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Biomedical subjects

E Devinoy

Publications and source records attributed to E Devinoy.

At least 37 records · Page 2Linked to original sources
PubMed1994

Variation of transferrin mRNA concentration in the rabbit mammary gland during the pregnancy-lactation-weaning cycle and in cultured mammary cells. A comparison with the other major milk protein mRNAs.

The concentration of transferrin mRNA was evaluated during pregnancy and lactation in rabbit mammary gland and liver using northern blot and dot blot assays. Transferrin mRNA was present in the virgin rabbit mammary gland and its concentration increased as pregnancy proceeded, with a major enhancement after day 15. A high concentration was reached 3 days after parturition, with no additional increase during lactation and with a marked decline after weaning. During the same period, the concentration of transferrin mRNA showed only a very weak variation in liver. This mRNA was six times more abundant in mammary gland than in liver of lactating rabbit. The accumulation of transferrin mRNA in the mammary gland was concomitant with the accumulation of alpha s1-, beta-, kappa-casein and WAP (whey acidic protein) mRNAs. The concentration of glyceraldehyde 3-phosphate dehydrogenase mRNA, taken as a non-inducible control mRNA, declined progressively during pregnancy to reach its lower level in lactation. These observations suggest that casein, WAP and transferrin mRNAs are subjected to a similar control mechanism in vivo, at least in the second half of pregnancy and during lactation. Experiments carried out in vitro using isolated rabbit epithelial mammary cells cultured on collagen I gel indicated that transferrin mRNA was abundant and only weakly inducible by the lactogenic hormones insulin, cortisol and prolactin, as opposed to caseins and WAP mRNAs. R5020, an analogue of progesterone, inhibited at most very slightly the accumulation of alpha s1-casein mRNA in the presence of prolactin and it did not reduce the expression of transferrin gene.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1993

Characterization of rabbit kappa-casein cDNA: control of kappa-casein gene expression in vivo and in vitro.

The rabbit kappa-casein cDNA was cloned and sequenced. One of the isolated clones included almost the entire 5' end, while another clone corresponded to the 3' end of the cDNA. No polyadenylation site was found and therefore this clone did not harbour the complete cDNA. The amino acid sequence of a full-length protein was deduced from the nucleotide sequence obtained for this partial cDNA. It revealed the presence of a chymosin cleavage site and five potential phosphorylation sites. Rabbit kappa-casein was compared with those already described in other species. The rabbit sequence is closer to the ovine than to the mouse sequence. This result supports the idea that Lagomorpha are not closer to Rodentia than to Artiodactyla. The cDNA described above was used to study kappa-casein gene expression in the rabbit mammary gland. This expression was induced primarily by prolactin in mammary gland organoids and was similar to alpha s1-casein gene expression in vivo. The kappa-casein gene present in the casein gene locus is thus subject to the same regulation as the alpha s1-casein gene, although it has evolved from a fibrinogen gene.

Amino Acid Sequence↗
PubMed1992

A 17.6 kbp region located upstream of the rabbit WAP gene directs high level expression of a functional human protein variant in transgenic mouse milk.

We have investigated whether DNA regions present in the rabbit whey acidic protein (WAP) promoter/5' flanking sequence could potentially confer, in vivo, high level expression of reporter genes. Transgenic mice were generated expressing a variant of human alpha 1-antitrypsin, which has inhibitory activity against plasma kallikrein under the control of a 17.6 kbp DNA fragment located upstream of the rabbit WAP gene. Up to 10 mg/ml of active and correctly processed recombinant protein were detected in mouse milk, thus suggesting that the far upstream DNA sequences from the rabbit WAP gene might be useful for engineering efficient protein production in the mammary glands of transgenic animals.

Animals↗
PubMed1992

Structure of the gene encoding rabbit alpha s1-casein.

The complete nucleotide sequence of the entire rabbit alpha s1-casein-encoding gene Aslca and its flanking regions was determined. These data represent the first complete primary sequence of an Aslca gene. The gene consists of 19 exons spread over 16 kb. Highly conserved sequences were found between this gene and other casein-encoding genes mainly upstream from the gene from position -180 to -10. Several repeated interspersed elements of unknown function were also identified within introns.

Amino Acid Sequence↗
PubMed1992

A distal region enhances the prolactin induced promoter activity of the rabbit alpha s1-casein gene.

Casein gene expression is induced in the rabbit mammary gland by prolactin (PRL). alpha s1-casein is the major casein secreted into milk. In order to define the position of the DNA sequences involved in the control of rabbit alpha s1-casein gene regulation by PRL, chimeric genes were constructed between upstream regions of the rabbit alpha s1-casein gene and the chloramphenicol acetyl transferase (CAT) reporter gene. A series of 5'-deleted fusion genes was obtained by nuclease digestion of the alpha s1-casein gene upstream region. These gene constructs were transfected into rabbit primary mammary cells, or cotransfected in CHO cells with the plasmid coding for the rabbit mammary receptor (PRL-R). A regulatory region has been located between nt -3768 and -3155. This region enhances the prolactin induced promoter activity of the alpha s1-casein gene. It might possess or cooperate with prolactin responsive elements located further downstream in the alpha s1-casein gene.

Animals↗
PubMed1991

Structure of the gene encoding rabbit beta-casein.

The entire rabbit beta-casein-encoding gene and 400 bp upstream were sequenced. Eight introns, located essentially at a position similar to the corresponding gene in other species, were found. Strong homology with several casein-encoding genes from rabbit and from other species was observed in the upstream region of the gene. Repeated sequences of unknown function were also located within introns.

Amino Acid Sequence↗
PubMed1991

Hormone responsive elements within the upstream sequences of the rabbit whey acidic protein (WAP) gene direct chloramphenicol acetyl transferase (CAT) reporter gene expression in transfected rabbit mammary cells.

Whey acidic protein gene transcription is induced in the mammary gland under the influence of lactogenic hormones: prolactin, insulin and cortisol. The rabbit WAP gene has already been isolated and sequenced in a previous work. In the present study, we have evaluated the role of the 5' flanking region of the rabbit WAP gene in the transcriptional regulation of the WAP gene by using a reporter CAT gene. Chimeric genes containing the upstream region of the WAP gene have been linked to the bacterial CAT gene and transfected into rabbit primary mammary cells. The results reported here show that two regions carrying important regulatory elements of the rabbit WAP gene are located between -6300 and -3000 bp, and between -3000 and -1800 bp upstream from the WAP transcription start point, respectively. The contribute to the high level of expression of the rabbit WAP gene in the mammary cell.

Animals↗
PubMed1988

Recent data on the structure of rabbit milk protein genes and on the mechanism of the hormonal control of their expression.

Mammary explants or isolated mammary cells from rabbit have been cultured in the presence of insulin, prolactin and cortisol alone or in combination. The cellular content in alpha s1-casein, beta-casein and whey acidic protein (WAP) mRNA have been evaluated using the corresponding cDNA as probes. In all cases alpha s1-casein mRNA was the most abundant and WAP mRNA the least abundant mRNA. The three genes showed essentially similar dependency towards hormones. Prolactin stimulated mRNA accumulation and insulin and cortisol amplified this stimulation. The induction by prolactin was rapid whereas stimulation by insulin was slower. Fragments of rabbit genomic DNA inserted in lambda phage and containing alpha s1-casein, and WAP genes have been cloned. The primary sequence around the CAP site of the three genes has been established. A comparison of the sequences located upstream from the CAP site shows several striking homologies with the corresponding genes from cow, rat and guinea-pig. This suggests that these sequences participate in the transcriptional control of the genes by hormones. The mechanism involved in the transduction of the prolactin message to milk protein genes in unknown. Using mammary explants in culture, several classical mechanisms of transduction have been examined. Phorbol ester, phorbol -12, 13-dibutyrate (PdiBu) inhibited prolactin action. However, another tumor promoter, 12-O-tetradecanoyl phorbol-13-acetate (TPA), did not alter prolactin action. Kinase C inhibitor H7 did not prevent prolactin action and did not overcome the inhibition by PdiBu. Kinase C is therefore not essential for the transduction of the prolactin message to milk protein gene. Neomycin, which inhibits phosphatidylinositol hydrolysis by phosphorylase C, prevented prolactin action, whereas other inhibitors of phosphatidylinositol metabolism remained uneffective. Degradation of phosphatidylinositol is therefore likely not an essential step of prolactin action on milk protein genes. Inhibitors of tyrosine kinase and phosphatase exhibited a poor capacity to modify the prolactin response. Hence, transduction mechanisms using tyrosine kinase activity likely cannot account for prolactin action.

Animals↗
PubMed1985

Hormonal action controlling mammary activity.

Mammary gland differentiation includes multiplication of cells, activation of genes specific to milk synthesis, and activation of "house-keeping" genes. These events are controlled by multiple hormones, the roles of which are not known in detail. Prolactin induction of milk synthesis is accompanied by accumulation of casein messenger ribonucleic acid resulting from acceleration of casein gene transcription as well as stabilization of messenger ribonucleic acid. Prolactin also favors translation of casein messenger ribonucleic acid. Glucocorticoids amplify and progesterone inhibits prolactin action on transcription of casein genes.

Animals↗
PubMed1979

Role of glucocorticoids and progesterone in the development of rough endoplasmic reticulum involved in casein biosynthesis.

Hydrocortisone acetate injected into pseudopregnant rabbits induced casein synthesis and a parallel accumulation of casein mRNA. These effects were not accompanied by any enrichment of total RNA in the mammary cell. Hydrocortisone acetate did not favour the attachment of polysomes to endoplasmic reticulum. Casein mRNA concentration was enhanced in free and membrane-bound polysomes. After long treatments, the concentration of casein mRNA reached a plateau in membrane bound polysomes whereas it continued to be accumulated in free polysomes, suggesting that a substantial part of casein synthesis is then carried out by free polysomes. Progesterone injected with high doses of prolactin was unable to prevent the stimulatory action of prolactin on the synthesis of casein, the accumulation of casein mRNA and mammary gland growth, as judged by DNA content. By contrast, the increase in the total RNA content of mammary gland was still significantly reduced by progesterone. In addition, progesterone inhibited almost completely the formation of membrane-bound polysomes and the anchorage of casein mRNA to endoplasmic reticulum. From these data, it was concluded that the formation of the endoplasmic reticulum is not a prerequisite for the initiation of casein synthesis. Glucocorticoids do not play a major role in the formation of the endoplasmic reticulum and the Golai apparatus and in the binding of casein synthesizing polysomes to membranes. Progesteronne is capable of inhibiting preferentially and gradually the stimulation of cellular functions requiring the most potent prolactin stimulation.

Animals↗
PubMed1978

Role of prolactin and glucocorticoids in the expression of casein genes in rabbit mammary gland organ culture. Quantification of casein mRNA.

Milk synthesis is initiated solely by prolactin in the pseudopregnant rabbit and glucocorticoids potentiate this action of prolactin. In organ culture, prolactin, in the presence or in the absence of insulin, enhances casein synthesis and cortisol (inactive alone) amplifies this action. Measurements of casein mRNA concentration in total cellular RNA, by hybridization with DNA complementary to casein mRNA, revealed that the stimulation of casein synthesis by the glucocorticoid is accompanied by an increase in the amount of casein mRNA. A systematic comparison of variations of these two parameters indicated that the major effect of glucocorticoids on lactogenesis in the rabbit at this stage of mammary gland development is mediated through an increase in the quantity of casein mRNA available for translation. No simultaneous control of casein mRNA translation by cortisol was observed.

Animals↗
PubMed1978

Role of spermidine in casein gene expression in the rabbit.

Spermidine concentration in rabbit mammary gland was estimated during pregnancy, lactation and after the induction of milk synthesis by prolactin and glucocorticoids in vivo and in vitro. It was observed that mammogenesis and lactogenesis during preganancy and the initiation of milk secretion at parturition are accompanied by an enhancement of spermidine concentration in the mammary gland. By contrast, the initiation of these phenomena by hormone injections does not require such variations of spermidine concentration. In organ culture, a slight increase in spermidine concentration was obtained under the influence of an hormonal combination including insulin, prolactin and cortisol. Spermidine added to the culture medium was unable to mimic cortisol action. An amplification of casein synthesis and a parallel increase of casein mRNA concentration was provoked by cortisol even when spermidine synthesis was blocked. Thus, one of the major actions of glucocorticoids during lactogenesis in the rabbit is not mediated through an increase in spermidine concentration in the mammary gland.

Animals↗