifiable in both skeletal muscle as well as in heart preparations by the presence on the surface of the vesicular membrane of 40-A particles and the capability of accumulating calcium. The amount of these vesicles is lower in cardiac SR than in the skeletal SR; however, no qualitative differences can be observed. Vesicles of cardiac SR labeled with the electron dense -SH group reagent, Hg-phenyl azoferritin, also bind asymmetrically the marker only at the outer surface of the membrane-like microsomes of skeletal muscle.

Animals↗