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M Elhilali

Publications and source records attributed to M Elhilali.

56 records · Page 4Linked to original sources

Evaluation of cortisone-heparin and cortisone-maltose tetrapalmitate therapies against rodent tumors. II. Pathological studies.

Pathological studies were undertaken in three tumor-host models which were subjected to cortisone based treatments. The first model was Fisher 344 rats with established orthotopically implanted syngeneic bladder tumor. Cortisone-herapin and cortisone-maltose tetrapalmitate (MTP) treatments induced focal areas of tumor necrosis and necrobiosis, whereas cortisone alone caused necrobiosis. The second model was C3HBA mammary tumor fragments implanted subcutaneously in syngeneic MTP responder C3H/HeN and MTP non-responder C3H/HeJ female mice. Only cortisone-MTP treatment led to an absence of capillary extension from surrounding blood vessels into the scant tumor stroma. The third model, ethyl carbamate induced primary lung cancer in AJ mice, was tested only with cortisone-herapin combination. The treatment caused central zones of necrosis.

Animals↗

Characterization of androgen receptor by high performance liquid chromatography and sucrose density gradient ultracentrifugation in normal and malignant human prostatic tissues.

In the present study we have characterized androgen-receptor complexes of normal and malignant human prostate cytosols using sucrose density gradient centrifugation, gel permeation and anion exchange high performance liquid chromatography (HPLC). Our results indicated that: 1) malignant tissue cytosols differed from normal by the presence of a 4-5S androgen receptor form which accounted for 30% of total specific-binding of malignant tissue cytosols, 2) 8-9S androgen-receptor complexes in normal and malignant prostate cytosols were estimated as 270kDa by gel permeation HPLC, 3) 8-9S complexes were retained and could be eluted by 0.22M KCl on a linear gradient anion exchange HPLC, 4) 4-5S androgen-receptor complexes were estimated as 90kDa by gel permeation HPLC and were not retained on anion exchange HPLC in our experimental conditions, and 5) either 10X dilution of the 4-5S complexes and subsequent anion exchange HPLC, or anion exchange chromatography of 8-9S complexes at 22 degrees C were causing fragmentation of the androgen receptor molecule from normal and malignant tissues. These fragments had enhanced affinity for anion exchange columns. These results are discussed in relation to the composition of the nontransformed androgen receptor macromolecule.

Adult↗