Biomedical subjects

F Sichel

Publications and source records attributed to F Sichel.

25 records · Page 2Linked to original sources

PubMed1995

Serum galactosyltransferase activities in newborn children and pregnant women.

We have compared serum galactosyltransferase activity in pregnant women and in newborn children. Subjects in this study were 75 women at different stages of pregnancy and 60 newborns, including premature infants. Activity ratios in pregnant women are based on the period of gestation, expressed in weeks of amenorrhea. Average values were 265 nmol/h/ml for up to 12 weeks of amenorrhea, 369 from 13 to 28 weeks and 483 over 28 weeks versus 232 nmol/h/ml for non-pregnant women. In infants, galactosyltransferase activity decreased with increasing age from conception, but the activity level was always much higher in newborns than in women at the ninth month of pregnancy. We discuss the origin of the enzyme in these various samples.

Female↗

PubMed1994

Biological markers and ovarian carcinomas: galactosyltransferase, CA 125, isoenzymes of amylase and alkaline phosphatase.

We present a comparative study of several biological markers (galactosyltransferase, CA 125, isoenzymes of amylase and alkaline phosphatase) with a view to ovarian carcinoma follow-up. Serum samples were obtained from a population of 75 patients under clinical observation. After a minimum 18-months period, we assessed the prognostic value of the markers. No marker permits the detection of discrete, evolving carcinomas. CA 125 is the marker that gives the best results, particularly in terms of sensitivity. Galactosyltransferase has a lower sensitivity except in the case of endometrioid carcinomas. Simultaneous analysis with CA 125 and galactosyltransferase results in no decisive improvement, other than greater precision in unfavourable prognoses. Isoenzymes of amylase and alkaline phosphatase are of no interest in the follow-up of such carcinomas.

Alkaline Phosphatase↗

PubMed1991

[Localization and modulation of galactosyltransferase during in vitro proliferation of a human ovarian adenocarcinoma cell line].

A cell line, IGROV1, originating from a human ovarian cancer, releases a galactosyltransferase activity in its culture medium during proliferation. The proliferating IGROV1 cells appear as two populations: some cells grow in floating clusters whereas the greater part of them adhere to the culture substrate. The study of galactose transfer by intact cells onto an exogenous glycoprotein acceptor (ovomucoid) shows the presence of surface-associated galactosyltransferase onto the two cellular sub-populations. Opposite to intracellular activity, surface-associated and released galactosyltransferase activities depend on cellular adhesion and proliferation.

Adenocarcinoma↗

PubMed1990

A simple serum galactosyltransferase assay method suitable for routine use.

UDP-Galactose: N-acetylglucosaminyl glycoprotein beta 1-4 galactosyltransferase (GT) catalyzes the transfer of galactose to N-acetylglucosamine from UDP-[3H]Gal. The uncharged reaction product (tritiated N-acetyllactosamine) is separated from the unreacted UDP-[3H]Gal by ion-exchange chromatography. The major advantage of this method is its rapidity compared to other isotopic techniques.

Chromatography, Ion Exchange↗

PubMed1990

Alteration in isoenzyme patterns of serum galactosyltransferase activity in ovarian cancer patients: preliminary results.

Isoelectric focusing on agarose gel was used to separate the isoenzymes of serum galactosyltransferase (uridine diphosphogalactose: N-acetylglucosaminyl galactosyltransferase, EC 2.4.1.22) from 8 healthy women, and 11 ovarian cancer patients of whom 4 were in clinical remission. In all cases, we found 7 major peaks with isoelectric points ranging from 4.0-5.4. The most acidic peaks were preferentially elevated in the tumor-bearing patients, particularly the peak with pI 4.44.

Aged↗

PubMed1988

Serum galactosyltransferase activity with three acceptors in ovarian cancer patients.

Several laboratories have demonstrated the usefulness of serum galactosyltransferase as a biological marker for ovarian neoplasms. However, contradictory results have been published recently, which might be partially explained by differences in methodology. We thus decided to measure serum galactosyltransferase activity in patients with ovarian cancer and benign gynecological diseases using three different assay systems. A very good correlation was obtained between the results of these assays. Furthermore, we confirm that serum GT is frequently elevated in cancer patients, and is of potential value for their follow-up.

Acetylglucosamine↗

PubMed1988

[Comparative study of various technics for the determination of human serum galactosyltransferase].

We have compared three assays for serum galactosyltransferase activity, which use ovomucoïd, asialo agalactofetuin and free N-acetylglucosamine respectively as exogenous acceptors. A very good correlation between the three assays is obtained, for the whole range of GT activity. When the methods are compared to one another, the slopes of the regression lines are similar whether the sera are collected from healthy controls, pregnant women, or women suffering from benign gynecologic diseases or ovarian neoplasms. The methods which uses free N-acetylglucosamine as acceptor is rapid, cheaper and easier to perform.

Female↗