Paola Finotti

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The (Na+-K+)ATPase and (Mg2+)ATPase activities of erythrocyte membranes of Type 1 (insulin-dependent) diabetic patients were found to be significantly reduced compared to matched controls (p < 0.005). On the contrary, erythrocyte Na+ and K+ contents were similar in diabetic patients and in normal subjects. When erythrocyte membranes from diabetic patients(More)
Although the Hsp90 chaperone family, comprised in humans of four paralogs, Hsp90α, Hsp90β, Grp94 and Trap-1, has important roles in malignancy, the contribution of each paralog to the cancer phenotype is poorly understood. This is in large part because reagents to study paralog-specific functions in cancer cells have been unavailable. Here we combine(More)
The overall increase in proteolytic activity in diabetes is known to be associated with the development and progression of vascular complications. Our aim was to investigate in detail the molecular nature of this activity in the plasma of Type 1 diabetic subjects. Plasma of both diabetic and control subjects was subjected to various purification procedures(More)
The possibility that distinct genetic factors may concur, in association with diabetes, to increase susceptibility to vascular morbidity, including hypertension, has been evaluated in ninety-four normotensive insulin-dependent diabetic patients by testing both the frequency and prevalence of hypertension in parents and by measuring membrane red blood cell(More)
Plasma from insulin-dependent diabetics shows an increased ability to specifically activate the (Na-K)ATPase from different sources. Several protease inhibitors like phenyl methyl sulfonyl fluoride, trypsin inhibitor, antithrombin III and aprotinin, produced a significant dose-dependent inhibition of the stimulatory effect produced by a 1/100 final dilution(More)
Canrenone, a spironolactone metabolite, was tested for its possible effects on (Na+-K+) adenosine triphosphatase (ATPase) activity [Mg++-dependent, (Na+-K+)-activated ATP phosphohydrolase (E.C. and ouabain interaction with the enzyme. Canrenone competitively antagonized the binding of [3H]ouabain to (Na+-K+)ATPase and inhibited (Na+-K+)ATPase(More)
The aim of the present study was to investigate whether or not alterations of the plasma proteinase-antiproteinase system were present in type 1 (insulin-dependent) diabetic patients and, if so, whether or not they were related to sex, age at onset and duration of the disease as well as to short- and long-term diabetic control. The plasma concentration of(More)
The possibility that platelet activation may also involve membrane (Na-K)ATPase was investigated by testing the effects of both proteinases on platelet shape change and aggregation in the absence and presence of the specific (Na-K)ATPase inhibitor ouabain. Ouabain (8 to 80 microM) completely antagonized trypsin-induced platelet shape change and aggregation(More)
Among substances which may prove useful in preventing or reducing the progression of glycooxidative modifications of proteins, heparin plays a unique role. To elucidate the mechanism whereby heparin may favourably influence the protein structure during glycation, human serum albumin (HSA) was glycated with both 25 and 50 mM glucose in the absence and(More)