Immunohistochemical localization of a gastrin-like peptide in the brain of an amphibian,Xenopus laevis Daud.

Summary The indirect immunofluorescence technique was used to demonstrate a substance reacting with gastrin antisera in the brain of Xenopus laevis.Immunoreactive material was found in two sites: (1) In the caudal hypothalamus more precisely in the nucleus infundibularis ventralis, (NIV) of the pars ventralis of the tuber cinereum, (PVTC). The fluorescent axons of the reactive parikarya of the NIV give rise to two symmetrical tracts which run rostro-ventrally and join, in the infundibular floor, the preoptico-hypophysial tract, where they form an uneven median tract coursing caudally and running along the medio-tuberal area before entering the external zone of the median eminence. (2) In the anterior preoptic area (APOA), where numerous nerve fibers and endings form a dense network near the preoptic recess. The exact origin of these terminals has not yet been determined.Control of immunohistochemical specificity shows that the labeling by gastrin antisera is suppressed by gastrin (2–17), but also by cholecystokinin (CCK) and pentagastrin (Peptavlon). These results indicate that the immunoreactive substance revealed belongs to the gastrin group and has an antigenic determinant composed of the amino acid sequence or a portion thereof common to gastrin, CCK and Peptavlon (Trp-Met-Asp-Phe).It should be emphasized that, in the brain of Xenopus laevis, both gastrinimmunoreactive sites correspond to the sites of uptake of steroid hormones (Kelley et al., 1975; Morrell et al., 1975).Supported by the D.G.R.S.T., Contrat n 77.7.0648     

Réflexions critiques sur l'écologieet la systématique des Lingules actuelles et fossiles

New topics on ecology and systematics of recent and fossil Lingulids lead to an obvious revision of our knowledges on this zoological group. At first, the recent species need systematics and taxonomy on the bases of new described specific criteria (as, morphology of deltidial areas, muscle disposition); the results are briefly indicated. But, in fossil species, disorder and disparity of used characteristics are emphasized.The general conceiving on ecology of Lingulids are reviewed and discussed, especially on bathymetry and salinity; sediment and oxygenation conditions; taphocoenosis and lingulid «communities. On recent species, all these points are also studied, especially some ecological requirements (salinity, bathymetry, grain size), and mechanism of burrowing ability, burrow living positions in the sediments, as shell preservations after death and fossilization, to facilitate the paleobiotope interpretations. Recent animals are euryhalin, surviving at salinities from about 13 to 42‰; they could be considered as well adapted to waters with strong salinity fluctuations. They show preference to fine sand bottoms (lowest particle size about 40–60 μm). Their bathymetric distribution occurs between 0 and about 500 m (Lingula especially between 5–50 m; Glottidia 15–70 m). The isotherms 8–10°C seem to restrict their geographical and bathymetric distribution.Therefore, some post-palaeozoic lingulid bedsare studied or redescribed on the bases of the above discussed characteristics, and new interpretations on the environmental situation are given (Trias of Vosges Mountains; Oligocene from Japan; Eocene of London Basin). More caution must be used in study of fossil Lingulids that are not especially animals living in infralittoral bottoms with low salinity and deficient oxygenation, as generally accepted.     

Mitochondrial protein alteration in active brown fat: A sodium dodecyl sulfate-polyacrylamide gel electrophoretic study

The polypeptide composition of mitochondria isolated from the brown adipose tissue of control rats (bred at 22°C) or cold-exposed animals (bred at 6°C) was compared using sodium dodecyl sulfate-polyacrylamide gel electrophoresis. A striking increase in the content of an unknown polypeptide (apparent molecular weight 32,000 daltons) was found after cold adaptation, a phenomenon which was reversed during re-adaptation to a normal temperature. This protein seems to be localized in the membrane fraction of the mitochondria.     

Association-dependent active folding of alpha and beta subunits of lutropin (luteinizing hormone).

The kinetics of the structural transition of ovine lutropin (luteinizing hormone) from a dissociated and partially unfolded state to a biologically active, folded and associated state were studied from pH 1.8 to 6.5 by difference spectroscopy, circular dichroism, light scattering and ultracentrifugation under various conditions of temperature and ionic strength. Between pH 2.8 and 5.3 there is a thermodynamically reversible equilibrium between the two states of the hormone with a half-transition pH of 4.3 ± 0.1 at 26 °C. The interconversion of native folding to dissociated state is strictly first-order, and most of the kinetic results can be described in terms of two exponential decays with lifetimes of 20 and 100 seconds at pH 2 and 26 °C with one intermediate. A second intermediate with a short lifetime (1.5 s) is detected with stopped-flow experiments; its spectroscopic contribution is small. Refolding from the dissociated state is always second-order in the concentration range studied (12 to 110 μm lutropin), with rates at 26 °C, 1.4 m⁻¹ s⁻¹ at pH 4.3 and 2.2 m⁻¹ s⁻¹ at pH 5.3. The temperature dependence of the rate constant of active folding at pH 5.3 corresponds to activation parameters $\text{ΔH}{}^1\text{= +23.5}\text{kcal mol}{}^{\mathrm{-1}}\text{and}\text{ΔS}{}^1\text{= +21.6}\text{cal deg}{}^{\mathrm{-1}}$ mol⁻¹.From these data and computer-simulation studies, a simplest possible mechanism is proposed that involves the formation of a loose complex between the α and β subunits of the hormone, followed by a slow step of formation of the active, folded state. In the pituitary gland this would be a necessary pathway towards the active form. The storage of the hormone in the gland would offer enough time for this activation step to proceed.     

Régulation et signification physiologique de l'aspartate-ammonium lyase (aspartase) de Pseudomonas fluorescens type R

The biosynthesis of aspartate-ammonium lyase, the enzyme which is induced by aspartic acid, is specifically repressed by fumaric acid. In the presence of aspartate, the enzyme permits the deamination of this compound by the cell. Aspartic acid is converted into fumaric acid which is an intermediate in the Krebs'cycle. The reaction may be considered as an anaplerotic sequence. In the absence of aspartic acid in the culture medium, its role is anabolic; the enzyme catalyses the biosynthesis of this amino acid. Therefore it appears that the reversible reaction fumarate+NH₃=aspartate catalysed by aspartase is included in amphibolic processes.     

Primary structure of sorghum malate dehydrogenase (NADP) deduced from cDNA sequence. Homology with malate dehydrogenase (NAD)

Malate dehydrogenase (NADP) (NADP-MDH) is an important enzyme of the photosynthetic CO2 fixation pathway of C4 plants. We have isolated two clones from a sorghum lambda gt11 cDNA library (CM3, 932 bp, and CM7, 1441 bp). Nucleotide sequence analysis of the cDNAs CM3 and CM7 showed the existence of two NADP-MDH mRNA species encoding different enzyme subunits. Microsequencing of the N-terminus of the mature protein indicated that a specific cleavage of 13 amino acids occurred during the purification steps of the enzyme. The full-length cDNA CM7 contains a large open reading frame encoding an NH2-terminal transit peptide of 40 amino acids and a mature protein of 389 amino acids (42.207 kDa). Alignment of the NADP-MDH sequence with those of several malate dehydrogenases revealed some similarities with NAD-MDHs.     

Anti-hypertensive effects of Rosuvastatin are associated with decreased inflammation and oxidative stress markers in hypertensive rats

Among their pleiotropic effects, statins exert antioxidant and anti-inflammatory properties. The aim of this study was to evaluate in normotensive (WKY) and in spontaneously hypertensive rats (SHR) the effect of rosuvastatin (ROSU) treatment on (1) plasma inflammation markers and endogenous NO synthase inhibitor (ADMA) levels, (2) reactive oxygen species (ROS) generated by circulating leukocytes and (3) vascular oxidative stress and tissue inflammation markers. Plasma cytokines were higher in SHR than in WKY, except for IL-4, which was lower in SHR than in WKY. SHR monocytes exhibited higher production of ROS than did WKY monocytes. In the experimental conditions, ROSU did not modify plasma cholesterol levels in SHR but attenuated the increase in systolic blood pressure. In SHR only, ROSU lessened pro-inflammatory cytokines and ADMA levels, increased IL-4 and reduced ROS production in circulating monocytes. These results demonstrate the beneficial effects of ROSU in SHR, independently of any lowering of cholesterol levels.