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C Jolicoeur

Publications and source records attributed to C Jolicoeur.

At least 19 recordsLinked to original sources
PubMed1990

Mucoadhesion of hydroxypropylmethacrylate nanoparticles to rat intestinal ileal segments in vitro.

The purpose of this study was to evaluate the adhesion of HPMA nanoparticles to mucus using a perfused rat ileum test system. Radiolabeled nanoparticles were prepared and deposited onto rat ileal segments in vitro. The segments were perfused and the perfusate was collected in fractions and assayed for radioactivity. Between 10 and 50% of the radioactivity was eliminated over the first 120-sec perfusion, whereas the remaining activity was firmly attached to the ileum. Among the variables tested, the time interval between nanoparticle deposition and perfusion played the major role, indicating that the mucus-nanoparticle interaction is likely to result from the diffusion of polymers into the mucus and of mucin into the polymeric matrix.

Acrylates↗
PubMed1990

Determinants of the B-cell response against a transgenic autoantigen.

The failure to induce self-tolerance of simian virus 40 large tumor antigen (T antigen) expressed in the pancreatic beta cells of transgenic mice results in an autoimmune response against this protein and the cells that synthesize it. In every transgenic mouse with delayed onset of T-antigen expression and consequent nontolerance, B cells, T cells, and macrophages are attracted to and infiltrate the pancreatic islets. In contrast, the incidence, onset, and intensity of the B-cell response to produce anti-T-antigen autoantibodies vary considerably with genetic background. Thus the initial attraction of lymphocytes to the cells synthesizing a non-self antigen can be separated from the activation of a B-cell response against it. Haplotypes of the major histocompatibility complex (MHC) differentially influence the character of the autoimmune response, with H-2d and H-2k conferring a high incidence of humoral autoimmunity. Additional non-MHC linked genes are also implicated in control of the B-cell response.

Animals↗
PubMed1990

Expression of two forms of prolactin receptor in rat ovary and liver.

The screening of a size-selected cDNA library from the ovary revealed the existence of a second form of PRL receptor in the rat. The polypeptide sequence deduced from cDNAs has a much longer cytoplasmic domain (357 amino acids) than the form previously identified in the liver (57 amino acids). Nucleotide sequence analysis and comparison with rabbit, mouse, and human PRL receptor cDNAs suggests that the two forms of rat PRL receptor result from alternative splicing of a primary transcript. Complementary DNAs encoding the long form of the receptor were also found in a library prepared from estradiol-treated rat liver, although they represent a minor fraction of total PRL receptor cDNAs obtained from this tissue. DNA polymerase chain reaction amplification of cDNA confirmed the presence of the two receptor forms in both the ovary and liver. Northern analysis, using probes that specifically hybridize with either form of mRNA, indicates a major transcript of 1.8 kilobases (kb) in estradiol-treated liver, which encodes the receptor with a short cytoplasmic domain, while the long form of the receptor is encoded by mRNAs of 2.5 and 3 kb. In the ovary, a complex pattern of hybridization to multiple mRNAs (1.8-5.5 kb) is obtained with the probe specific to the long form, and essentially only a 5.5-kb mRNA is obtained with the probe specific to the short form. The predicted size of the mature form of the long PRL receptor (PRL-R2) is 591 amino acid residues.(ABSTRACT TRUNCATED AT 250 WORDS)

Amino Acid Sequence↗
PubMed1989

New method for the preparation of cyanoacrylic nanoparticles with improved colloidal properties.

The purpose of this study was to prepare nanoparticles with a size significantly smaller than 0.1 micron. It was shown that when sulphur dioxide was dissolved in the cyanoacrylic monomer at a high concentration, subsequent anionic polymerization in an aqueous phase produced particles as small as 10 nm. Moreover, the obtained particles displayed an important negative charge which improve their stability against aggregation. Finally, nanoparticles were successfully prepared in double-distilled water, thereby avoiding the use of dextran which can induce anaphylactoid reactions.

Chemistry, Pharmaceutical↗
PubMed1989

Identification and sequence analysis of a second form of prolactin receptor by molecular cloning of complementary DNA from rabbit mammary gland.

Two lambda gt11 clones containing fragments of cDNA encoding the prolactin receptor from rabbit mammary gland were isolated using a rat liver prolactin receptor cDNA probe. An 1848-base-pair open reading frame encodes a mature prolactin-binding protein of 592 amino acids that contains three domains: (i) the extracellular, amino-terminal, prolactin-binding region of 210 residues; (ii) the transmembrane region of 24 residues; and (iii) the intracellular, carboxyl-terminal domain of 358 residues. This latter domain is much longer than the cytoplasmic domain (57 residues) previously described for the rat liver prolactin receptor. In addition, the sequence identity of this form of prolactin receptor with the growth hormone receptor is extended in the cytoplasmic domain.

Amino Acid Sequence↗
PubMed1989

Purification, cloning, and expression of the prolactin receptor.

The rat liver prolactin receptor has been purified to homogeneity, and partial amino acid sequences have been obtained. The structure of the receptor has been deduced from a single complementary DNA clone. The mature protein of 291 amino acids has a relatively long extracellular region, a single transmembrane segment, and a short (57 amino acids) cytoplasmic domain. With the rat cDNA used as a probe, the prolactin receptor in rabbit mammary gland and human hepatoma cells has also been isolated. These tissues contain a second, longer form of the receptor (592 and 598 amino acids, respectively). Both the short and long forms of the prolactin receptor show regions of strong sequence identity with the human and rabbit growth hormone receptors, suggesting that the prolactin and growth hormone receptors originate from a common ancestor.

Amino Acid Sequence↗
PubMed1989

Multiple regulation of prolactin receptor gene expression in rat liver.

Sex steroids are major regulators of PRL receptor expression in rat liver. Using a probe encoding the rat PRL receptor we have studied receptor mRNA levels in female rat liver during ontogeny and in response to estrogen treatment. Steady state mRNA levels were determined by Northern blot and densitometric analysis. Messenger RNA levels have been compared to the number of binding sites, which was assessed by Scatchard analysis of [125I]ovine PRL binding in membrane preparations. Our results show that steady state mRNA and binding levels of PRL receptors are both regulated by development and estrogens, but that binding does not exactly parallel mRNA levels. From the developmental stages of prepuberty to adult, receptor numbers increase 8-fold, whereas mRNA levels increase 3-fold. Estrogen treatment stimulates receptor levels 6-fold, but mRNA levels are only increased 3-fold. These results suggest that PRL receptor gene expression in rat liver is regulated at the transcriptional or posttranscriptional level as well as at the translational level.

Animals↗
PubMed1989

Identification of a cDNA encoding a long form of prolactin receptor in human hepatoma and breast cancer cells.

Human PRL receptor cDNA clones from hepatoma (Hep G2) and breast cancer (T-47D) libraries were isolated by using a rat PRL receptor cDNA probe. The nucleotide sequence predicts a mature protein of 598 amino acids with a much longer cytoplasmic domain than the rat liver PRL receptor. Although this extended region has additional segments of localized sequence identity with the human GH receptor, there is no identity with any consensus sequences known to be involved in hormonal signal transduction. This cDNA will be a valuable tool to better understand the role of PRL in the development and growth of human breast cancer.

Amino Acid Sequence↗
PubMed1989

[Prolactin receptor: characterization by monoclonal antibodies and cloning of complementary DNA].

Rat liver prolactin receptor has been partially characterized and purified to homogeneity using monoclonal antibodies. Pure receptor was digested with trypsin and amino acid sequence of receptor fragments determined. This allowed us to clone the prolactin receptor cDNA. Our approach to clone the receptor cDNA consisted of synthesizing oligonucleotides corresponding to the amino acid sequence of receptor fragments, and to screen a cDNA library. Sequencing reveals that prolactin receptor is a 291 amino acid protein, containing an extracellular domain of 210 residues, a single transmembrane segment of 24 amino acids and a cytoplasmic domain of 57 amino acids. Introduction of the prolactin receptor cDNA into various cell types demonstrates that the single protein is sufficient to bind prolactin with the same affinity and specificity reported for the prolactin receptor.

Animals↗
PubMed1988

Cloning and expression of the rat prolactin receptor, a member of the growth hormone/prolactin receptor gene family.

The primary structure of the rat liver prolactin receptor has been deduced from a single complementary DNA clone. The sequence begins with a putative 19 amino acid signal peptide followed by the 291 amino acid receptor that includes a single 24 amino acid transmembrane segment. In spite of the fact that the prolactin receptor has a much shorter cytoplasmic region than the growth hormone receptor, there is strong localized sequence identity between these two receptors in both the extracellular and cytoplasmic domains, suggesting that the two receptors originated from a common ancestor.

Amino Acid Sequence↗
PubMed1987

Lipid analysis of a novel type of cell secretion in the exocrine pancreas: the pancreasomes.

A novel type of cell secretion termed 'microvesicular secretion' has been described recently in the exocrine pancreas. According to this process, microvesicles are released by acinocytes in the pancreas acinar lumen. These microvesicles, identified as 'pancreasomes', were characterized by the presence of a major glycoprotein component originating in the exocrine acinar cell. In the present work, phospholipids of pancreasomes have been identified. Five classes of phospholipid were found: phosphatidylcholines, phosphatidylethanolamines, lysophosphatidylcholines, sphingomyelins and another minor class of ninhydrin-positive phospholipid (phosphatidylserines or lysophosphatidylethanolamines). The ratios of neutral lipids to phospholipids were particularly high (3:1), as estimated by GLC of their fatty acid content. Analysis of fatty acid composition of pancreasomes lipids revealed a very high proportion of two saturated fatty acids, palmitic (40%) and stearic (24%), whereas two main unsaturated fatty acids, oleic (17%) and linoleic (8%), were found in smaller proportions. Differential scanning calorimeter studies on washed pancreasomes indicated that there was no lipid phase transition in their membrane, despite the absence of cholesterol. Our observations show that pancreasomes have an unusual lipid composition and confirm our previous conclusion based on protein analysis that the release of pancreasomes occurs according to an hitherto undescribed type of secretion, in which a glycoprotein is released associated with specific domains of the luminal plasma membrane.

Animals↗
PubMed1987

Changes in the messenger RNA population from the heart of cardiomyopathic hamsters.

Messenger RNAs were extracted from the heart of cardiomyopathic hamsters at different phases of the disease and from age-matched control hamsters. They were translated into proteins in a rabbit reticulocyte lysate in the presence of [35S]methionine, the translational products were fractionated by two-dimensional polyacrylamide gel electrophoresis and analyzed by fluorography. No difference between cardiomyopathic and control hamsters could be detected when comparing the spots corresponding to the major contractile proteins. However, we observed that three translational products of minor abundance were reproducibly decreased in cardiomyopathic hamsters at 60 days (necrotic phase) and 200 days (final phase) but not at 30 days (prenecrotic phase). At 120 days (hypertrophic phase), the decrease could also be detected but was much less pronounced.

Animals↗
PubMed1987

Flow microcalorimetry investigation of the influence of surfactants on a heterogeneous aerobic culture.

The influence of various surfactants on the biological activity of a mixed aerobic culture has been investigated by using flow microcalorimetry. The response of the culture to the addition of homologous n-alkylcarboxylates (C2 to C16) and n-alkylpyridinium bromides (C11 to C14) has been examined under endogenous and substrate saturation conditions, and inhibitory concentrations (MIC or the concentration which decreased the initial activity (heat flux) of the culture by 50%) were determined for each state. Under both conditions, the n-alkylpyridinium bromides were found to be more toxic than the n-alkylcarboxylates of identical chain length, thus confirming that the head group of the amphiphiles plays an important role in the microbial toxicity of surfactants. The relationship observed between the concentration at which 50% of the activity is lost and the chain length of the surfactant further confirms that cellular toxicity is also dependent on surfactant hydrophobicity. In relation to the biodegradability of surfactants in mixed aerobic cultures, the low concentration effects of n-alkylcarboxylates on endogenous culture were investigated in some detail. There appear to be compounded indications that these surfactants are rapidly metabolized by the microorganisms of the mixed culture, at least for homologs lower than C10.

Bacteria, Aerobic↗
PubMed1983

The 60S ribosomal subunit is altered in the skeletal muscle of dystrophic hamsters.

Polysomes from the skeletal muscle of normal and dystrophic hamsters were dissociated into ribosomal subunits by treatment with puromycin and the subunits from both strains were reassociated in all possible combinations. When their protein synthesis activity was assayed in a poly(U)-directed cell-free system at a low magnesium concentration, the reassociated ribosomes from dystrophic hamsters were less active than the ribosomes from control animals. The ribosomal defect is a property of the 60S subunit and is due to a ribosomal component rather than to abnormal binding of a non-ribosomal protein.

Animals↗
PubMed1983

A ribosomal defect in dystrophic hamsters.

Polysomes were isolated from the skeletal muscle, the heart, and the liver of dystrophic and normal hamsters and their protein synthesis activity was assessed in a cell-free wheat germ extract as a source factors and tRNAs. Our results show that there is a shift of the optimal magnesium concentration required for protein synthesis with polysomes from the skeletal muscle and the heart of dystrophic hamsters, as compared with control hamsters. As a consequence of this shift, polysomes from the skeletal muscle and the heart of dystrophic hamsters, were less active than normal ones at low magnesium concentrations, but more active at high magnesium concentrations. These changes in activity were age dependent since, with skeletal muscle, they were observed at 30 days and disappeared at 60 days but reappeared at 120 and 200 days. With heart polysomes, on the other hand, the changes in activity were observed at 60 days but not in younger or older animals. No change in activity was observed with liver polysomes. Similar results were obtained when endogenous mRNAs were replaced by an exogenous messenger such as poly(U). This suggests that the differences in protein synthesis activity between polysomes from dystrophic and normal hamsters are not due to changes in the endogenous mRNAs but result from a ribosomal abnormality.

Animals↗
PubMed1983

Endometrial hyperplasia and neoplasia. Cytologic screening with the Endopap endometrial sampler.

A new endometrial sampling device, the Endopap, was tested in a series of 851 patients. This sampler is of simple design, without moving parts, inexpensive and easy to use. Cellular samples proved adequate in 90% of the cases, usually with very abundant material. Endometrial cancer shed atypical cells in all 20 cases studied. However, only about half the patients with adenomatous hyperplasia were correctly identified by the endometrial sample. This fact seems to reflect the lack of adequate morphologic criteria for the recognition of endometrial hyperplasia; this situation prevails with all types of endometrial cell samplers.

Adenocarcinoma↗