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Biomedical subjects

D Romeo

Publications and source records attributed to D Romeo.

At least 73 records · Page 4Linked to original sources
PubMed1982

[Polycardiography in the diagnosis of latent cardiac insufficiency].

A group of heart patients and another group of healthy subjects have been studied and their systolic intervals (PEP-LVET - PEP/LVET ratio and the telediastolic index) evaluated using the mechanocardiographic system. In both long-standing and recent heart patients, the parameters studied showed significant deviations from the norm. These were even more marked after exercise on the ergonometer bicycle. Acute doses of digitalis reduced deviations from the norm observed under basal conditions and after exercise. Polycardiography, it is concluded, assists in the gathering of extremely valuable information about cardiac performance in relation to latent cardiac insufficiency. Especially useful information can be deduced from PEP indications and from the PEP/LVET ratio. The use of digitalis is suggested for physically active post-infarction subjects in order to give greater tolerance of physical exercise. The concept of long-term polygraphic studies as part of out-patient follow-ups on such patients is outlined.

Adult↗
PubMed1982

[A fourth tone and latent cardiac insufficiency in ischemic heart disease].

An assessment was made of the fourth heart sound as a non-invasive clinical and instrumental aid in the diagnosis of latent cardiac insufficiency. The sound was recorded in various decubitus positions in a series of healthy subjects and patients with recent and past infarction, under basal conditions, after exercise on the cycle ergometer, and after digitalis i.v. Persistence of the fourth sound in the standing position was noted in nearly all infarct patients, while its incidence decreased significantly after digitalis. It is felt that this finding can be interpreted as evidence of the non-existence of latent heart failure. Its further investigation and correlation with other invasive and non-invasive instrumental examinations is proposed.

Adult↗
PubMed1982

Active extrusion of Ca2+ from epiphysial chondrocytes of normal and rachitic chickens.

Chondrocytes isolated from the epiphysial cartilage of chickens were exposed to either the ionophore A23187 or KCN, in the presence of 0.4 mM-extracellular Ca2+. This treatment elicits a prompt release of cell Ca2+, which can be measured as net cation efflux by a highly sensitive Ca2+-selective electrode system. Pre-exposure of chondrocytes to the metabolic inhibitors 2-deoxy-D-glucose or oligomycin causes a parallel decrease in both cell ATP and ionophore-mediated Ca2+ extrusion. Conversely, substitution of extracellular Na+ with choline produces only a very small decrease in the rate of Ca2+ efflux. This indicates that the ionophore A23187 and cyanide induce the mobilization of intracellular Ca2+, which is then extruded from the cell mainly by an ATP-driven pump system. Chondrocytes isolated from the cartilage of rachitic chickens also exhibit the capacity for extruding Ca2+ by the same mechanism, with an efficiency comparable with that of their normal counterpart.

Adenosine Triphosphate↗
PubMed1982

ATP-driven Ca2+ pump activity of macrophage and neutrophil plasma membrane.

The results of the investigations here described permit us to conclude that macrophages and neutrophils have a peripheral, outwardly directed Ca2+ extrusion system, which is very similar to the well known Ca2+ pump of the red cell, with regard to capacity and mechanism (16, 21, 29). In fact, all the three cell types have similar maximum pumping rates (about 0.1-0.2 microgram-ions Ca2+/min/ml cells) and use ATP for extruding Ca2+. Furthermore, the plasma membrane of all the three cell types catalyzes a Ca2+-dependent ATPase reaction, which is very likely the enzyme manifestation of the Ca2+ pump activity. Further investigation is needed to establish whether the peripheral Ca2+ pump system of macrophages and neutrophils is utilized to restore steady-state levels of cytosolic Ca2+ upon cell stimulation, or is somehow involved in the triggering of cell response to various stimuli. In fact impairment of the pump activity by a cell stimulant would unbalance Ca2+ passive leaks and active cation extrusion, thereby leading to higher steady-state levels of Ca2+ in the cytosol and to stimulation of Ca2+-dependent functions (1-12).

Biological Transport, Active↗
PubMed1982

Calcium movement and membrane potential changes in the early phase of neutrophil activation by phorbol myristate acetate: a study with ion-selective electrodes.

To quantitate calcium movements and membrane potential changes in stimulated neutrophils, we have measured net fluxes of Ca2+ and of the lipophilic cation tetraphenyl phosphonium by a very sensitive ion-selective electrode system. Activation of neutrophils by 3 X 10(-8) M phorbol 12-myristate, 13-acetate induces a release of approximately 20% of total cell calcium, with an initial lag period of less than 10 s. The Ca2+ outflux is markedly reduced in ATP-depleted cells and in the presence of a calmodulin inhibitor, thereby suggesting that it occurs by activation of the ATP-driven Ca2+ pump of the neutrophil plasmalemma. Activation of neutrophils also induces a transiently increased exchange of medium 45Ca with cell calcium, which is measurable a few seconds after cell exposure to the stimulant and peaks at approximately 40 s. Stimulation of neutrophils after attainment of steady-state accumulation of tetraphenyl phosphonium (resting potential of -67 mV) results in a marked depolarization, with a lag period of approximately 60 s. The rate and extent of depolarization are reduced by 40 and 65%, respectively, in a low Na+ medium but are not modified by an inhibitor of anion exchange across membranes. A high-K+ medium depolarizes neutrophils without either modifying their resting oxidative metabolism or impairing stimulability by the phorbol ester. Phorbol 12-myristate, which also exhibits no effect on the oxidative metabolism of neutrophils, does not induce Ca2+ extrusion and membrane potential changes. The causal relationship between Ca2+ mobilization, membrane potential changes and activation of neutrophil functions is discussed.

Animals↗
PubMed1980

Inhibition by quercetin of activation of polymorphonuclear leucocyte functions. Stimulus-specific effects.

The effect of some bioflavonoids on the activation of polymorphonuclear leucocyte respiration and exocytosis was examined. At 10-5-10-4 M concentration, quercetin, but not morin and rutin, was found to inhibit the concanavalin A-induced enhancement of oxygen consumption markedly, without impairing leucocyte viability and concanavalin A binding. The inhibition could be reversed by either washing the leucocytes or adding a 10-fold molar excess of 1-anilino-8-naphthalene sulphonate. Concanavalin A-dependent cell secretion of lysozyme was also totally inhibited by 30 muM quercetin. The effect of quercetin on the activation of leucocyte respiration appeared to be stimulus specific. In fact, at a concentration of the flavonoid (75 muM) which provided a 95% inhibition of the concanavalin A-induced stimulation, the respiratory activation produced by phospholipase C was inhibited by about 50% and that caused by myristic acid and by the antibiotic Br-X537A by less than 25%. These data suggest that quercetin exerts its activity at specific sites of the plasma membrane of the leucocytes, and that this compound might be used to identify the membrane domain whereon different stimuli act to originate the initial stimulatory signal.

Animals↗
PubMed1980

Isolation and partial characterization of the plasma membrane of purified bovine neutrophils.

1. Large amounts of granulocytes can be isolated from bovine blood by differential centrifugation and hypotonic lysis of erythrocytes, followed by separation of neutrophils and eosinophils by centrifugation through a gradient of colloidal silica. 2. Careful homogenization of the purified neutrophils and subfractionation of the postnuclear supernatant by centrifugation through a discontinuous sucrose gradient provides a membrane fraction (at the 20/32%, w/w, sucrose interface), which collects about 20--35% of the activity of plasma membrane marker enzymes. 3. Treatment of the plasma membrane fraction with 0.5 M KCl removes some protein and activity of granule enzymes, leading to an about 20--35-fold enrichment in specific activity of plasma membrane marker enzymes. In particular, there is a 25-fold enrichment in a Ca2+-dependent ATPase, whose half-maximal reaction velocity is reached at 2.2 X 10(-7) M Ca2+. 4. High-resolution sodium dodecyl sulphate/polyacrylamide gel electrophoresis reveals a complex composition of the neutrophil plasma membrane, with about 40 polypeptides stained by Coomassie blue. Ten of these peptides are more intensely stained by the dye; their apparent molecular weight ranges from 81 000 to 34 000. All these ten polypeptides but one (which is likely to be actin) are markedly enriched in the plasma membrane fraction over the original homogenate. 5. Since bovine blood can be obtained in unlimited amounts, the procedures here described can be applied to a large-scale purification of the neutrophil plasma membrane, suitable for biochemical studies.

Animals↗
PubMed1979

Calcium ion-dependent adenosine triphosphatase activity and plasma-membrane phosphorylation in the human neutrophil.

A plasma-membrane fraction was isolated from a post-nuclear extract of human neutrophils by centrifugation through a linear sucrose density gradient. This fraction exhibited a Ca2+-dependent adenosine triphosphatase (ATPase) activity that could be differentiated from mitochondrial or myosin ATPase and from plasma-membrane Mg2+-dependent ATPase. When assayed in the presence of [gamma-32P]ATP, the Ca2+-dependent ATPase reaction resulted in the formation of an acid-resistant hydroxylamine-sensitive bond between the gamma-[32P] phosphate group and a membrane protein subunit with an apparent mol.wt. of 135000. Half-maximal activating effect of Ca2+ was found at 82nM and 0.18 microM for the ATPase and the formation of the 32P-membrane complex respectively. Generation of the phosphorylated product attained the steady state at 0 degrees C by about 30s, and was rapidly reversed by ADP. These results suggest that the Ca2+-activated ATPase reaction occurs through the formation of a phosphoprotein intermediate, similar to that described for some Ca2+-dependent ATPase enzymes associated with Ca2+ transport. The possibility thus exists that the neutrophil Ca2+-dependent ATPase catalyses a process of Ca2+ extrusion from the cell, thereby participating in the regulation of several Ca2+-dependent neutrophil functions.

Adenosine Triphosphate↗
PubMed1979

Ca2+-dependent ATPase activity of alveolar macrophage plasma membrane.

A plasma membrane fraction was isolated from lysates of Bacillus Calmette-Guérin-induced alveolar macrophages of rabbit. On the basis of morphological and biochemical criteria this fraction appeared to be minimally contaminated by other subcellular organelles. Concentrations of Ca2+, but not of Mg2+, from 6.10(-8) to 1.10(-5) M markedly stimulated the basal ATPase (EC 3.6.1.3) activity of the plasma membrane, with an apparent Km (Ca2+) of 1.10(-6) M. The specific activity of the Ca2+-ATPase assayed at pCa = 5.5 was enriched about 8-fold in the plasma membrane fraction over the macrophage lysate. In contrast, the specific activity of the K+, EDTA-activated ATPase, associated to macrophage myosin, increased only 1.3-fold. Oligomycin and -SH group reagents exerted no influence on the Ca2+-ATPase activity, which was on the contrary inhibited by detergents such as Triton X-100 and deoxycholate. The activity of the Ca2+-ATPase was maximal at pH 7, and was decreased by 50 mM Na+ and 5 mM K+. On the contrary, the activity of Mg2+-ATPase, also present in the plasma membrane fraction, had a peak at about pH 7.8, and was stimulated by Na+ plus K+. On account of its properties, it is suggested that the Ca2+-ATPase is a component of the plasma membrane of the alveolar macrophage, and that its function may be that of participating in the maintenance of low free Ca2+ concentrations in the macrophage cytosol.

Adenosine Triphosphatases↗
PubMed1979

Phosphorprotein intermediate in the Ca2+-dependent ATPase reaction of macrophage plasma membrane.

ATPase activity and phosphorylation by [gamma-32P] ATP of isolated plasma membrane of alveolar macorphages are stimulated in a parallel fashion by physiologic concentrations of Ca2+, with half-maximal activating effect of this ion at (3--7) X 10(-7) M. For various membrane preparations, a direct proportionality exists between Ca2+-dependent ATPase activity and amount of 32P incorporated. Labeling of membrane attains the steady-state level by 10 sec at 0 degrees C, and is rapidly reversed by adenosine diphosphate (ADP), K+ decreases the amount of membrane-bound 32P, mainly by enhancing the rate of dephosphorylation of the 32P-intermediate. Hydroxylamine causes a release of about 90% of 32P bound to the membrane, thus indicating that the 32P-intermediate contains an acyl-phosphate bond. When the labeled plasma membrane is solubilized and electrophoresed on acrylamide gels in the presence of sodium dodecyl sulphate, the radioactivity appears to be largely associated with a single protein fraction of 132,000 +/- 2,000 aarent molecular weight. These features of the macrophage Ca2+-ATPase suggest that the enzyme activity might be part of a surface-localized Ca1+-extrusion system, participating in the regulation of Ca2+-dependent activities of the macrophage.

Animals↗
PubMed1978

Metabolic stimulation of polymorphonuclear leucocytes: effects of tetravalent and divalent concanavalin A.

Polymorphonuclear leucocytes (PMNL) undergo a marked activation of their oxidative metabolism upon interaction with surface-reactive soluble stimuli as well as with phagocytosable objects. To get some insight into the mechanism of this stimulation, we have compared the stimulatory activity of the tetravalent lectin concanavalin A (Con A) with that of the divalent derivative succinyl-Con A (S-Con A). Both lectins bind to the PMNL surface to the same extent. S-Con A, however, is much less efficient in stimulating the PMNL metabolism. When S-Con A-treated PMNL are further reacted with antiserum to Con A, a potentiation of the metabolic stimulation is observed. Normal serum or addition to PMNL of antiserum to Con A in the absence of lectin has no effect. Furthermore, if S-Con A is displaced from its receptors on the cell membrane with alpha-methyl mannopyranoside, the addition of antiserum fails to cause a respiratory stimulation. These results suggest that the initial triggering of the metabolic stimulation of PMNL is in part accomplished through cross-linkage of membrane constituents.

Antibodies↗