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R Parisot

Publications and source records attributed to R Parisot.

8 recordsLinked to original sources

A universal method for determining intensive care unit bed requirements.

OBJECTIVE: Most methods used to estimate ICU bed needs rely either on simple formulas that do not consider the actual needs of the population or on simulations that are too specific to be applicable to all hospitals. We sought to develop a universally applicable nonparametric method. DESIGN AND SETTING: For each day, the number of immediate patient transfers to other ICUs because of a full unit and the number of patients treated in the ICU were collected. The number of beds needed was selected according to the minimization of both the mean and the variance of three parameters (accessibility, safety, and efficiency). This method was applied to the ICU of a general hospital. Robustness of the model was assessed using outliers. MAIN RESULTS: During the 5-month study period, 215 ICU stays were collected. The method selected a ten-bed model whereas length-of-stay ratio and case-mix methods selected a twelve- and height-bed models respectively. An unusual increase in admission requests had no consequence on the bed number selected, indicating that the method was robust. None of the parameters were dependent on specific ICU characteristics, establishing that this method is applicable to any type of hospital ward. CONCLUSION: Our model is reliable for determining the number of beds needed in any type of ICU and can be used by all ICU managers. The software is available.

Beds↗

[Severe intoxication probably from olanzapine (Zyprexa). Beneficial effect of glucagon].

We report the case of a 43-year-old schizophrenic who sustained, after 12 days of treatment including olanzapine (20 mg.day-1), carbamazepine, levomepromazine and alprazolan, a severe shock with bradycardia (HR: 40 b.min-1), circulatory collapse (SAP: 60 mmHg), hypothermia (T: 27 degrees C), coma and disseminated intravascular coagulation. A significant improvement was obtained with high doses of intravenous glucagon, whereas the normalization of central temperature, atropine, adrenaline and volume loading had been inefficient. Olanzapine, alone of associated with other psychotropics, could cause severe circulatory collapse with hypothermia and coma responding to a treatment including glucagon.

Adult↗

Wide tissue distribution of axolotl class II molecules occurs independently of thyroxin.

Unlike most salamanders, the Mexican axolotl (Ambystoma mexicanum) fails to produce enough thyroxin to undergo anatomical metamorphosis, although a "cryptic metamorphosis" involving a change from fetal to adult hemoglobins has been described. To understand to what extent the development of the axolotl hemopoietic system is linked to anatomical metamorphosis, we examined the appearance and thyroxin dependence of class II molecules on thymus, blood, and spleen cells, using both flow cytometry and biosynthetic labeling followed by immunoprecipitation. Class II molecules are present on B cells as early as 7 weeks after hatching, the first time analyzed. At this time, most thymocytes, all T cells, and all erythrocytes lack class II molecules, but first thymocytes at 17 weeks, then T cells at 22 weeks, and finally erythrocytes at 26-27 weeks virtually all bear class II molecules. Class II molecules and adult hemoglobin appear at roughly the same time in erythrocytes. These data are most easily explained by populations of class II-negative cells being replaced by populations of class II-positive cells, and they show that the hemopoietic system matures at a variety of times unrelated to the increase of thyroxin that drives anatomical metamorphosis. We found that administration of thyroxin during axolotl ontogeny does not accelerate or otherwise affect the acquisition of class II molecules, nor does administration of drugs that inhibit thyroxin (sodium perchlorate, thiourea, methimazole, and 1-methyl imidazole) retard or abolish this acquisition, suggesting that the programs for anatomical metamorphosis and some aspects of hemopoietic development are entirely separate.

Ambystoma↗

MHC-like molecules in some nonmammalian vertebrates can be detected by some cross-reactive monoclonal antibodies.

mAb to human and mouse MHC molecules were tested for binding to blood or spleen cells of various nonmammalian vertebrates by immunofluorescence and flow cytometry. Those that bound were used to immunoprecipitate cross-reactive molecules from biosynthetically or cell surface-labeled spleen or blood cells. In addition, mAb to human MHC molecules were screened by Western blots. As expected from the results with xenoantisera, there were few mAb that cross-reacted, and many of these cross-reactions were not specific for MHC-like molecules. Less than 10% of the mAb tested bound to the cells of any particular species, with very few positive for more than one species. Of those mAb that bound cells, many failed to precipitate any radioactive bands, and most bands precipitated were not recognizable as MHC-like molecules. Five mAb reacted with Xenopus class II, one of which also immunoprecipitated axolotl class II. Another of these reacted with a candidate for class II in the lamprey, but this molecule had features unlike those expected for mammalian class II molecules. Four other mAb reacted with candidate molecules. in the trout and shark. None of the mouse alloantibodies immunoprecipitated nonmammalian vertebrate MHC-like molecules. In contrast to the results with most xenoantisera, the mAb cross-reacting with amphibian class II molecules recognized a number of different linear epitopes on the surface of the polymorphic non-Ig beta 1 domain of class II molecules. Few mAb recognized bands in Western blots of nonmammalian vertebrate cells and the candidate molecules from fish had features different from known mammalian MHC molecules.

Amphibians↗

MHC-like molecules in some nonmammalian vertebrates can be detected by some cross-reactive xenoantisera.

Rabbit antisera raised to human and chicken MHC molecules were used to immunoprecipitate cross-reactive molecules from biosynthetically and cell surface-labeled spleen and/or blood cells of representative vertebrate species. Five major points emerged: 1) There were many nonspecific cross-reactions using these techniques, so various criteria were developed to distinguish these from true MHC-like molecules. 2) Only very small subpopulations of immunogen-specific antibodies cross-reacted with MHC-like molecules in other nonmammalian species. These subpopulations were different for each species and even within a species, sometimes being so limited as to behave like alloantisera. This led to a very scattered pattern of true cross-reactions that sometimes failed to reflect the properties of the bulk antibody population. 3) Antisera containing antibodies to class II beta- and class I alpha-chains cross-reacted better and more widely than those to B-G, class II alpha and, in general, beta 2-microglobulin. 4) Some cross-reactive antibodies were clearly directed to epitopes on the surface of the mature heterodimers, but many seemed to recognize nonlinear cryptic determinants, presumably in the contact regions between the chains. These latter antibodies recognized biosynthetic intermediates and also a variety of unusual cell surface MHC-like molecules present in reptile and amphibian, but absent in the mammal and chicken cells tested. These included E homodimers whose relationship to chicken B-G molecules is unknown. 5) MHC-like molecules were identified in a bird, three reptiles, and two amphibians, but no molecules with the expected properties were found with these reagents in any of the fish tested.

Amphibians↗

Major histocompatibility complex-encoded class I molecules are absent in immunologically competent Xenopus before metamorphosis.

The expression of class I and class II major histocompatibility complex (MHC)-encoded antigens has been examined at various stages of the development of the clawed frog, Xenopus. By immunoprecipitation with alloantisera or xenoantisera from radio-labeled spleen and thymus lysates, and by mixed lymphocyte reaction analysis, it was determined that the same class II molecules are expressed throughout ontogeny. In contrast, by fluorescence on frozen sections of tadpoles and by immunoprecipitation, the class I molecule is not detected in tadpoles, but appears on all tissues at the climax of metamorphosis. Animals maintained as tadpoles for long periods of time by chemical treatment do express class I antigens; thus, their expression can be independent of other biochemical and morphological changes that occur at metamorphosis. Immunofluorescence detects an otherwise uncharacterized MHC-linked alloantigen on tadpole thymic epithelium from the earliest stages of thymus differentiation.

Animals↗

Small nuclear U-ribonucleoproteins in Xenopus laevis development. Uncoupled accumulation of the protein and RNA components.

The accumulation of protein and RNA components of small nuclear U-ribonucleoprotein particles is non-co-ordinate during oogenesis and early embryogenesis in Xenopus laevis. Northern blot hybridization of a cloned Xenopus U2-RNA gene to oocyte and embryo RNAs demonstrates that the amount of small nuclear U2-RNA per oocyte reaches a plateau early in oogenesis (at the start of yolk deposition); further accumulation is not observed in oogenesis, nor in embryogenesis until the late blastula stage. In contrast, we show by immunoblot analysis that the proteins that bind to small nuclear U-RNAs continue to be accumulated after vitellogenesis begins, reaching maximum amounts only at the end of oocyte development. No further accumulation of these proteins is seen during embryogenesis. The consequences of this non-co-ordinate synthesis of small nuclear RNA and small nuclear RNA-binding proteins are as follows: a 10- to 20-fold excess of the protein components of the small ribonucleoprotein particles over small nuclear RNA exists in large oocytes; the bulk of the protein is cytoplasmic, while the RNA is nuclear. Thus the excess protein in the cytoplasm is uncomplexed with RNA. The imbalance between protein and RNA is not corrected until the late blastula or early gastrula stages of embryogenesis, when a tenfold increase in the amount of small nuclear U2-RNA is detected. Thus the protein, but not the RNA, components of small nuclear U-ribonucleoprotein particles are stockpiled in oocytes for later use in embryonic development. During the course of these studies, we also found that there are tissue-specific differences in the Sm-antigenic proteins of X. laevis.

Animals↗