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Biomedical subjects

D Guillaume

Publications and source records attributed to D Guillaume.

At least 37 records · Page 2Linked to original sources

Genetic variability in melatonin concentrations in ewes originates in its synthesis, not in its catabolism.

We investigated whether the genetic difference in plasma melatonin concentration in ewes was due to differences in the synthesis pathway from the pineal gland or in the catabolism of the hormone. Two groups of ewes [9 low (L) and 10 high (H)] were selected according to the breeding value of their mean nighttime plasma melatonin concentrations estimated at winter and summer solstices. In response to an identical dose of melatonin administered intravenously at 9:00 AM, no differences between groups were observed for any of the kinetic parameters: clearance rate, steady-state volume of distribution, terminal half-lives, and mean residence times. In the second experiment, two series of frequent blood samples were performed, one in the middle of the dark phase with samples taken every 5 min, and the other over 24 h with hourly samples. Highly significant differences between groups in nocturnal melatonin production rate were observed (L: 25.7 +/- 2.8 vs. H: 63.1 +/- 8.9 microg . kg-1 . h-1, P < 0.01). Thus the genetic differences in plasma melatonin concentrations in ewes originate in the synthesis pathway of the melatonin from the pineal gland rather than from differences in the catabolism of the hormone.

Animals↗

Herniaria saponin B. a novel triterpenoid saponin from Herniaria fontanesii.

The aerial parts of Herniaria fontanesii have yielded a new saponin named herniaria saponin B. Its structure was characterized by means of mass spectrometry. NMR techniques, and chemical analysis gave 28-O-[alpha-L-rhamnopyranosyl-(1-->2)-[(alpha-L-rhamnopyranosyl-(1--> 3)]-beta-D-xylopyranosyl (1-->2)-beta-D-fucopyranosyl) ester of 3-O-[beta-D-glucopyranosyl uronic-(1-->4)-alpha-L-rhamnopyranosyl]-2 beta. 3 beta-16 alpha-trihydroxy-olean-12-ene-23, 24-dioic acid.

Carbohydrate Conformation↗

Matesaponin 5, a highly polar saponin from Ilex paraguariensis.

The structure of matesaponin 5, a novel saponin isolated from the leaves of the Ilex paraguariensis, was established as ursolic acid-3-0-{beta-D-glucopyranosyl-(1->3)-[alpha-L-rhamnopyranosyl-(1->2)]-alpha-L- arabino pyranosyl}-(28->1)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1 ->6)-beta-D-glucopyranosyl] ester.

Carbohydrate Conformation↗

Triterpenoid saponins from Herniaria fontanesii.

Two new saponins have been isolated from the aerial parts of Herniaria fontanesii. Their structures were established as 28-O-[alpha-L-rhamnopyranosyl-(1-->2-[(alpha-L- rhamnopyranosyl)-(1-->3)-]-(beta-D-4-acetoxyfucopyranosyl] ester of 3-O-[alpha-L-rhamnopyranosyl-(1-->2)-beta-D-glucopyranosyl uronic]-2 beta-3 beta-16-alpha-trihydroxy-olean-12-ene-23, 28-dioic acid and 28-omicron-[alpha-L-rhamnopyranosyl-(1-->2-[alpha-L-rhamnopyranosyl (1-->3)]-(beta-D-fucopyranosyl] ester of 3-omicron-[alpha-L-rhamnopyranosyl-(1-->2)-beta-D-glucopyranosyl uronic]-2 beta-3 beta-16-alpha-trihydroxy-olean-12-ene-23, 28 dioic acid.

Carbohydrate Sequence↗

Structure elucidation of three triterpene glycosides from the trunk of Argania spinosa.

The structures of three novel saponins from Argania spinosa, named arganines G, H, and J, have been elucidated by MS and NMR techniques as 3-O-beta-D-apiofuranosyl- (1-->4)-beta-D-glucopyranosyl-28-O-beta-D-glucopyranosylbayogenin (1), 3-O-beta-D-apiofuranosyl-(1-->4)-beta-D-glucopyranosyl-28-O-alpha- L- arabinopyranosylbayogenin (2), and 3-O-beta-D-apiofuranosyl-(1-->4)-beta-D-glucopyranosyl-28-O- [beta-D-apiofuranosyl-(1-->3)-beta-D-xylopyranosyl-(1-->4)-alpha-L - rhamnopyranosyl-(1-->2)-alpha-L-arabinopyranosyl]bayogenin (3), respectively.

Carbohydrate Sequence↗

Apolipoprotein E and low-density lipoprotein binding and internalization in primary cultures of rat astrocytes: isoform-specific alterations.

Apolipoprotein (apo) E is likely involved in redistributing cholesterol and phospholipids during compensatory synaptogenesis in the injured CNS. Three common isoforms of apoE exist in human (E2, E3, and E4). The apoE4 allele frequency is markedly increased in both late-onset sporadic and familial Alzheimer's disease (AD). ApoE concentration in the brain of AD subjects follows a gradient: ApoE levels decrease as a function of E2 > E3 >> E4. It has been proposed that the poor reinnervation capacity reported in AD may be caused by impairment of the apoE/low-density lipoprotein (LDL) receptor activity. To understand further the role of this particular axis in lipid homeostasis in the CNS, we have characterized binding, internalization, and degradation of human 125I-LDL to primary cultures of rat astrocytes. Specific binding was saturable, with a KD of 1.8 nM and a Bmax of 0.14 pmol/mg of proteins. Excess unlabeled human LDL or very LDL (VLDL) displaced 70% of total binding. Studies at 37 degrees C confirmed that astrocytes bind, internalize, and degrade 125I-LDL by a specific, saturable mechanism. Reconstituted apoE (E2, E3, and E4)-liposomes were labeled with 125I and incubated with primary cultures of rat astrocytes and hippocampal neurons to examine specific binding. Human LDL and VLDL displaced binding and internalization of all apoE isoforms similarly in both astrocytes and neurons. 125I-ApoE2 binding was significantly lower than that of the other 125I-apoE isoforms in both cell types. 125I-ApoE4 binding was similar to that of 125I-apoE3 in both astrocytes and neurons. On the other hand, 125I-apoE3 binding was significantly higher in neurons than in astrocytes. These isoform-specific alterations in apoE-lipoprotein pathway could explain some of the differences reported in the pathophysiology of AD subjects carrying different apoE alleles.

Animals↗

Triterpenoid saponins from the root of Sideroxylon foetidissimum.

Two novel triterpenoid saponins named sideroxyloside B and sideroxyloside C were isolated from the root of Sideroxylon foetidissimum. On the basis of spectroscopic and chemical methods, their structures were established as 3-O-beta-D-glucopyranosyl-28-O([beta-D-apiofuranosyl-(1-->3)-beta- D- xylopyranosyl-(1-->4)-alpha-L-rhamnopyranosyl-(1-->4)] [beta-D-apiofuranosyl(1-->3)]-alpha-L-rhamnopyranosyl-(1-->2)-alph a-L- arabinopyranosyl) protobassic acid and 28-O([beta-D-xylopyranosyl-(1-->4)- alpha-L-rhamnopyranosyl-(1-->4)] [beta-D-apiofuranosyl-(1-->3)]-alpha-L- rhamnopyranosyl-(1-->2)-alpha-L-arabinopyranosyl) protobassic acid, respectively.

Carbohydrate Conformation↗

Triterpenoid saponins from Ilex paraguariensis.

The leaves of Ilex paraguariensis have yielded three new saponins named matesaponins 2, 3, and 4 [1-3], which have been characterized by chemical and nmr methods as ursolic acid 3-O-[beta-D-glucopyranosyl-(1-->3)-[alpha-L-rhamnopyranosyl- (1-->2)]]-alpha-L-arabinopyranosyl]-(28-->1)-beta-D-glucopyranosyl ester, ursolic acid 3-O-[beta-D-glucopyranosyl-(1-->3)-alpha-L-arabinopyranosyl]-(28-- >1)- [beta-D-glucopyranosyl-(1-->6)-beta-D-glucopyranosyl]ester, and ursolic acid 3-O-[beta-D-glucopyranosyl-(1-->3)-[alpha-L- rhamnopyranosyl-(1-->2)]]-alpha-L-arabinopyranosyl]-(28-->1)-[beta -D- glucopyranosyl-(1-->6)-beta-D-glucopyranosyl]ester, respectively.

Acetylation↗

Triterpenoid saponins from Mimosa pigra.

Two novel triterpene glycosides have been isolated from Mimosa pigra. The aglycone of these two compounds was identified as machaerinic acid by 1H- and 13C-nmr spectroscopy and by comparison with an authentic sample. This aglycone is substituted at position C-3 by an identical oligosaccharide chain in these glycosides, and at position C-21 by either a Z/E-methoxycinnamic [1] unit or an E-cinnamic acid [2] unit.

Carbohydrate Sequence↗

Kinetic studies and production rate of melatonin in pony mares.

The aims of the present study were to determine basic kinetic parameters and the nycthemeral production rate of melatonin in the horse. Seven pony mares were used for the kinetic studies. Five other pony mares were used under long and short days for the production rate studies. Melatonin was administered by intravenous, oral, and intragastric routes at different dose levels. The plasma melatonin clearance was 1.02 +/- 0.31 l.kg-1.h-1, and the volume of distribution was 0.89 +/- 0.53 l/kg for the 0.4 microgram/kg melatonin dose. The systemic availability after oral and intragastric administration was consistently low (< or = 10%). The hourly melatonin production rates during short (36 +/- 33.6 ng.kg-1.h-1) and long nights (42 +/- 24.0 ng.kg-1.h-1) were not significantly different. It is concluded that the oral dose of exogenous melatonin required to control reproductive pattern in horses would need to be 10 times higher than the nocturnal melatonin production (0.5 microgram/kg) to obtain a physiological plasma melatonin concentration.

Analysis of Variance↗

Triterpenoid saponins from the root of Sideroxylon cubense.

Two triterpenoid saponins were isolated from the root of Sideroxylon cubense and their structures were established as 3-O-beta-D-glucopyranosyl-28-O-[alpha-L-rhamnopyranosyl(1-->3)- beta-D-xylopyranosyl(1-->4)-alpha-L-rhamnopyranosyl(1-->2) beta-D-xylopyranosyl] protobassic acid and 3-O-beta-D-glucopyranosyl protobassic acid. The first, designed as sideroxyloside A, is a new natural product.

Carbohydrate Sequence↗

Mabiosides C-E: triterpenoid saponins from the bark of Colubrina elliptica.

Three novel saponins, mabiosides C-E, were isolated from the bark of Colubrina elliptica together with the known mabioside B and [alpha-L-rhamnopyranosyl-(1-->2)-beta-D-glucopyranosyl-(1-->3)-alpha-L- arabinopyranosyl]-(1-->3)-jujubogenin. All the structures were established by spectroscopic methods.

Carbohydrate Sequence↗

Characteristics of putrescine uptake and subsequent GABA formation in primary cultured astrocytes from normal C57BL/6J and epileptic DBA/2J mouse brain cortices.

Brain maturation and GABA metabolism are known to play a key role in epileptogenesis. The metabolism of the polyamines (putrescine, spermidine and spermine) is closely linked to the process of brain maturation. Putrescine has been shown to be catabolized to GABA in brain tissue and astrocytes. In order to better understand the importance of glial putrescine transport and metabolism, a model of age-dependent epilepsy was used to study the kinetic properties of [14C]putrescine uptake into cultured astrocytes from normal C57/BL and audiogenic DBA/2 newborn mice, and the subsequent GABA formation. (1) Putrescine uptake exhibited non-Michaelian allosteric kinetics with positive co-operativity (Hill factor = 2), suggesting a physiological importance of putrescine uptake by astrocytes. (2) The Vmax of putrescine uptake was significantly higher in C57/BL astrocytes than in DBA/2J, but the uptake affinity for putrescine was higher in DBA/2J than in C57/BL. (3) Higher K+ concentrations (18 mM) had little effect on putrescine uptake in either strain. (4) Ten-micromolar N-acetylputrescine, the first putrescine metabolite, stimulated putrescine uptake into astrocytes of both strains, but to a different degree: +46% in C57/BL and + 102% in DBA/2J. (5) The specific radioactivity of the GABA formed from labelled putrescine was four times higher in astrocytes from DBA/2J than from C57/BL mice. (6) The molar ratio of glutamate/GABA in the cerebral cortex of the DBA/2J mice was significantly higher during the period of audiogenic seizure susceptibility than in age-matched C57/BL mice. Our results show characteristics of putrescine uptake into astrocytes; we demonstrated distinct kinetic properties between normal and epileptic strains of mice.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗

Contribution of Na+,K(+)-ATPase to focal epilepsy: a brief review.

The authors review some of their experimental data on the contribution of Na(+)- and K(+)-dependent adenosine triphosphatase (Na+,K(+)-ATPase) to focal epilepsy. It has been previously demonstrated that high extracellular K+ concentration increases glial Na+,K(+)-ATPase specific activities in normal conditions while this was not observed in neuronal preparations. At this time, it was hypothesized that this molecular mechanism could play a role in removing K+ released in the extracellular space during neuronal firing. These results have therefore been investigated in acute and chronic epileptogenic lesions of cats with freeze lesion. It was demonstrated that within the primary (F) and the secondary or 'mirror' (M) focus the K+ activation of the glial Na+,K(+)-ATPase dramatically decreased compared to both control animals (C) and the perifocal (PF) non epileptogenic area. Similar results were observed in man when using specimens of anterolateral temporal neocortex obtained during temporal lobectomies in patients with intractable temporal lobe epilepsy, compared with postmortem human specimens or control brain tissues. The modifications of the level of phosphorylation of partially purified Na+,K(+)-ATPase was also investigated in the epileptic cortex in these two experimental conditions. The catalytic subunits were resolved by sodium dodecylsulfate (SDS) gel electrophoresis and their phosphorylation levels were measured in the presence of various concentrations of K+ ions which dephosphorylate the catalytic subunit. K(+)-induced dephosphorylation was decreased in primary and secondary foci of acutely lesioned cats. Those alterations, due to a decreased affinity for K+, were limited to the alpha (-) subunit. In cats with chronic lesions, the dephosphorylating step of the Na+,K+-ATPase catalytic subunit recovered to normal affinity for K+.(ABSTRACT TRUNCATED AT 250 WORDS)

Epilepsies, Partial↗

Phosphorylation of brain (Na+,K+)-ATPase alpha catalytic subunits in normal and epileptic cerebral cortex: I. The audiogenic mice and the cat with a freeze lesion.

Partially purified (Na+,K+)-ATPase (E.C. 3.6.1.3.) was investigated in the epileptic cortex of audiogenic DBA/2 mice and in the primary and secondary foci of cats with acute or chronic freeze lesions. No differences in specific activities measured at 3 mM K+ were observed between epileptic and control cortex, except an increase of enzymic activities in the primary focus of acutely lesioned cats. The (Na+,K+)-ATPase catalytic subunits were resolved by SDS-gel electrophoresis and their phosphorylation levels were measured in presence of K+ ions and phenytoin. K+ was more effective in inducing maximal dephosphorylation of (Na+,K+)-ATPase in C57/BL, with identical affinity in the two strains. Phenytoin decreased the net phosphorylation level of (Na+,K+)-ATPase by about 50% in C57/BL mice, but only by 20% in DBA/2 mice. Both K+ and phenytoin dephosphorylating influences were decreased in primary and secondary foci of acutely lesioned cats. Those changes were limited to the alpha(-) subunit. In chronic cats, the dephosphorylating step of the (Na+,K+)-ATPase catalytic subunit recovered a normal affinity to K+, but its sensitivity to phenytoin remained decreased. Those differences in K+ and phenytoin influences on brain (Na+,K+)-ATPases between control and epileptic cortex might be responsible for the ictal transformation and seizure spread. In cats, the alteration of the alpha(-) isoform could mainly affect the glial cells.

Acoustic Stimulation↗