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C Jean

Publications and source records attributed to C Jean.

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

Diminished diabetogenic effect of streptozotocin in adrenodemedullated rats.

Although stress is suspected to play a role in the development of diabetes mellitus, no direct experimental evidence for involvement of the adrenal medullae in onset of the disease has yet been found. We recently observed that, in comparison with sham-operated rats, fewer adrenodemedullated rats become diabetic after an i.v. injection of streptozotocin (STZ); thus, the present study examined the role of the adrenal medullae in the development of experimental diabetes. Male Wistar rats were surgically adrenodemedullated (ADM) or sham-operated (SHAM). After a 3-week recovery period, they were injected with 40 mg STZ/kg freshly dissolved in citrate buffer or buffer alone. A 1-mL arterial blood sample was withdrawn 12 days later in previously cannulated animals; then the rats were killed and their pancreas was removed. The plasma glucose levels were lower in ADM rats injected with buffer alone than in their SHAM counterparts (7.7 +/- 0.1 vs. 8.5 +/- 0.1 mmol/L; p < 0.05). The glucose levels were higher (p < 0.001) in both groups of STZ-treated rats, with values 28% lower in ADM than in SHAM rats (14.7 +/- 1.6 vs. 18.8 +/- 1.2 mmol/L; p < 0.03). Whereas plasma insulin levels did not differ between ADM and SHAM rats injected with buffer alone (431 +/- 38 vs. 428 +/- 35 pmol/L; p > 0.05), they were diminished in SHAM animals injected with STZ (292 +/- 37 vs. 428 +/- 35 pmol/L; p < 0.02).(ABSTRACT TRUNCATED AT 250 WORDS)

Adrenal Medulla↗
PubMed1993

Modulation of the interaction between G-actin and thymosin beta 4 by the ATP/ADP ratio: possible implication in the regulation of actin dynamics.

The interaction of G-actin with thymosin beta 4 (T beta 4), the major G-actin-sequestering protein in motile and proliferating cells, has been analyzed in vitro. T beta 4 is found to have a 50-fold higher affinity for MgATP-actin than for MgADP-actin. These results imply that in resting platelets and neutrophils, actin is sequestered by T beta 4 as MgATP-G-actin. Kinetic experiments and theoretical calculations demonstrate that this ATP/ADP dependence of T beta 4 affinity for G-actin can generate a mechanism of desequestration of G-actin by ADP, in the presence of physiological concentrations of T beta 4 (approximately 0.1 mM). The desequestration of G-actin by ADP is kinetically enhanced by profilin, which accelerates the dissociation of ATP from G-actin. Whether a local drop in the ATP/ADP ratio can allow local, transient desequestration and polymerization of actin either close to the plasma membrane, following platelet or neutrophil stimulation, or behind the Listeria bacterium in the host cell, while the surrounding cytoplasm contains sequestered ATP-G-actin, is an open issue raised by the present work.

Actins↗
PubMed1993

Effect of adrenal demedullation and (or) physical training on glucose tolerance in the rat.

Physical training increases insulin sensitivity by mechanisms not yet fully understood. Because exercise also modulates adrenergic system activity, the present study was designed to ascertain whether the improved glucose homeostasis observed in trained rats is influenced by epinephrine secretion from the adrenal medullae. Male Wistar rats previously submitted to adrenal demedullation or sham operated were kept sedentary or trained on a treadmill over a 10-week period. An intravenous glucose tolerance test (IVGTT) was done 64 h after the last bout of exercise. Basal plasma glucose levels were reduced by physical training (p < 0.005) and by adrenal demedullation (p < 0.001). Adrenodemedullated rats had lower (p < 0.005) plasma glucose levels than sham-operated animals over the whole glucose tolerance curve. Trained animals had lower (p < 0.01) plasma glucose levels than sedentary rats throughout the IVGTT, except at 45 min. The glucose disappearance rate measured after the glucose bolus injection was increased by training (p < 0.05), whereas it was not modified by adrenal demedullation. Basal plasma insulin levels were reduced (p < 0.001) by physical training but unaffected by adrenal demedullation. During the IVGTT, adrenodemedullated rats had higher (p < 0.01) plasma insulin levels at 2, 4, and 6 min, whereas trained animals had lower (p < 0.05) plasma insulin levels throughout the test. Moreover, insulin in adrenodemedullated and trained rats had returned to basal levels at 30 min. The area under the curve for insulin was diminished by physical training (p < 0.001) but was not modified by adrenal demedullation.(ABSTRACT TRUNCATED AT 250 WORDS)

Adrenal Medulla↗
PubMed1993

Cloning and sequence analysis of a cDNA encoding an androgen-dependent mouse seminal vesicle secretory protein.

We report the cloning and sequencing of a new cDNA sequence encoding a protein from the mouse seminal vesicle. An open reading frame of 297 nucleotides encoded a protein of 99 amino acids with a calculated molecular mass of 11.454 kDa. The first 21 amino acids constituted a signal peptide followed by 78 amino acids encoding the secreted protein. The cDNA sequence comprised a 3' untranslated region of 226 bp and the polyadenylation signal AATAAA, 19 bp upstream from the poly(A)+ tail. A high degree of homology was found between this protein and members of the family of seminal vesicle secretory (SVS) proteins, especially rat SVS VI. Northern blot analysis indicated the presence of a 0.7 kb mRNA species in the mRNAs of seminal vesicle tissue. Castration resulted in a marked decrease in the level of the 0.7 kb mRNA encoding the protein, whereas administration of testosterone to castrated males restored the 0.7 kb mRNA.

Amino Acid Sequence↗
PubMed1993

Radioimmunoassay of mouse vas deferens protein: developmental profile and hormonal regulation.

This study investigated the hormonal regulation of the developmental pattern of a major protein of the mouse vas deferens (MVDP) which represents 10% of the vas deferens protein content. Using a specific radioimmunoassay, MVDP was first detected in 10-day-old males and its concentration increased sharply between 10 and 30 days, reaching adult levels at 40 days. In adult males, MVDP disappeared after castration, and testosterone treatment for 15 days was necessary to reverse the effect of castration completely. In 10-day-old mice castrated at birth, MVDP levels were similar to those measured in controls of the same age. Testosterone administration from 1 to 10 days of age did not induce precocious accumulation of MVDP. These results suggested that the neonatal expression of MVDP is independent of androgens. From 10 to 30 days, the increase in MVDP levels was androgen-dependent as shown by the castration and injection experiments. In males castrated at birth, the androgen-induced accumulation of MVDP was greatly reduced in adulthood. This suggested that neonatal androgens are necessary to obtain full expression of the MVDP gene in adults.

Aging↗
PubMed1992

Adrenodemedullation does not impair the beneficial effect of physical training in streptozotocin-diabetic rats.

This study was designed to ascertain if the improvement in glucose homeostasis found in diabetic animals submitted to physical training is due to an increased secretion of epinephrine by the adrenal medullae. Male Wistar rats were surgically adrenodemedullated (ADM group) or sham-operated (SHAM group). After a 3-week recovery period, a bolus of streptozotocin (40 mg/kg) was injected intravenously (IV), and the animals presenting 1 week later with a blood glucose value between 14 and 22 mmol/L were retained in the protocol and randomly assigned to a sedentary (SHAM-DS and ADM-DS) or trained (SHAM-DT and ADM-DT) group. Physical training was done on a treadmill according to a 10-week progressive program. An IV glucose tolerance test (0.5 g/kg) was performed in previously cannulated rats, 64 hours after the last bout of exercise. Pancreatic insulin and glucagon content was also determined. In sedentary diabetic rats, adrenodemedullation had no effect on plasma glucose, insulin, or glucagon levels, neither in the basal state nor following the glucose load. Basal glucose levels were diminished by training in both SHAM (16.1 +/- 1.5 v 21.8 +/- 0.4 mmol/L; P less than .01) and ADM (12.4 +/- 1.7 v 21.1 +/- 1.2 mmol/L; P less than .01) groups, with values lower in ADM-DT than in SHAM-DT rats (P less than .05). After glucose loading, the glucose levels were significantly lower (P less than .01) throughout the test in both SHAM-DT and ADM-DT rats than in their sedentary counterparts.(ABSTRACT TRUNCATED AT 250 WORDS)

Adrenal Medulla↗
PubMed1992

The genomic organization and DNA sequence of the mouse vas deferens androgen-regulated protein gene.

The gene for mouse vas deferens protein (MVDP) is expressed, under androgenic control, exclusively in the epithelial cells of the deferent duct. As a first step in correlating cell-specific and hormonal regulations with the structure of the gene, the complete sequence of the MVDP gene (11 kb) and 0.5 kb of the 5' flanking region have been determined. The size range for the 10 exons is 78 to 168 bp, whereas that of introns is 292 to 2833 bp. A major site of transcription is located on an A residue 46 nucleotides upstream from the A of the ATG initiation codon. A TATA (CATAA) box, a CAAT box, a GC-rich motif and a (5'-TGTTCT-3') element that closely resembles the consensus sequence of the androgen response elements are present in the 5' flanking region of the MVDP gene.

Aldehyde Reductase↗
PubMed1992

In vitro androgenic induction of a major protein in epithelial cell subcultures from mouse vas deferens.

Pure epithelial cell cultures, obtained from primary culture of vas deferens tissue collected from 20- to 30-day-old mice, were amplified by subculturing the cells over 3T3 feeder layer in a serum-free defined medium. Adhesion and proliferation of epithelial cells did not require androgens, but a minimal concentration of 5.10(-7) M hydrocortisone. In that system, epithelial cells expressed cytokeratin but failed to produce the tissue specific mouse vas deferens protein (MVDP) in response to androgens. Various culture procedures and medium compositions were assayed for induction of MVDP expression. Culture onto microporous membrane inserts, which allow polarization of cells, is absolutely required for androgenic induction of MVDP. Androgen action did not require the presence of hydrocortisone, insulin, triiodothyronine, pituitary extracts, epidermal growth factor and acetylcholine. A minimal supplemented medium was then defined in which the expression of MVDP by epithelial cells in response to androgens was dose dependent. It has also been shown that this response at each concentration of dihydrotestosterone was heterogeneous at individual cell level. Highly reproducible results were obtained from epithelial cell cultures between 8th to 16th passages, showing that subcultured cells have maintained their ability to differentiate and express specialized functions.

Acetylcholine↗
PubMed1991

Androgen dependence during development of the mouse vas deferens protein mRNA.

The mRNA encoding a major protein of the mouse vas deferens (MVDP) was first detected in 10-day-old males and its concentration increased sharply between 10 and 20 days, reaching adult levels at 40 days. This increase was not associated with an increase in tissular androgen concentrations. In 30-day-old mice castrated at birth or treated with cyproterone acetate over 29 days, MVDP mRNA levels were not abolished and were similar to those measured in 10- and 20-day-old controls. These results suggest that the neonatal expression of MVDP gene is independent of androgens. In addition, precocious accumulation of MVDP mRNA could be induced by injection of excess amounts of androgens in 20- but not in 10-day-old animals. The prepubertal increase in MVDP mRNA levels is androgen-dependent but other factors may be necessary for MVDP expression.

Aldehyde Reductase↗
PubMed1991

Plasma epinephrine in chronically adrenodemedullated rats: lack of response to acute or chronic exercise.

Even if it is well established that epinephrine is a hormone originating from the adrenal medullae, the reappearance of circulating epinephrine has been reported in rats a few days after adrenodemedullation. To verify if the extra-adrenal tissue responsible for this epinephrine production can be stimulated, sham-operated or adrenodemedullated rats, either trained or kept sedentary, were submitted to an acute exercise stimulation test. Blood sampling was done before and after the test in precannulated rats for the determination of plasma epinephrine, norepinephrine, and corticosterone levels. Basal epinephrine levels were significantly reduced in trained and sedentary adrenodemedullated rats compared with their sham-operated counterparts. In response to exercise, there was no significant rise in epinephrine levels in both groups of adrenodemedullated rats. The norepinephrine levels in the basal state and in response to exercise were not altered by adrenodemedullation nor by physical conditioning. Basal corticosterone levels were similar between adrenodemedullated and sham-operated animals, either trained or kept sedentary. In response to exercise, corticosterone levels increased significantly in each group of rats but to a lesser extent in both groups of adrenodemedullated animals. These data indicate that the extra-adrenal epinephrine secretion that develops in the absence of adrenal medullae is not influenced by acute exercise nor by physical training.

Adrenal Medulla↗
PubMed1991

Lack of expression of the mRNA encoding a major protein of the mouse vas deferens after neonatal exposure to oestrogens.

We have previously characterized an androgen-inducible secretory protein from the mouse vas deferens (MVDP), and a cDNA to its mRNA has been obtained. This report describes altered MVDP gene expression after neonatal exposure to oestrogens. As shown by immunohistochemistry and Western blot analysis, MVDP was missing in the vas deferens from adult mice neonatally exposed to oestrogens. Northern blot analysis showed that the expression of MVDP mRNA was also suppressed. Exogenous testosterone was unable to stimulate MVDP production (either message or protein) in neonatally oestrogenized males. The results suggest that the alterations in gene expression in the oestrogen-exposed vas deferens reflect changes in the programme of differentiation of the organ itself.

Aldehyde Reductase↗
PubMed1991

[Characterization of cDNA and of the gene corresponding to androgen-dependent protein of the vas deferens in mice].

A 34.5 kDa abundant protein named MVDP (Mouse Vas Deferens Protein) is produced and secreted by vas deferens epithelial cells from adult mice. Steady-state levels of MVDP and its 1.4 kb mRNA are markedly decreased 30 days after castration. Testosterone treatment for 2 weeks is necessary to completely reverse the effect of castration. A cDNA encoding MVDP has been cloned and entirely sequenced. A protein of 316 amino acids encoded by an open reading frame of 948 nucleotides shows 82% homology with a human placental aldose reductase. A gene corresponding to MVDP cDNA has been recently isolated ans characterized. The gene extends over approximately 11 kb and consists of 10 exons. Its structure is very similar to that of the human aldose reductase gene. The promotor region of MVDP gene contains an androgen responsive element consensus located 97 nucleotides upstream the transcription initiation site.

Aldehyde Reductase↗
PubMed1991

Developmental and hormonal regulation of specific proteins in mouse vas deferens and seminal vesicle.

This paper is concerned with hormonal regulation of the developmental pattern of major proteins of the mouse vas deferens (mouse vas deferens protein: MVDP, 34.5 kD) and seminal vesicle (15.5, 120 and 140 kD) whose expression is regulated by testosterone at adulthood. The ontogeny of these proteins, studied by SDS-polyacrylamide gel electrophoresis, appeared to be uncoordinated. MVDP was not accumulated until animals were 20 days old and its concentration increased sharply from 20 to 30 days of age. In seminal vesicle, the 15.5 kD protein did not accumulate before day 30 whereas 120 and 140 kD proteins appeared and accumulated between 30 and 40 days. In 30-day-old mice castrated at birth or treated with cyproterone acetate over 29 days, MVDP levels were not abolished and were similar to those measured in 20-day-old males. Testosterone administration, from 1 to 10 days of age, did not induce precocious expression of MVDP. These results suggest that the neonatal expression of MVDP is independent of androgens. In seminal vesicle, the first expression of the 3 proteins studied was dependent upon testicular androgens as shown by neonatal castration and injection experiments. The marked increase in the levels of the 4 proteins studied, during sexual maturation, was not associated with quantitative or qualitative changes in tissular androgen concentrations, suggesting that other factors may be necessary for protein expression. Whereas thyroxine may induce a precocious accumulation of MVDP, prolactin had no stimulatory effect on the accumulation of proteins from vas deferens and seminal vesicle. The results suggest that during sexual maturation gene activation by androgens was progressive.

Aldehyde Reductase↗
PubMed1990

Androgen regulation of the mRNA encoding a major protein of the mouse vas deferens.

A cDNA encoding the major mouse vas deferens protein (MVDP) has been cloned and characterized. Using in situ hybridization we have identified the epithelial cells of the vas deferens as the site of synthesis of MVDP mRNA. Northern blot analysis suggests that a high level of an mRNA corresponding to the MVDP gene is present in the mouse vas deferens whereas the amount of MVDP mRNA in vas deferens of other species studied, or in other mouse tissues, even if present, is undetectable. Steady-state levels of MVDP mRNA are decreased by approximately 42% 3 days after castration but a significant hybridization signal is still observed even 50 days after castration. Testosterone treatment for 2 weeks is necessary to completely reverse the effect of castration. In vitro transcription assays on isolated nuclei showed that the hormonal induction of the MVDP gene is achieved mainly at transcriptional level.

Aldehyde Reductase↗
PubMed1990

Neonatal exposure to oestrogens alters the protein profiles and gene expression in the genital tract of adult male mice.

After neonatal administration of supraphysiological doses of oestradiol, the concentration of tissue proteins, in adult mice, was significantly reduced by 39, 45 and 56% in epididymis, vas deferens and seminal vesicle respectively. The protein profiles showed persistent alterations. In epididymis, 4 protein bands were differentially increased (14.4, 43 and 67 kDa) or reduced (24 kDa) in oestrogenized males. In vas deferens, 4 proteins were increased (14.4, 49,67 and 76 kDa) and one (34 kDa) virtually absent. In seminal vesicle, about 20 proteins of varying molecular weights (12-140 kDa) were differentially increased or decreased. Testosterone substitution, at adulthood, was unable to reverse these effects. Treatments with oestradiol during adult life induced persistent alterations in the protein profiles of the 3 organs but, in contrast to neonatal treatment, these alterations could be reversed by androgen therapy. A cDNA library has been constructed with RNA prepared from adult seminal vesicle and screened by differential hybridization. Neonatal oestrogenization strongly reduced the abundance of some mRNA species. Eleven recombinants containing putative oestrogen-sensitive sequences were isolated. Two of them, having an insert of about 500 base pairs, were used for dot-blot hybridization. Results showed that the two clones contained sequences which were differently regulated by androgens.

Aging↗
PubMed1990

[Backaches].

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Aged↗
PubMed1989

The effect of fatigue on the binding of glycolytic enzymes in the isolated gastrocnemius of Rana pipiens.

Fatigue of isolated gastrocnemius muscles from R. pipiens leads to a marked increase in the proportion of phosphofructokinase bound to the particulate fraction and a decrease in the binding of lactate dehydrogenase, pyruvate kinase, creatine phosphokinase and glyceraldehyde-3-phosphate dehydrogenase. Only the proportion of aldolase bound to the particulate fraction was unaffected by fatigue. This pattern was unchanged when fatigued muscles were extracted at pH 6.5 rather than 7.5. Thus, muscle fatigue leads to opposite changes in the binding of the glycolytic enzymes.

Animals↗