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Biomedical subjects

F Tedesco

Publications and source records attributed to F Tedesco.

At least 91 records · Page 5Linked to original sources

Studies on the mechanism of metabolic stimulation in polymorphonuclear leucocytes during phagocytosis. II. Presence of the NADPH2 oxidizing activity in a myeloperoxidase-deficient subject.

1. The biochemical properties of leucocytes from a myeloperoxidase-deficient subject were compared with those of leucocytes from healthy subjects. 2. Myleoperoxidase-deficient leucocytes responded to phagocytosis of heat-killed bacteria with increased respiration, increased oxidation of glucose through the hexose monophosphate shunt and increased production of H2O2 as normal leucocytes do. 3. The ability of granules isolated from myeloperoxidase-deficient leucocytes to oxidize nicotinamide coenzymes was comparable to that of granules isolated from normal leucocytes. 4. The results argue against the hypothesis that oxidation of NADPH2 in leucocytes is performed by myeloperoxidase.

Adult↗

Effect of human erythrocyte stromata on complement activation.

Stroma from either normal or PNH-like red cells is capable of inhibiting, to some extent, lysis in the sucrose test and enhancing lysis in the acidified-serum test. The same opposing effects are displayed by the exclusion peaks from Sephadex G-200 obtained from each stroma preparation, suggesting that the same factor could be responsible for both activities. Stromata and peaks also induce lysis of PNH-like cells in unacidified serum, indicating activation of complement through the alternate pathway. This is confirmed by immunoelectrophoretic observation. When serum previously activated through the alternate pathway is used in the sucrose test the amount of lysis is markedly reduced. This would indicate that the classical pathway activation can be controlled by the alternate pathway. The possible clinical significance of these factors in determining the haemolytic crisis in PNH patients is discussed.

Complement System Proteins↗

A computerized microassay for complement hemolytic activity using an automated spectrophotometer.

A microassay carried out with V-bottomed microplates was developed as a simplified procedure to estimate the complement hemolytic activity. This microassay has the advantage of permitting the evaluation of the extent of lysis without the need to separate the supernatants from the unlysed erythrocytes. This is accomplished by calculating the ratio between the absorbance at 405 nm and that at 450 nm. The results, read automatically on a Dynatech MR580 spectrophotometer, are transformed into CH50 U by means of a computer program. Finally, a kinetic assessment of complement hemolytic activity, easily carried out by this simple procedure, may reveal complement abnormalities otherwise undetected by the standard hemolytic assay.

Animals↗

Selective C3 deficiency due to C3 nephritic factor in an apparently healthy girl.

Routine laboratory investigations performed on the serum of an 8-year-old girl examined because of a moderate degree of iron-deficiency anemia showed a markedly reduced C3 level. More detailed complement studies revealed a selective C3 deficiency, as indicated by the almost undetectable C3 concentration tested by both hemolytic and immunochemical assays and by the normal or slightly reduced levels of all the other complement components. The hemolytic activity of the serum was restored by the addition of partially purified C3 component. The isolated C3 deficiency could be attributed to the presence of a C3-cleaving activity in the serum of the propositus. This activity was identified as C3 nephritic factor (C3NeF) since it was heat-stable, was absorbed by Cowan I strain of Staphylococcus aureus and was-eluted in the IgG fraction after DEAE-chromatography of the serum. The levels of H and I factors of the alternative pathway in the serum of the propositus and of C3 in the serum samples of her parents and two siblings were found to be within the normal range. The previous clinical history of the girl and the follow-up for a period of approximately 5 years showed that she was apparently healthy and did not reveal clinical and/or laboratory evidence of glomerulonephritis, lipodystrophy or repeated bacterial infections usually associated with the presence of C3NeF in the serum.

Anemia, Hypochromic↗

Complement-endothelial cell interactions: pathophysiological implications.

The function of the endothelial cells can be modulated by humoral factors present in the circulation and in the extravascular fluid, including proteins of the complement system. This review examines the multiple interactions between the complement system and the endothelial cells and their functional consequences on inflammation, coagulation and regulation of vascular tone. The implications of these interactions in the induction and progression of the vascular lesions occurring in atherosclerosis, ischemia/reperfusion and xenotransplantation and the possible therapeutic approaches in terms of complement regulation are also discussed.

Animals↗

Inhibition of in vitro adherence of antibody-coated red cells to monocytes by the dialyzable leukocyte extract.

The red cell-monocyte assay (RMA), which has been used to evaluate the clinical significance of red cell (RBC) antibodies, was employed to test the effect of the dialyzable leukocyte extract (DLE) on in vitro adherence to monocytes of human RBCs coated with alloantibodies or autoantibodies. The total association index (TAI) of the RMA, expressing the number of RBCs adhering to or phagocytosed by 100 monocytes, indicated a potent inhibitory activity of DLE in the test system. TAI values of 100.4 +/- 20.1 (mean +/- SD) in the control sample, consisting of RBCs coated in vitro with anti-D, dropped to 4.0 +/- 2.1 when DLE was present in the assay medium at a concentration of 0.5 U per mL. Similar results were obtained with RBCs coated with IgG antibodies in vivo. The inhibition was dose dependent and was associated with a thermolabile component of DLE. This study establishes that DLE can modulate monocyte function by inhibiting the recognition of IgG sensitized red cells.

Cell Adhesion↗