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D Mocini

Publications and source records attributed to D Mocini.

8 recordsLinked to original sources
PubMed1995

Dipyridamole echocardiography and 99mTc-MIBI spect dipyridamole scintigraphy for cardiac evaluation prior to peripheral vascular surgery.

Coronary artery disease accounts for most of the early and late mortality and morbidity associated with vascular surgery. Cardiac pre-operative evaluation is mandatory for the assessment of cardiac risk. The aim of this study is to compare dipyridamole scintigraphy with 99mTc-MIBI (MIBI-dipy) and dipyridamole echocardiography (ECHO-dipy) and to evaluate their capability in identifying cardiac risk for strong events such as death, unstable angina or myocardial infarction. METHODS. Sixty consecutive patients (mean age 67 +/- 7) were enrolled. 52 performed ECHO-dipy, 51 MIBI-dipy. 40 patients went to aorto-femoral or aorto-iliac graft replacement and 15 to vascular angioplasty. Five patients did not undergo surgery. RESULTS. Eighteen patients (30%) had stress defects and 9 patients also rest defects with MIBI-dipy. Six patients new asinergic areas at ECHO-dipy. Three pts died in the first year follow-up for a cerebrovascular event, a myocardial infarction and a sudden death respectively. Sensitivity and specificity, positive and negative predictive value were 100%, 69%, 16%, 100% for MIBI-dipy and 66%, 94%, 40%, 98% for ECHO-dipy. CONCLUSIONS. As other authors reported, stress scintigraphy is a pre-operative test showing high sensitivity but with no satisfying specificity. Stress echocardiography, in our population, can produce a good negative predictive value. It is a less expensive and widespread clinical tool useful in the evaluation of preoperative patients. Its positive predictive power is not satisfying but it is shared with all non-invasive pre-operative tests available now.

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PubMed1984

Characterization of a calmodulin-dependent high-affinity cyclic AMP and cyclic GMP phosphodiesterase from male mouse germ cells.

Two cyclic nucleotide phosphodiesterase activities were separated by ion-exchange chromatography of cytosol from male mouse germ cells. A form eluted at low salt concentration showed high affinity (Km congruent to 2 microM) and low affinity (Km congruent to 20 microM) for cyclic AMP, and high affinity (Km congruent to 3.5 microM) for cyclic GMP. A second form, eluted at high salt concentration, showed high affinity (Km congruent to 5 microM) for cyclic AMP and was similar to a phosphodiesterase activity described in rat germ cells. The present study was performed to characterize the first form, which represents most of the phosphodiesterase activity in mouse germ cells. The enzyme was sensitive to Ca2+ and calmodulin stimulation, which increased its activity 3-4-fold. Calmodulin stimulation depended on direct interaction of the activator with the enzyme, as indicated by the reversible changes in the chromatographic elution pattern in the presence of Ca2+, as well as by the increase in the sedimentation coefficient in the presence of calmodulin. Reciprocal inhibition kinetics between cyclic AMP and cyclic GMP for the calmodulin-dependent form demonstrated a non-competitive inhibition between the two substrates, suggesting the presence of separate catalytic sites. This is in agreement with kinetic parameters and different thermal stabilities of cyclic AMP- and cyclic GMP-hydrolysing activities. Furthermore, the relevant change in s value, depending on the absence or presence of Ca2+ and calmodulin, suggested that the enzyme is composed of subunits, which aggregate in the presence of the activator. A model for catalytic site composition and reciprocal interaction is also proposed.

3',5'-Cyclic-AMP Phosphodiesterases↗