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F Llopis

Publications and source records attributed to F Llopis.

8 recordsLinked to original sources

Aromatase activity and estradiol in human breast cancer: its relationship to estradiol and epidermal growth factor receptors and to tumor-node-metastasis staging.

PURPOSE: The present report attempts to clarify whether there is a relationship between aromatase activity (ARAC) and estradiol (E2), hormonal receptors, E2 receptor (ER), and epidermal growth factor receptor (EGFR), as well as with tumor stage and histopathology in human breast cancers. MATERIALS AND METHODS: We studied 225 breast carcinomas, 67 of which were premenopausal and 158 postmenopausal. In each sample, ARAC, EGFR, ER, and E2 were quantified. ARAC was quantified by Thompson and Siiterii's method, EGFR was quantified with a two-point assay method using radioactive iodine (125I)-EGF as ligand, and ER was measured by the Scatchard method using 3H-E2. E2 was quantified by radioimmunoassay in the diethylether tumor extract. RESULTS: ARAC was found in 64% of the cancers studied. There is a strong direct association between ARAC and tumor size in postmenopausal patients (P = .001). In the postmenopausal group, the proportion of ARAC-positive (ARAC+) tumors is significantly higher among ER-positive (ER+) than ER-negative (ER-) ones (P less than .001). ER+ tumors also have significantly higher levels of E2 than do ER- ones (P less than .0001); similarly, ARAC+ tumors have significantly higher levels of E2 than do ARAC- ones (P less than .0001). There is a significant multiple linear correlation between the log of the levels of ARAC, ER, and EGFR and the log of tumor E2 (P less than .0001). The correlation coefficients obtained show that ARAC and ER have a positive effect on tumor E2. CONCLUSION: The results obtained suggest the importance of tumor ARAC in the tumoral levels of E2 and reinforce the possible biologic significance of tumor ARAC, especially in postmenopausal breast carcinoma patients.

Adult

[ELISA method for the determination of factor VII antigen].

The low plasma concentration of clotting factor VII makes it difficult to assay its antigenic fraction by the conventional methods of precipitation with specific antigens. Simple and peroxidase-conjugated antisera are currently available from commercial sources, thus allowing one to determine F VII:Ag by enzyme immunoassay. An ELISA method has been developed in this laboratory which provides sensitivity limits about 0.1% of the plasma concentration of F VII and correlates significantly with its functional activity (r = 0.603, n = 44, p less than 0.001). This technique can be highly helpful in characterising molecular variants of F VII, as well as in detecting acquired deficiencies of this factor.

Antigens

[A fast and simple method for obtaining specific anti-von Willebrand factor IgG].

Date expired commercial F.VIII concentrates (1.000 I.U. in 15 ml) were chromatographed through a Sepharose 4B in Tris-HCI (0.15 M, pH = 7.4) column. The void volume of this column was found to constitute an enriched vWF preparation. Half a milliliter of this preparation (protein content: 200 micrograms/ml) was mixed (1: 3) with Freund's complete adyuvant and administered to two rabbits by intramuscular route. A total of 3 doses were administered at days 1, 15 and 21 and the 2 animals were bled at day 30. The serum samples so obtained were pooled and analysed (DGD and IEP) for anti-vWF and anti-NHP activity. Strong anti-vWF specificity could be demosntrated. However, since a weak anti-fibrinogen and anti-IgG contaminant activity was also detected, the pool was filtered through a column containing normal human plasma coupled to a periodate activated Sephacryl S-1.000 immunoadsorbent. The filtrate, which was found to contain only a strong anti-vWF activity, was again processed by affinity chromatography through another Sephacryl immunoadsorbent containing a commercial F.VIII concentrate of the same lot employed for purifying the vWF. The eluate so obtained demonstrated to be constituted only by a pure rabbit IgG with strong anti-vWF specificity and was completely devoid of activity against any other human plasmastic protein. The method was found to be rapid, simple and economic, yielding as much as 5 mg of specific IgG for every 10 ml of antiserum so processed.

Antibody Specificity

[Biologic reagents].

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ABO Blood-Group System