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M Titeux

Publications and source records attributed to M Titeux.

57 records · Page 4Linked to original sources

Expression of the blood group I, i, H, and A1 antigens on erythrocyte membranes studied by immunofluorescence.

A double immunofluorescence technique was used to study the expression of I, i, H and A1 antigens on individual erythrocytes of neonates, adult controls and patients with various haematological disorders. I, i and H staining was heterogeneously distributed from cell to cell as was already demonstrated for A1 antigen. i staining occured in 41 to 64% of cord cells (11 to 32% were strongly fluorescent) but only in 0.2 to 2.3% of adult erythrocytes. I staining occurred in 54 to 97.5% of adult erythrocytes but only in 1 to 14% of those of cord blood. Patients' cells tended to mimic a foetal pattern of heterogeneity in that an increase of i stained cells occured associated with a decrease of A1 or H stained cells. It is suggested that the foetal-like red cells observed in patients with haematological disorders result from an expansion of a normal process of differentiation rather than clonal development of abnormal cells.

ABO Blood-Group System↗

Characterization of phorbol esters binding to K 562 cells.

Binding of 20-[3H]-phorbol 2, 13-dibutyrate [( 3H] PDB) to intact human K 562 cells was characterized. Specific binding of [3H] PDB to K 562 cells at 20 degrees C or 37 degrees C reached a maximum within 15-20 min. Maximal specific [3H] PDB binding to K 562 cells was followed by a decline (down regulation) of radioacticity. This down regulation was temperature dependent; no loss of radioactivity occurred by 1 hour at 4 degrees C. When [3H] PDB binding was carried out a 4 degrees C, [3HDB bound to K 562 cells in a rapid, specific, and reversible manner. Phorbol esters which lack tumor-promoting activity, did not inhibit [3H] PDB binding. A Scatchard analysis was compatible with one class of binding sites, Kd = 50 nM and about 2 X 10(5) binding sites per cell. Human serum inhibited specific binding of [3H] PDB. The effect of several chemical compounds on [3H] PDB binding was also investigated. Most of the compounds tested such as butyrate, hemin, gamma-globulins, transferrin, insulin, EGF, and albumin failed to significantly affect the binding of [3H] PDB. In contrast, retinoic acid and quinacrine significantly affected the binding of [3H] PDB: retinoic acid induced a marked increase of [3H] PDB binding which was dose dependent; quinacrine induced a decrease of [3H] PDB binding, even at low concentration.

Binding, Competitive↗