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Y Briand

Publications and source records attributed to Y Briand.

At least 19 recordsLinked to original sources
PubMed2002

Effect of endurance training and/or fish oil supplemented diet on cytoplasmic fatty acid binding protein in rat skeletal muscles and heart.

Endurance training and/or a fish oil supplemented diet affect cytoplasmic fatty acid binding protein (FABP(c)) content in rat skeletal muscles and heart. After 8 weeks of swimming, trained rats exhibited higher FABP(c) content in the extensor digitorum longus (EDL) and in the gastrocnemius than did control rats (30%). The FABP(c) increase was associated with an increase of citrate synthase activity (85% and 93%, respectively, in the two muscles), whereas lactate dehydrogenase activity decreased significantly. In contrast, in the soleus and in the heart we did not observe any effect of exercise either on FABP(c) or on the metabolic profile. Therefore, increasing oxidative capacities of muscle by exercise resulted in a concomitant increase of the FABP(c) content. Giving a polyunsaturated fatty acid (omega-3) supplemented diet for eight weeks induced a large rise of the FABP(c) in EDL (300%), gastrocnemius (250%), soleus (50%) and heart (15%) without a concurrent accumulation of intramuscular triglycerides or modification of the citrate synthase activity, suggesting that polyunsaturated fatty acids may increase FABP(c) content by up-regulating fatty acid metabolism genes via peroxisome proliferator-activated receptor alpha activation. Endurance trained rats fed with an omega-3 diet had similar FABP(c) content in the gastrocnemius muscle when compared to sedentary omega-3 fed rats, whereas an additive effect of exercise and diet was observed in the EDL. The FABP(c) in the soleus and in the heart of rats fed with omega-3 supplements remained constant whether rats performed exercise or not. As a result, both exercise and omega-3-enriched diet influenced FABP(c) content in muscle. These two physiological treatments presumably acted on FABP(c) content by increasing fatty acid flux within the cell.

Animals↗
PubMed2000

Distribution of proteasomes and of the five proteolytic activities in rat tissues.

Five peptidase activities (ChT-L, T-L, PGPH, BrAAP, and SNAAP) of the proteasome, and its caseinolytic activity, were measured in crude extracts of 10 rat tissues under experimental conditions simulating those found in vivo, thereby eliminating the alterations observed with the purified enzyme. The total and individual peptidase activities varied considerably from one tissue to another, whereas the proteolytic activity measured with [(14)C]methylcasein varied no more than twofold. The tissue-specific variations in individual peptidase activities may reflect tissue-specific differences in proteasome subunit composition, or the presence of regulators. Immunological assay using an antibody directed against the iota (alpha1) subunit showed that there was no correlation between protein abundance and peptidase activity. The results also show that the different peptidase activities are not representative of proteasome distribution in the different tissues.

Animals↗
PubMed1999

Changes in 20S proteasome activity during ageing of the LOU rat.

Muscular functions decline and muscle mass decreases during ageing. In the rat, there is a 27% decrease in muscle protein between 18 and 34 months of age. We examined age-related changes in the proteasome-dependent proteolytic pathway in rats at 4, 18, 24, 29 and 34 months of age. The three best characterised activities of the proteasome (chymotrypsin-like, trypsin-like and peptidylglutamyl peptide hydrolase) increased to 29 months and then decreased in the senescent animal. These variations in activity were accompanied by an identical change in the quantity of 20S proteasome measured by Western blot, whereas the S4 subunit of the 19S regulator and the quantity of ubiquitin-linked proteins remained constant. mRNA of subunits C3, C5, C9, and S4 increased in the senescent animal, but ubiquitin mRNA levels were unchanged. These findings suggest that the 20S proteasome may be partly responsible for the muscular atrophy observed during ageing in the rat.

Aging↗
PubMed1997

Involvement of proteasomal subunits zeta and iota in RNA degradation.

We have identified two distinct subunits of 20 S proteasomes that are associated with RNase activity. Proteasome subunits zeta and iota, eluted from two-dimensional Western blots, hydrolysed tobacco mosaic virus RNA, whereas none of the other subunits degraded this substrate under the same conditions. Additionally, proteasomes were dissociated by 6 M urea, and subunit zeta, containing the highest RNase activity, was isolated by anion-exchange chromatography and gel filtration. Purified subunit zeta migrated as a single spot on two-dimensional PAGE with a molecular mass of approx. 28 kDa. Addition of anti-(subunit zeta) antibodies led to the co-precipitation of this proteasome subunit and nuclease activity. This is the first evidence that proteasomal alpha-type subunits are associated with an enzymic activity, and our results provide further evidence that proteasomes may be involved in cellular RNA metabolism.

Animals↗
PubMed1997

Proteasome (prosome) associated endonuclease activity.

The 20S proteasome (prosome) is a highly organized multiprotein complex with approximate molecular weight of about 700 kDa. Whilst the role of the proteasome in the processing and turnover of cellular proteins is becoming clearer, its relationship with RNA remains still obscure. Here we focus on the nature and function of proteasome associated endonuclease activity. Thus the involvement of a proteasome alpha-type subunit in RNA-degradation, the catalytic requirements, the interaction of proteasomes with their RNA-substrate and the identification of a well defined cleavage site in the 3'UTR of short-lived cellular mRNAs will be described in detail. All data indicate that proteasomes associated endonuclease activity could be involved in post-transcriptional gene control at the level of translation.

Animals↗
PubMed1995

Identification and initial characterization of a specific proteasome (prosome) associated RNase activity.

We have identified and characterized a specific nuclease activity to be tightly associated with proteasomes. Using tobacco mosaic virus RNA (TMV-RNA) as substrate to analyze and quantify the cleavage reaction, we supply several lines of evidence that this nuclease activity is an integral part of proteasomes. Thus, RNase activity was coincident with the elution profiles of proteasomes at each stage of purification. Proteasomal nuclease activity was resistant to strong dissociation conditions using 480 mM KCl, 0.5% sodium lauroylsarcosinate, and 6 M urea. This nuclease activity remained associated with an urea-resistant subcomplex of the proteasome comprising a specific set of proteins. Finally the digestion of TMV-RNA led to a well defined pattern of RNA fragments while 5 S ribosomal RNA and globin mRNA were not degraded. These results provide further evidence that proteasomes are able to discriminate between different RNAs, and the possible involvement of proteasomes in translation control is discussed.

Animals↗
PubMed1995

Relationships between proteasomes and RNA.

The 20S proteasome (prosome) is a highly organized multi-protein complex with approximate molecular weight of about 700 kDa. Whilst the role of the proteasome in the processing and turnover of cellular proteins is becoming clearer, its relationship with RNA remains obscure. Over the last decade the possibility of association of proteasomes with specific RNAs or mRNPs have been particularly controversial. Proteasomes were reported to inhibit translation of viral mRNAs and to be tightly associated with RNase activity. It is possible that proteasomes are also involved in cellular RNA breakdown and RNA processing like prokaryotic RNase E.

Animals↗
PubMed1995

Proteolytic activity of proteasome on myofibrillar structures.

The physiologic function of proteasome remains unclear. Evidence suggests a role in degradation of ubiquitin-protein conjugates, MHC antigen presentation, and some specificity of substrate within certain cell types. To explore further the properties of proteasome we have examined its effect on a well defined structure, the myofibril. We find that despite its large size (20S) proteasome is able to degrade myofibrils and intact, permeabilized muscle fibrils. The proteins degraded showed some specificity because actin, myosin and desmin were degraded faster than alpha-actinin, troponin T and tropomyosin. Changes in ultrastructure were slow and included a general loss of structure with Z and I bands effected before the M band and costameres.

Animals↗
PubMed1994

Proteasomes (prosomes) inhibit the translation of tobacco mosaic virus RNA by preventing the formation of initiation complexes.

Proteasomes (prosomes) are large multiprotein complexes. They are involved in protein degradation of ubiquitin-conjugated proteins and in the generation of MHC class I peptides. We gave further evidence that they interfere with in vitro protein synthesis. Proteasomes inhibit the translation of Tobacco mosaic virus RNA. Analysis of cell-free systems by sucrose gradient centrifugation revealed that they prevent the formation of 80S initiation complexes but not the early phase of initiation.

Animals↗
PubMed1994

Expression of lactic dehydrogenase isoenzymes in rabbit muscle during development.

1. Rabbit cDNA probes for H and M lactic dehydrogenase subunits were used to monitor mRNA levels in different muscle types during growth. 2. At the same time, lactic dehydrogenase activity and relative quantities of H and M protein subunits were measured. 3. The main results are that mRNA abundance depends on muscle type and age, and mRNA abundance is not correlated with enzymatic activity.

Age Factors↗
PubMed1993

Metabolic and contractile differentiation of rabbit muscles during growth.

1. A study was carried out of post-natal evolution of the oxidative, glycolytic and contractile capacities in various types of rabbit muscle. 2. At birth, muscles are non-differentiated and present very limited metabolic and contractile activity, metabolism is mainly oxidative in all muscles. 3. Although muscular discrimination is manifest from the sixth week after birth, the glycolytic metabolism reaches its maximum capacity only after six to eight weeks. 4. Subsequently, oxidative metabolic capacity steadily decreases until adulthood.

Animals↗
PubMed1993

Glycosylation and deglycosylation of proteasomes (prosomes) from calf-liver cells: high abundance of neuraminic acid.

Proteasomes (prosomes) of calf-liver cells were probed with three different biotinylated lectins: Limulus polyphemus agglutinin (LPA), specific for neuraminic acid; Solanum tuberosum agglutinin (STA), specific for GlcNac; and concanavalin A (Con A), specific for Man/Glc. While only one proteasomal protein reacted with STA, most of the proteasomal proteins reacted with LPA and several with Con A. Deglycosylation with N-glycosidase F showed that the detected glycan residues were asparagine-linked. Finally we demonstrate an alternative method for the isolation of proteasomes based on the affinity of certain proteasomal proteins to Con A.

Animals↗
PubMed1991

Muscle differentiation in the bovine fetus: a histological and histochemical approach.

The chronology of muscle fiber differentiation was analysed in 37 fetal calves of 69 to 266 days of age. Semitendinosus muscle weight was measured throughout the experimental period and biochemical, histological and histochemical investigations were made to determine respectively the protein and DNA content of the muscle, the size and the number of the fibers and their ATPase and SDH activity. The relative growth of all the quantitative characteristics (muscle weight, protein and DNA content) was much greater in the early stages of gestation than in the new-born animal. In the younger fetuses DNA relative growth was faster than protein relative growth, whereas at the end of gestation the reverse progression was observed. Before 90 days, the muscle tissue was composed of myotube-like cells without any clear organization. The organization of muscle tissue into clear bundles occurred around 120 days of age, and about 30 days later the large myotubes transformed into myofibers. The myotubes reacted positively for acid-ATPase activity, whereas the large population of smaller cells which developed in parallel did not. The number of muscle cells increased up to 240 days of age, as did the percentage of fibers positive for acid-ATPase activity. Finally, oxidative differentiation occurred around 260 days of age, with the appearance of a population of cells characterized by increased SDH activity. A comparison of these results with previous findings suggests that the muscular tissue differentiates through similar stages in various species, but over different lengths of time. The percentage of mature weight might provide a better inter-species time scale than chronological age.

Adenosine Triphosphatases↗
PubMed1989

Characterization of rabbit lactate dehydrogenase-M and lactate dehydrogenase-H cDNAs. Control of lactate dehydrogenase expression in rabbit muscle.

Two cDNA clones were isolated, one corresponding to the mRNA coding for lactate dehydrogenase-M (LDH-M), the other to the mRNA coding for lactate dehydrogenase-H (LDH-H). The cDNA inserts consist of the entire open reading frame for LDH-M and a partial sequence, from amino acid 117 to 332, for LDH-H. Using these two clones as probes we demonstrate that: (a) the abundance of mRNA is muscle-type dependent; (b) the ratio M/H subunit for protein and mRNA is well related in the muscles studied; and (c) the M + H mRNA level is not relative to the total LDH activity.

Amino Acid Sequence↗
PubMed1986

Metabolic and contractile properties of rabbit muscles: a statistical approach.

The metabolic and contractile properties of rabbit muscles representative of the three main muscle types have been studied. A statistical analysis of the results indicates the more discriminant variables for this characterization and shows in particular that the myosin light chains represent a very significant discriminant factor of the muscular type. Results also show that lactate dehydrogenase activity is strongly correlated with the percentage of lactate dehydrogenase M-subunit and with myosin light chains.

Adenosine Triphosphatases↗