Search PubMed⌕ Search

Biomedical subjects

A Jullienne

Publications and source records attributed to A Jullienne.

At least 73 records · Page 4Linked to original sources
PubMed1984

Calcitonin mRNA activity in young obese (fa/fa) Zucker rats.

Alterations in both calcitonin (CT) secretion and plasma calcium were recently described in adult obese Zucker rats. We have investigated the CT biosynthetic activity of thyroid glands in 30-day-old obese Zucker rats (fa/fa), and their controls (Lean). Plasma calcium level was significantly increased (+0.6 mg/dl) in obese animals, but plasma phosphate was unchanged. Plasma CT levels measured by radioimmunoassay (RIA) were significantly decreased in fatty (0.50 +/- 0.03 vs 0.68 +/- 0.03 ng/ml in Leans; P less than 0.001), but thyroidal hormone content was not different between Lean and fatty rats (68.7 +/- 5.1 in Leans vs 60.5 +/- 3.6 ng/gland in fatty rats). mRNA was extracted from 10 thyroids, and translated in a rabbit reticulocyte lysate (NEN) in the presence of [35S]methionine. After polyacrylamide gel electrophoresis, specific immunoprecipitates were autoradiographed and quantified by integration. A 50% decrease in translatable CT mRNA was observed in fatty rats. In basal conditions, the biosynthetic activity of C cells in obese rats correlates with the secretion rate of the hormone in the face of unchanged thyroidal CT contents.

Animals↗
PubMed1984

Rapid increase of calcitonin-specific mRNA after acute hypercalcemia.

The regulation of calcitonin (CT) secretion by calcium was studied by measuring CT mRNA extracted from thyroids of normal rats subjected to acute calcium stimulation in vivo. The 15000-Mr primary translation product of CT mRNA was identified by immunoprecipitation using specific antibodies. While total mRNA and total radioactivity incorporated after translation of total mRNA remained unaffected by the calcium stimulation, a fourfold increase in radioactivity incorporated in CT primary translation product occurred as early as 2 min after calcium administration. This peak coincided with a rise in plasma levels of the hormone and preceded a detectable decrease in tissue stores. These results suggest that calcium ion, either directly or indirectly via its action on intracellular stores of the hormone or its precursors, causes a rapid increase in cell levels of translatable CT mRNA. In view of the extremely short time (2 min) in which this increase occurs, the action is probably at the post-transcriptional level as no increase in CT mRNA levels could be detected by hybridization assay using a specific cDNA probe for human CT mRNA.

Acute Disease↗
PubMed1984

The complete sequence of human preprocalcitonin.

DNA complementary to mRNA extracted from the thyroid glands of patients suffering from medullary carcinoma of the thyroid (MCT), a calcitonin-producing tumour, was inserted in the Pst site of pBR 322 by G-C tailing. The recombinant plasmids were used to transform Escherichia coli DP 50. Ampicillin-resistant clones were screened using a 32P-labelled cDNA to mRNA extracted from a case of MCT particularly rich in calcitonin (CT) mRNA. Positive clones were subsequently rescreened using a 32P poly(T) probe. Eighty clones were thus purified, and the inserts obtained by digestion with PstI were subjected to positive hybridization selection with subsequent translation in vitro. An insert stimulating synthesis of the protein and containing restriction sites compatible with the previously published complete sequence of calcitonin mRNA from rat was sequenced. This cDNA insert contained the entire coding region of 426 bp, 70 bp at the 5'-end, and 295 bp upstream from the poly(A) tail. The complete amino acid sequence of human preprocalcitonin could thus be deduced.

Amino Acid Sequence↗
PubMed1984

Ultrastructural localization of immunoreactive calcitonin in the two cell types of the ultimobranchial gland of the common toad (Bufo bufo L.).

The ultimobranchial (UB) glands of the common toad Bufo bufo consist of several cellular masses containing two quite different cell types which line a central lumen filled with amorphous material. The morphologically defined Type I cell is akin to a typical calcitonin secretory cell as observed for all vertebrates, with small dense-core secretory granules. On the contrary the Type II cell displays large apical dense bodies which may be related to the secretion and/or absorption of the amorphous material. Cells morphologically related to Type II cells have been described in the UB glands of Sauropsidea and in the UB follicles of mammalian thyroid gland. An immunocytochemical stain using an antiserum raised against synthetic salmon calcitonin demonstrated the specific localization of an immunoreactive product in both Type I and Type II cell granules, suggesting that both cell types could be involved in calcitonin metabolism. Moreover, the presence of immunoreactive calcitonin in the Type II cells of the Bufo UB gland raises the question of the function of the morphologically equivalent cells of other species.

Animals↗
PubMed1983

Cell free translation of chicken calcitonin messenger RNA.

The primary step of calcitonin biosynthesis was studied in a normal organ: chicken ultimobranchial gland, a tissue particularly rich in calcitonin secretory cells. Poly(A)-rich RNA was extracted and purified from ultimobranchial organs and translated in a reticulocyte lysate in the presence of labelled methionine. Polyacrylamide gel electrophoresis of specific immunoprecipitates revealed a major band of Mr 14 500 and a band of Mr 13 300. Thus, in chicken the precursor of calcitonin is a Mr 14 500 polypeptide. The minor component of Mr 13 300 could represent limited processing by the reticulocyte lysate.

Animals↗
PubMed1980

Physicochemical characteristics of carcinoembryonic antigen extracted from medullary carcinoma of the thyroid.

Carcinoembryonic antigen (CEA) and calcitonin (CT) were extracted from medullary carcinoma of the thyroid (MCT) tissues, fractionated on Sephacryl S-200 and chromatographed on Concanavalin A. CEA purified from MCT is closely related to CEA extracted from colonic tumors. It has an equivalent molecular weight, is a glycoprotein and has a similar electrophoretic mobility in both SDS and basic polyacrylamide electrophoresis. A certain degree of heterogeneity is present in the form of a smaller molecular weight component. Large molecular forms of CT which are present in MCT tissues and which co-elute with the minor component of CEA on Sephacryl chromatography can be separated by Concanavalin A chromatography.

Carcinoembryonic Antigen↗
PubMed1979

Immunochemical studies on rabbit calcitonin.

Cross reaction studies using radioimmunoassays specific for human and porcine calcitonin showed that rabbit calcitonin is structurally more closely related to human than to porcine calcitonin.

Animals↗
PubMed1978

[Hypercalcemia and biologically active parathyroid hormone].

Hypercalcaemia always results in serious clinical sequalae and, if not treated, carries a most unfavourable prognosis. The clinician will gain major diagnostic help from an evaluation of the calcitonin and parathyroid hormone blood levels. With regard to parathyroid hormone we have developed, for the first time, a radioimmunoassay which is specific for the estimation of biologically active hormone in the circulation. We are dealing here with an unusual radioimmunological situation as the immunochemical sites are generally quite distinct from those associated with hormonal activity. We are presenting in this first paper the normal values and also the variations that occur in different types of hypercalcaemia. The comparison of these results with those obtained by the usual methods of estimation for parathyroid hormone assay lacking in biological activity shows the value of this new technique.

Calcitonin↗
PubMed1975

[Heterogeneity of immunoreactive calcitonin in the plasma of patients with bone marrow cancer].

Plasma from patients with medullary carcinoma containing very high levels of immunoreactive calcitonin were fractionated by filtration on Sephadex gel. In all cases the elution gave four immunoreactive fractions. Two of these fractions correspond to the volume of elution of the monomere and of the dimere of human calcitonin. The two other fractions emerge at an elution volume corresponding to much higher molecular weights. After stimulation of calcitonin secretion in vivo, by dynamic tests, the fractions corresponding to the monomere and dimere increase more strongly than the two other fractions. Preliminary studies of secretion, in vitro, of calcitonin by medullary carcinoma tissue, show the presence in the incubate of four immunoreactive forms having the same elution characteristics as those found in the plasma. The significance of these results is discussed.

Bone Marrow Diseases↗