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Biomedical subjects

H Mouray

Publications and source records attributed to H Mouray.

At least 19 recordsLinked to original sources
PubMed1997

Evolution of grass-cutter (Thryonomys swinderianus) inflammation markers: comparison with rabbit (Oryctolagus cuniculus) and rat (Rattus norvegicus).

An inflammatory reaction was induced in grass-cutters (Thryonomys swinderianus) by injecting turpentine. The changes in the plasma haptoglobin, fibrinogen, alpha 2 macroglobulin and immunoglobulin G was followed for 23 days by immunonephelometry. The results were compared to rat and rabbit. They showed that (a) the inflammatory reaction is delayed in the grass-cutter compared to rats and rabbits; (b) the concentration of haptoglobin increases less than in rat and rabbit; (c) the fibrinogen concentration is very low in the grass-cutter, despite hypercoagulability of blood; (d) the changes in the plasma alpha 2-macroglobulin in the grass-cutter seems to be comparable to that of rabbit alpha 1 macroglobulin in amplitude and in its slow return to the initial concentration; and (e) fibrinogen and haptoglobin are suitable markers for grass-cutter inflammation monitoring.

Animals↗
PubMed1997

[Selection criteria for the establishment of reference values in tropical zones. Application to specific proteins: C-reactive protein, haptoglobin, transferrin in gabonese children].

About 220 children (110 boys and 110 girls) aged 18 months to 10 years, 65.9% have been selected from anamnesis, clinical, and biological criteria to produce reference values on specific proteins dependent inflammatory, anemia and hemolysis (C-reactive protein = CRP; Transferrin = TRF and Haptoglobin: HPT). Specimens have been analysed by Nephelometric immuno-chemical method. For the two groups, A1 [18 months-5 years] and A2 [5-10 years], the reference values of the whole study population are reported: CRP (A1 3.35 +/- 3 mg/l: A2 2.40 +/- 2.30 g/l, with a significant difference at Student Fisher "t" test p < 0.03); TRF (A1 4.05 +/- 1.5 g/l; A2 4.50 +/- 1.4 g/l; NS, p > 0.05) HPT (A1 2.55 +/- 2.0 g/l: A2 1.20 +/- 1.10 g/l; S(r) p < 10(-5)). Furthermore, for TRF, HPT we must consider the sex in the results meaning because of significant difference into boys and girls.

Age Factors↗
PubMed1996

Detection of circulating antigens in Gabonese patients with Loa loa filariasis.

Circulating antigens were detected in sera of Gabonese patients with Loa loa filarial infection by co-electrosyneresis (Co-ES). The serum samples selected for this study were exposed to rabbit hyperimmune antifilarial antisera and human immune antisera: specific arcs were observed in 35/60 filarial patients, of whom 24/47 were microfilaraemic and 11/13 amicofilaraemic. The identity of rabbit hyperimmune antisera and loiasial immune sera was confirmed by the continuity of precipitation arcs. These preliminary studies were carried out to develop diagnostic tools for loiasis and to study the physiopathology of immune complexes.

Animals↗
PubMed1994

[Effects of refeeding on serum immunoglobulin (IgA, IgG, IgM) concentrations in children with severe protein-energy malnutrition].

BACKGROUND: Published studies on the serum immunoglobulin concentrations of patients with protein-energy malnutrition (PEM) have been contradictory. This report describes such a study in 21 Senegalese children. POPULATION AND METHODS: Twenty one Senegalese infants (mean age: 19 +/- 2 months) with severe PEM were included in the study. Their weight was less than 32% of the normal range-for-height and all had sparse, thin hair and dyspigmentation of the skin. They were all suffering from hypoproteinemia (less than 70% of normal) and hypoalbuminemia (less that 61% of normal). The presence or absence of edema, loss of subcutaneous fat and mental changes were used to classify them into three groups. 1) kwashiorkor: eight infants; 2) marasmus: eight infants; 3) kwashiorkor plus marasmus: five infants. The control group comprised 27 infants living in the same area and having the same dietary habits as the 21 sick infants. The 21 infants with malnutrition were refed for 3 weeks with a diet supplying 100-150 Kcal/kg/d and 5-8 g/kg/d protein. The plasma concentration of proteins, prealbumin and immunoglobulins was measured on days 0, 8, 15 and 21. RESULTS: The only significant change was in the IgG concentrations of group 1, which increased to normal levels by day 15 as did the total protein and prealbumin. CONCLUSION: Severe PEM can lead to a loss of one class of immunoglobulins, but this can be restored by refeeding.

Female↗
PubMed1992

[Rational prescription if protein evaluation in the diagnosis and follow up of protein-energy malnutrition].

In our countries, a good prescription of analysis would help to reduce hospital costs without modifying the efficiency of the diagnosis approach. In this work, the authors establish a bond between medicos and biologists by a good indication of protein check-up in the diagnosis and follow up of protein-energy malnutrition (PEM). After a discriminant analysis of all the results of protein check-up, two groups of markers are individualized depending on whether the PEM is accompanied or not by inflammatory complications. Finally, they recommend a systematic prescription of the useful group in case of inflammation associated with PEM, because infectious and parasitic diseases are almost constant among our malnourished infants.

Anthropometry↗
PubMed1991

Apolipoprotein A1 as an early index of protein-energy malnutrition.

Protein-energy malnutrition (PEM) is, together with infectious and parasitic diseases, a major cause of childhood illness in Africa. Diagnosis and treatment of PEM requires an accurate, simple and reliable method of assessing nutritional status from a blood sample. Plasma apolipoprotein (apo A1), prealbumin and albumin were measured in a group of Senegalese children suffering from PEM who had been hospitalized for refeeding, and in a group of control children. Statistical analysis of the results indicated that: (1) Plasma apo A1 was significantly correlated with prealbumin in assessing nutritional status (P less than 0.005 on day 8 of refeeding); (2) plasma apo A1 alone was sufficient for diagnosing and monitoring the dietary treatment of PEM; it was capable of detecting subclinical forms; (3) apo A1 could be used for differential diagnosis of forms of PEM; (4) plasma apo A1 concentration began to increase earlier (94% of control values at day 8) than did prealbumin (73% on day 8). We therefore propose apo A1 as an index of nutritional status in children living in areas where infectious and parasitic diseases are endemic.

Apolipoprotein A-I↗
PubMed1989

Erythrocyte and plasma cholesterol exchange in sickle cell anemia.

The effects of sickling on cholesterol exchange between red cell membranes and serum lipoproteins were studied by following the movement of tritiated cholesterol incorporated into erythrocytes. The initial rate of this exchange was greater in sickled cells than in normal cells. One quarter of the cholesterol in the sickled cells is quickly exchanged with plasma lipoproteins. After 15 minutes, the rate becomes identical for these two types of cells, reaching similar equilibrium at end. The sickling of red cells would explain the observed differences, although conditions of hypoxia and the saturation of the incubation medium with oxygen tend respectively to accentuate and to cancel this phenomenon.

Anemia, Sickle Cell↗
PubMed1986

Modifications in plasma levels of alpha macroglobulins and fibrinogen trypsin perfusion in normal rabbits and in rabbits in acute phase reaction.

During trypsin perfusions in normal rabbits and in rabbits in acute phase reaction (APR), there is no modification in cardiorespiratory functions except in the instant preceding death. The fibrinogen level decreases and fibrin is deposited in the vascular lumen. The alpha 2 macroglobulin (alpha 2 M) content diminishes more rapidly than the alpha I macroglobulin (alpha I M) content; moreover, in subjects in APR, the decrease of alpha I M is further slowed with increasing perfusion rates, whereas the decrease in alpha 2 M remains constant. All the alpha M are completely combined at death. Therefore, it can be assumed that only the hepatic filtering of the alpha I M enzyme complex is subject to saturation.

Animals↗
PubMed1984

An abnormal plasma antithrombin with no apparent affinity for heparin.

Congenital antithrombin abnormality was found in several members of a French family. No history of thrombotic episodes was associated with this abnormality. Plasma antithrombin concentration as well as the rate of thrombin inactivation by defibrinated plasma in the absence of heparin were normal. However, the heparin cofactor activity was decreased by about 50% in plasma of affected patients. Accordingly, about half the amount of plasma antithrombin did not bind to gel bound heparin. Moreover the crossed immunoelectrophoretic pattern in the presence of heparin demonstrated two peaks of antithrombin, the slower one migrating as normal antithrombin when heparin was omitted from the first agarose gel. It was concluded that molecular alteration of the antithrombin molecule seemed to affect only the heparin binding site thus preventing from any rate enhancement of thrombin inactivation.

Antithrombin III Deficiency↗
PubMed1983

Comparison of immunochemical and biological properties of human anti thrombin during blood clotting and upon interaction with exogenous thrombin.

Modification of immunological and biological properties of human antithrombin were studied in plasma-serum pairs and in defibrinated plasma supplemented with human thrombin. Modified antithrombin obtained through whole-blood clotting or upon addition of exogenous thrombin appeared the same with regards to its electrophoretic or biological properties. However, amounts of thrombin higher than that physiologically available, had to be used to obtain a "serum-like" antithrombin in thrombin supplemented plasma suggesting different pathways for this transformation. This was in agreement with the observation in plasma of a modification of antithrombin antigenic properties upon thrombin addition whereas no difference was demonstrated when comparing serum to normal plasma. It may be concluded that the inactivation of antithrombin and the appearance of electrophoretically modified forms in normal serum is not mainly due to the formation of enzyme-inhibitor complexes and therefore that proteolytically modified, enzyme-free forms of antithrombin demonstrated in purified systems (Fish et al. 1979) could be of physiological relevance.

Antithrombins↗
PubMed1979

Interactions in vitro and in vivo between rat serum protease inhibitors and anodal and cathodal rat trypsin and chymotrypsin.

Reaction mixtures of increasing amounts of the pancreatic homologous proteases, anodal and cathodal chymotrypsin and trypsin, respectively, and normal rat serum were analyzed by immunoelectrophoretic methods in order to determine their distribution on serum protease inhibitors. This paper concerns three proteins occurring in normal serum and capable of binding protease viz. alpha1-macroglobulin, alpha1-antitrypsin and alpha1-inhibitor 3. The distribution of the enzymes among these protease inhibitors differed significantly from one protease to another. The distribution of the proteases among the serum protease inhibitors following intravenous injection of 125I-labelled proteases corresponded to that in vitro. Complexes formed with alpha1-macroglobulin and alpha1-inhibitor 3 were quickly eliminated irrespective of the enzyme species used, whereas those formed with alpha1-antitrypsin persisted much longer in the circulation.

Animals↗