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Biomedical subjects

E Corvazier

Publications and source records attributed to E Corvazier.

26 records · Page 2Linked to original sources
PubMed1989

Platelet-dependent induction and amplification of polymorphonuclear leucocyte lysosomal enzyme release.

Degranulation of human polymorphonuclear leucocytes induced by opsonized zymosan (OpZ) was studied in the presence or absence of platelets, either resting or stimulated by thrombin. Lysozyme secretion from polymorphonuclear leucocytes stimulated with OpZ increased in the presence of platelets. A further increase was observed when platelets had been stimulated with thrombin. The effect was dependent on platelet concentration (10-80 platelets/polymorphonuclear leucocytes). Resting polymorphonuclear leucocytes could be activated by platelets that had been stimulated with thrombin with an optimal effect observed at 0.1 U/ml of thrombin. Substitution of platelets with platelet-released products only resulted in significant stimulation of polymorphonuclear leucocytes at concentrations above those used in the coincubations experiments. Zymosan coated with various opsonins showed a gradient in the relative intensity of polymorphonuclear leucocytes degranulation. Platelet-dependent enhancement of polymorphonuclear leucocytes degranulation was higher with opsonins that were poorer at inducing lysosomal secretion. The role of platelets as helper cells in the activation of polymorphonuclear leucocytes appears to be dominant when polymorphonuclear leucocytes are challenged in suboptimal conditions. Positive interactions between platelets and polymorphonuclear leucocytes may be relevant in vivo at the site of inflammation where platelets could enhance effector functions of polymorphonuclear leucocytes.

Blood Platelets↗
PubMed1986

Development of a radioimmunoassay for prostaglandin D2 using an antiserum against 11-methoxime prostaglandin D2.

A sensitive and specific radioimmunoassay for prostaglandin D2 has been developed using its stabilized 11-methoxime derivative, which was obtained after treatment of prostaglandin D2 with methoxamine-HCl. The antiserum was obtained after injection of prostaglandin D2-methoxamine coupled to bovine serum albumin. A (125I)-Histamide prostaglandin D2-methoxamine tracer was prepared by iodination of the corresponding histamide, followed by thin layer chromatography purification. The sensitivity of the assay was 280 femtomoles per ml at 50% displacement. The cross reactivities were 15% with prostaglandin D1-methoxamine and less than 0.20% with other prostaglandins. Determination of the half-life of prostaglandin D2 in a solution containing albumin was also carried out, since it has been shown to catalyze prostaglandin D2 destruction. The unstability of this prostaglandin is due to the presence of a beta-hydroxy ketone group, and all prostaglandins possessing this labile moiety could be stabilized by such a derivatization before developing a radioimmunoassay.

Chromatography, Thin Layer↗
PubMed1986

Release of prostacyclin after erythrocyte adhesion to cultured vascular endothelium.

Endothelial cell damage is considered to be the initial step in the genesis of thrombosis and atherosclerosis. Recently, the adhesion of erythrocytes from patients with diabetes or sickle cell anemia to endothelial cells was found to be increased and correlated with the severity of vascular complications. We have measured by radioimmunoassay the release of 6-keto-prostaglandin F1 alpha (6-keto-PGF1 alpha) as an index of prostacyclin (PGI2) production, during red cell adhesion to endothelial cells in culture. The amount of 6-keto-PGF1 alpha released after incubation with normal red cells was similar to that observed with buffer (1.07 +/- 0.32 nmol/10(6) endothelial cells). However, after the adhesion of erythrocytes from patients with diabetes or sickle cell anemia, the amount of 6-keto-PGF1 alpha produced was significantly increased (P less than 0.01) and was correlated with the extent of erythrocyte adhesion (P less than 0.05). Tritium-labeled PGI2 was found to bind to erythrocytes, and the binding was time and concentration dependent. PGI2 release was inhibited by the cyclooxygenase inhibitor (flurbiprofen), whereas red cell adhesion remained unchanged. Fibrinogen potentiated erythrocyte adhesion and PGI2 production. The increase in PGI2 production after the adhesion of red cells from patients with diabetes or sickle cell anemia to endothelial cells indicates that endothelium may be damaged by abnormal erythrocyte adhesion.

6-Ketoprostaglandin F1 alpha↗
PubMed1985

Interference of some flavonoids and non-steroidal anti-inflammatory drugs with oxidative metabolism of arachidonic acid by human platelets and neutrophils.

The effect of ten flavonoids was studied on the stimulation of washed human platelets by either arachidonic acid or thrombin. The oxygenated metabolites released were analyzed by radioimmunoassay, glass-capillary-column gas chromatography and high-pressure liquid chromatography. No effect was evidenced for naringenin, rutinose and phloridzin up to 1000 microM. Thromboxane B2 and 12-hydroxyeicosatetraenoic acid production was depressed simultaneously by all other compounds at different IC50. When tested for their effect on reversibility, however, cyclooxygenase and lipoxygenase inhibition was found to be different depending upon the flavonoid used. All compounds, except morin and rutin, inhibited platelet aggregation and [14C]serotonin release with parallel inhibition of thromboxane synthesis when tested on arachidonic acid-induced platelet-rich plasma stimulation. Some flavonoids inhibited the metabolism of human neutrophils stimulated by ionophore A23187 as assessed by high-performance liquid chromatography. Our results show that flavonoids interfere with the different oxidative metabolisms of arachidonic acid. No clearcut specificity could be found between one compound and one metabolic pathway.

Anti-Inflammatory Agents↗
PubMed1985

Activated platelets stimulate human neutrophils functions.

Opsonized zymosan is able to induce polymorphonuclear leucocyte activation as reflected by lysosomal degranulation and light emission. However this stimulus is a weak inducer of arachidonic acid metabolism in these cells. We have studied the effects of co-incubation of polymorphonuclear leucocytes and platelets, each of them exposed with its specific stimulus (i.e. opsonized zymosan and thrombin). The granule constituent release was enhanced in the presence of activated platelets, but not the chemiluminescence. The same results were found in time-course experiments. Another important effect of this co-incubation was the potentiation of the synthesis of 5-lipoxygenase metabolites of arachidonic acid by activated platelets. The in vitro study of cellular cooperation may be of great interest in evaluating the role of the messenger processes occurring from one cell to another.

Blood Platelets↗
PubMed1984

Minimal effect of estrogens on endothelial cell growth and production of prostacyclin.

The effects of natural and synthetic sex hormones (10(-8)M) have been studied on human umbilical endothelial cell proliferation and prostacyclin production. 17 B estradiol and progesterone had no effect on cell multiplication. Ethinyl-estradiol increased proliferation when the initial plating density was 40,000 cells/cm2. However, the production of 6-keto PGF1 alpha induced by the Ca++ ionophore A 23187 was not different between control, 17 B estradiol-or ethinyl estradiol-treated cultures. These results demonstrate an in vitro effect of synthetic estrogen, ethinyl estradiol on endothelial cell proliferation. At the present time it is however difficult to correlate these results with the clinical observation of an increase in thromboembolic complications in women under oral contraceptives.

6-Ketoprostaglandin F1 alpha↗
PubMedDate not supplied

How many Ca(2)+ATPase isoforms are expressed in a cell type? A growing family of membrane proteins illustrated by studies in platelets.

Ca(2+) signaling plays a key role in normal and abnormal platelet functions. Understanding platelet Ca(2+) signaling requires the knowledge of proteins involved in this process. Among these proteins are Ca(2+)ATPases or Ca(2+) pumps that deplete the cytosol of Ca(2+) ions. Here, we will particularly focus on two Ca(2+) pump families: the plasma membrane Ca(2+)ATPases (PMCAs) that extrude cytosolic Ca(2+) towards the extracellular medium and the sarco/endoplasmic reticulum Ca(2+)ATPases (SERCAs) that pump Ca(2+) into the endoplasmic reticulum (ER). In the present review, we will summarize data on platelet Ca(2+)ATPases including their identification and biogenesis. First of all, we will present the Ca(2+)ATPase genes and their isoforms expressed in platelets. We will especially focus on a member of the SERCA family, SERCA3, recently found to give rise to a number of species-specific isoforms. Next, we will describe the differences in Ca(2+)ATPase patterns observed in human and rat platelets. Last, we will analyze how the expression of Ca(2+)ATPase isoforms changes during megakaryocytic maturation and show that megakaryocytopoiesis is associated with a profound reorganization of the expression and/or activity of Ca(2+)ATPases. Taken together, these data provide new aspects of investigations to better understand normal and abnormal platelet Ca(2+) signaling.

Animals↗