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Biomedical subjects

C Francois

Publications and source records attributed to C Francois.

At least 19 recordsLinked to original sources
PubMed1997

[Coronary embolism and myocardial infarction with heat rupture during infectious endocarditis].

We report a case of transmural myocardial infarction due to coronary embolism complicating infective endocarditis in a 41 year old woman. The infarction, clinically silent, was followed by rupture of left ventricular free wall, leading to hemopericardium and cardiac tamponade. The case is an uncommon complication of infective endocarditis, at the same time an uncommon cause of myocardial infarction.

Adult↗
PubMed1996

Stability study of nanoparticles of poly(epsilon-caprolactone), poly(D,L-lactide) and poly(D,L-lactide-co-glycolide).

The objective was to evaluate the stability of nanoparticles prepared with poly(epsilon-caprolactone), poly(D,L-lactide) and poly(D,L-lactide-co-glycolide) polymers and stored at different temperatures and in different media. The stability parameters studied were molecular weight and crystallinity of the polymer, nanoparticle size and pH. The results show that the stability of polymeric nanoparticles depends on (i) the type of polymers with the following increasing order of polymer stability: PLA25GA50 < PLA37.5GA25 < PLA50 = PCL, (ii) the storage temperature: PCL and PLA50 nanoparticles can be kept at 4 degrees C and RT during one year, while PLA37.5GA25 and PLA25GA50 nanoparticles have to be stored at 4 degrees C, and (iii) the storage conditions: buffering or freeze-drying nanoparticles improves stability.

Biopolymers↗
PubMed1994

Heterodimerization of the IL-2 receptor beta- and gamma-chain cytoplasmic domains is required for signalling.

The interaction of interleukin-2 (IL-2) and IL-2 receptors critically regulates the T-cell immune response following antigen activation. IL-2 can signal through high or intermediate affinity receptors which contain IL-2R alpha (refs 3, 4) +beta (refs 5-8) +gamma (ref. 9) or beta+gamma chains, respectively. IL-2R gamma is a common gamma chain, gamma c, also shared by the IL-7 (ref. 10) and IL-4 (refs 11, 12) receptors, which when mutated results in X-linked severe combined immunodeficiency. Using chimaeric receptor constructs together with monoclonal or bispecific antibodies we demonstrate here that IL-2 signalling requires ligand-induced extracellular-domain-mediated heterodimerization of the beta- and gamma c-chain cytoplasmic domains. Anti-IL-2R alpha monoclonal antibodies trigger proliferation of cells transfected with chimaeric constructs in which the extracellular domains of IL-2R beta and gamma c are replaced by that of IL-2R alpha. Other experiments using chimaeric constructs indicated that IL-2 binds monomerically and monovalently to IL-2R alpha and that the beta-transmembrane domain is not required for receptor chain interactions. Finally, we provide a method for mapping residues in the gamma c cytoplasmic domain even in cells that constitutively express gamma c.

Animals↗
PubMed1993

Construction of a bispecific antibody reacting with the alpha- and beta-chains of the human IL-2 receptor. High affinity cross-linking and high anti-proliferative efficiency.

A bispecific antibody recognizing both the alpha- and beta-chains of the IL-2R was generated by sulfhydryl-directed chemical reassociation of monovalent Fab' fragments prepared from the anti-alpha mAb 33B3.1 (rat IgG2a) and from the anti-beta mAb A41 (mouse IgG1). Whereas the 33B3.1/A41 bispecific mAb (bi-mAb) binds to isolated alpha- and beta-chains with low affinity (Kd = 4 nM), its binding to cells co-expressing the two chains shows both low and high affinity components. The high affinity-binding sites (Kd = 100 pM) most probably correspond to the cross-linking by the bi-mAb of alpha- and beta-chains, whereas the low affinity component corresponds to the excess of alpha-chains. High affinity binding of bi-mAb on activated T cells is observed at 37 degrees C and not at 4 degrees C, suggesting that i) the two chains are dissociated at 4 degrees C in the absence of ligand and ii) the mechanism of bi-mAb catalyzed cross-linking of these two chains is temperature dependent. In contrast to parental 33B3.1 and A41 IgG, which recognize single positive (alpha + and beta +, respectively) and double positive alpha +/beta + cells with similar affinities, the 33B3.1/A41 bi-mAb is specific for activated alpha +/beta + cells with respect to its high affinity binding. In contrast to A41, which does not affect IL-2-induced proliferation of 4AS cells or anti-CD3-activated PBL, and to 33B3.1, which do inhibit proliferation but only partially and at high doses, the bi-mAb showed full blocking efficiencies at low concentrations (IC50 of 300 to 400pM) corresponding to the formation of high affinity alpha/bi-mAb/beta complexes. These half-maximal effects were observed at 10-fold lower concentrations than when using a combination of equimolar concentrations of parental 33B3.1 and A41 IgG. Because of their specificity and high blocking efficiencies, anti-alpha/anti-beta bi-mAb may constitute a better alternative for IL-2R-directed immunosuppression.

Humans↗
PubMed1991

Could non steroidal anti-inflammatory drugs be used to potentiate L.M.W.H activity in thrombosis? (Part I).

Heparin fractions are antithrombotic drugs prescribed for preventive treatment but their efficacy must be optimized to permit curative use without side effects. The present study was performed on 144 rats receiving a low molecular weight heparin (L.M.W.H), Fraxiparine, and a non steroidal anti-inflammatory drug (Phenylbutazone), which were injected simultaneously or separately. Neither Phenylbutazone nor L.M.W.H at their lowest dose (1 mg/kg) reduced thrombus size. However, administered together, they produced a significant limitation of thrombus growth. Variation in anti Xa activity limitation was only observed with the highest dose of Fraxiparine alone or in combination with Phenylbutazone (1 mg/kg) corresponding to its antithrombotic effect.

Animals↗
PubMed1991

Topographic distribution of the neurons of the central complex (centre médian-parafascicular complex) and of other thalamic neurons projecting to the striatum in macaques.

The distribution of the neurons of the central complex (or "centre médian-parafascicular complex") and of other thalamic regions projecting to the striatum was studied using a cartographic technique based on ventricular landmarks. The brain of a macaque was used as a reference for the cytoarchitectonic study of the complex. Three parts were isolated: the pars parafascicularis (or medial part), the pars media (or middle part) and the pars paralateralis (or lateral part). Wheat germ agglutinin conjugated to horseradish peroxidase was stereotaxically injected into either the sensorimotor or the associative territory of the striatum (i.e. the striatal space occupied by the axonal endings coming from either the sensorimotor or the associative cortex) of four macaques. Neurons projecting to the sensorimotor territory of the striatum were found to be located within the pars media (middle part) of the central complex while neurons projecting to the associative territory of the striatum were located within the pars parafascicularis. In all experimental cases, labelled neurons were scarce or absent in the pars paralateralis (or lateral part). Outside the central complex, neurons projecting to the sensorimotor territory of the striatum were scattered within the lateral part of the lateral mass, in the intralaminar nuclei and in the posterior part of the internal lamina. Neurons projecting to the associative territory of the striatum were observed mainly in the paraventricular region, dorsal to the rostral part of the lateral mass, and in the dorsolateral part of the nucleus oralis medialis. Our three-dimensional analysis of the clusters of the central complex cells projecting to the two striatal territories justifies the partitioning of the central complex into three parts. The pars media (or middle part), which projects to the sensorimotor territory of the striatum, receives selectively pallidal afferent axons. It belongs to the Nauta-Mehler loop, a closed loop linking the central complex to the basal ganglia. The pars parafascicularis, which projects to the associative territory of the striatum, seems more related to oculomotor neuronal systems. The pars paralateralis (or lateral part) appears to have very little, if any, relation with the striatum.

Afferent Pathways↗
PubMed1990

Mouse mammary tumor virus (MMTV) infection in SWISS and RIII mice. Correlation between resistance to exogenous infection and anti-MMTV serum response.

Host-virus relationships were examined in mice from the two mouse mammary tumor virus (MMTV)-infected strains SWISS MB+ and RIII, which harbour the same MMTV variant, and from the derived sublines Swiss MB- and RIIIf, which were freed of milk-borne MMTV by foster-nursing. These two strains are not phylogenetically related, the SWISS strain bearing the endogenous Mtv-3 locus in its DNA. In RIII and SWISS MB+ mice, the incidence of early mammary tumors, which was of 96% and 8%, respectively, was correlated to the level of MMTV expression in milk. In the SWISS MB-line, a non-coordinate expression of the provirus associated with the Mtv-3 locus was observed in the mammary glands, the salivary glands and the spleen. This expression was not tumorigenic and was characterized by the presence of the p28 gag antigen and the absence of the gp52 env antigen, except, however, in mammary glands of elder mice where traces of gp52 were found. In the mammary glands of SWISS MB+ mice, the expression of the Mtv-3 locus was masked by large amounts of antigens resulting from exogenous virus expression. RIIIf mice were MMTV-negative. Viral antigens coexisted with anti-MMTV antibodies in the serum of infected and tumor-bearing mice, but not in the form of immune complexes as verified by a method that allowed to detect specific antigen-containing-soluble immune complexes. An anti-MMTV serum reactivity was also detected in SWISS MB- and RIIIf mice. However, the serum response was higher in the two SWISS lines than in the two RIII lines. Except in tumor-bearing mice, the anti-MMTV response was not significantly modified by the presence of exogenous virus and thus resulted essentially from exposure to endogenous MMTV expression. In experimental infection studies, RIII mice were more susceptible to MMTV infection than SWISS mice. The correlation between resistance to MMTV infection and serum response to endogenous MMTV expression, suggests that the non-tumorigenic expression of an endogenous provirus can protect at least partially, against exogenous MMTV infection.

Animals↗
PubMed1985

Natural infection of Swiss mice with mouse mammary tumor virus (MMTV): viral expression in milk and transmission of infection.

Quantitative determinations of gp52, the main envelope glycoprotein, and p28, the main core protein, of MMTV, have been performed in about 1000 individual samples of milk of breeding females from our colony of MMTV-infected Swiss mice, a line characterized by a moderate incidence of mammary tumors. A computer analysis of the results showed: 1-- an important individual variation, ranging from 0 to 120 micrograms per ml of milk for p28, and from 0 to 320 micrograms per ml of milk for gp52; 2-- a variation of the release of both antigens during a single lactation, with a maximum on the 7--8th day of nursing; 3-- an increase of the release of both antigens with parity up to the 6th lactation, followed by a marked decrease during later lactations; 4-- a higher degree of infection in the offspring of 2nd and 3rd litters. The possible dependence of viral expression and transmission of infection upon factors such as cyclic activity of the mammary gland and progressive immunization of mice against MMTV is analyzed. The status of our laboratory line of MMTV infected Swiss mice is discussed in comparison with high and low tumor incidence strains.

Animals↗
PubMed1985

A histological atlas of the macaque (Macaca mulatta) substantia nigra in ventricular coordinates.

An atlas of the macaque substantia nigra was established in ventricular coordinates. Having verified that nigral contours are stable in both Macaca mulatta and Macaca speciosa, the antero-posterior sequence of four subdivisions was described on eight vertico-transverse levels after a comparison between histological and histochemical data. The pars reticulata constitutes the anterior pole containing pale, small cell-bodies scattered among the numerous endings of the striato-pallido-nigral fibres. Anteriorly, the pars compacta forms the dorsal border of the substantia nigra, but more posteriorly, it leaves the dorsal border and develops ventral fringes. Its large cell-bodies, most often pigmented, rich in Nissl bodies and in acetylcholinesterase, are closely spaced among a few axonal fascicles. The pars lateralis contains a low density of cell-bodies and corresponds to the hilum of entrance of the striato-pallido-nigral fibres and gives rise to a nigro-tectal projection. The pars mixta, dorsally located, contains a low density of neurons varying considerably in size. It represents the hilum of exit of nigral axons which project to various targets.

Anatomy, Artistic↗
PubMed1984

Accessibility and cross-linking of native neurofilaments to chemical reagents.

Native neurofilaments were submitted to cross-linking reactions with bifunctional reagents (DMA, DMS and DSS) and to chemical reactions with sterically bulky reagents such as EEDQ and DTAF , as well as a glutaraldehyde-activated gel. The 160K and 70K neurofilament proteins reacted slightly more than the 210K neurofilament protein with DMS and DSS. The accessibility of the three neurofilaments to the other chemical reagents was identical. These results were unexpected since neurofilament antibodies seem to react preferentially with 210K protein which is at the periphery of the filament, whereas the 70K protein, which is the backbone of the filament, is probably buried inside the filament. In the same way, it has been shown that the side of the 210K proteins are probably able to cross link the neurofilaments with non covalent and covalent bridges. Using different cross link reagents, we did not observe a characteristic reactivity of the 210K protein towards the different chemicals. We conclude that the three neurofilament proteins are equally exposed to the different sterically bulky reagent and that part of the polypeptide chain of the 70K and the 160K proteins are located at the outside of the filament.

Animals↗
PubMed1984

Localization of nigrostriatal, nigrothalamic and nigrotectal neurons in ventricular coordinates in macaques.

The topography of the substantia nigra and its subdivisions was first analysed in macaques by using a topographic technique based on ventricular landmarks. This study shows the stability of the contours of the substantia nigra and its subdivisions in various species of macaques. The anteroposterior sequence of four subdivisions was standardized by defining eight verticotransverse levels, regularly interspaced and systemically used for each experimental case. Neurons of the substantia nigra sending axons to the striatum, thalamus and superior colliculus were identified by the technique of retrograde transport of horseradish peroxidase. The nigrostriatal labeled neurons were essentially located in the ipsilateral pars compacta but also scattered dorsally in the pars mixta and ventrally in the pars reticulata. In addition, the existence of a crossed nigrostriatal pathway was demonstrated in monkeys. Nigrothalamic labeled neurons were found in the whole pars reticulata at rostral levels and only in the medial part at more caudal levels. Comparatively, nigrotectal labeled neurons were also found in the whole pars reticulata at rostral levels, but caudally, they were confined to the lateral part of the pars reticulata and the pars lateralis. It thus appears that these three nigral components may overlap at some levels of the substantia nigra. This is discussed in relation to the existence of branched axons already documented. However, the present results underline the strong tendency of the nigrotectal neurons to be segregated from the nigrothalamic ones and to be laterally located in monkeys. In addition, two nigrotectal components have been identified on the basis of their topography and their somata size: one with large somata located in the pars lateralis, probably specific to primates, and the other with smaller somata located in the pars reticulata. These two components may indicate the existence of two different functional systems.

Animals↗
PubMed1983

Peroral infection of suckling mice with milk-borne mouse mammary tumour virus: uptake of the main viral antigens by the gut.

Persistence of mouse mammary tumour virus (MMTV) components in the digestive tract of suckling mice was investigated by immunoperoxidase staining of the main viral antigens and micro-immunoenzyme assays of gp52 and p28; these latter assays were also performed after ingestion of milk enriched in viral antigens using Cr2O3 as a marker for the alimentary bolus migration. When compared to the ingested antigens, the amounts of gp52 and p28 decreased during transit, p28 being more rapidly digested than gp52. The antigens were, however, destroyed to a much larger extent in the gut of the adult than in that of the newborn mouse. A fraction of the marker remained for a long time in the stomach; a prolonged retention was also observed with gp52 and especially with p28. Significant amounts of viral antigens were detected in the intestinal walls: both p28 and gp52 were found in the duodenum and small intestine. Moreover, the four viral antigens gp52, gp36, p28 and p8 were clearly observed in very large supranuclear vacuoles inside the epithelial cells of the distal part of the gut. Total particles can reach the intestine; the viral material could then be either destroyed or taken up in the epithelial cells by endocytosis, so that the intestinal epithelium might serve as a portal of entry for MMTV in the suckling mouse.

Animals↗
PubMed1981

Topographical and cytological localization of iron in rat and monkey brains.

The topographical localization of endogenous iron in rat and monkey brains coincides with the striato-pallido-nigral and the cerebellar corticonuclear pathways. EM observation reveals that iron is located in the soma and processes of glial cells and, above all, in the inner and outer loop of the myelin sheets. This raises the question of whether iron intervenes in some GABAergic systems.

Animals↗
PubMed1981

Immunological characterization of a mammary tumour virus from Swiss mice: multiple epitopes associated with the viral gene products.

The major antigens of a mouse mammary tumour virus (MMTV) isolated from the milk of exogenously infected MB+ Swiss mice were compared with the viral components of other MMTV strains by using the methodology developed by Teramoto et al. (1977 a). The anti-gp47 (Swiss) serum differentiated between type- and group-specific antigenic determinants on the major glycoprotein; two distinct type-reactivities were demonstrated, one of them being shared by the MMTVs (Swiss) and (RIII), and the other by the MMTVs (C3H) and (GR). The MMTVs (Swiss) and (RIII) also reacted identically in a 'type-specific' assay using an anti-p28 (Swiss) serum, but a distinct reactivity was observed with the MMTV (C3H). In the isologous test where an anti-(total RIII) serum was used to bind intact, externally labelled RIII virions, the Swiss virus was seen to possess a type-specific determinant on its surface which distinguished itself from both MMTVs (RIII) and (C3H). The Swiss/fC57BL mice (which are devoid of the milk virus and for this reason are referred to as MB-), expressed only the internal virus antigens in their mammary glands. Under the 'type-specific' assay conditions, the p28 antigen present in the mammary gland extracts of the MB+ mice was indistinguishable from the p28 antigen purified from the Swiss virion, but was clearly distinct from the p28 reactivity present in the mammary gland extracts of the MB- mice. The p28 (MB-) antigen may thus represent the expression of an endogenous virus sequence different from the milk virus genome.

Animals↗