Food allergy to peanuts in France--evaluation of 142 observations

BACKGROUND: The increase in frequency of peanut allergy and fatal cases have been reported. OBJECTIVES: The objective of this study is to document the severity of food allergy to peanuts by evaluating the reactive dose of peanuts and to search for the role of peanut oil. METHODS: This study is carried out on the basis of 142 observations collected according to the same diagnostic methodology in two allergy centres in France. Skin-prick-tests were performed with peanut powder, peanut oil and peanut oil proteinic extract. Labial provocation tests were performed on 121 patients. The reactive dose of peanuts and the role of peanut oil were determined by standardized oral provocation tests in 50 and 62 patients respectively. The data are computerized and the data bank includes 509 food allergic patients. RESULTS: Allergy to peanuts represents 28% of food allergies and occurs under 1 year of age in 46% of cases, under 15 years of age in 93%. The clinical features were atopic dermatitis (40%), angioedema (37%), asthma (14%), anaphylactic shock (6%) and digestive symptoms (1.4%). The specific IgE were class 3 or higher in 80% of cases. The total reactive dose was less than 100 mg in 25% of cases, from 100 mg to 1 g in 62.5%. All patients reacted to a dose of less than 7.1 g. The threshold of peanut reactivity was lower than the threshold of egg reactivity. An allergy to peanut oil was demonstrated in 14 patients. CONCLUSION: The severity of peanut allergy and the early onset of the occurrence of this allergy is documented. The role of residual allergenic proteins in peanut oil is established by positive skin-prick tests to proteic extracts from peanut oil and by double-blind placebo-controlled challenges to peanut oil. The increased consumption of allergens in the form of peanut oil and fats can contribute to the occurrence or persistence of symptoms and may be suspected to increase the risk of sensitisation.     

Evolving magnetic resonance spinal cord trauma in child: from hemorrhage to intradural arachnoid cyst

Acquired arachnoid cysts of the spinal cord are uncommon causes of spinal cord compression in the pediatric group. Meningitis, trauma and hemorrhage are considered to be causative or contributing factors. Interestingly, no spinal arachnoid cysts have been reported in patients after subarachnoid hemorrhage or meningitis, conditions expected to cause arachnoid scarring. We describe a child of 1 year and 10 months with thoracic spine trauma with crural paraplegia and anesthesia at level T5 submitted to serial magnetic resonance imagery at 5 days and 18 months, after trauma showing evolution from subarachnoid hemorrhage and adhesions of the arachnoid space to a posterior hypertensive thoracic intradural arachnoid cyst.     

Molecular modeling of immunoglobulin light chains implicates hydrophobic residues in non-amyloid light chain deposition disease

Light chain deposition disease is a severe complication of certain immunoproliferative disorders, due to the secretion of a monoclonal light chain which precipitates close to basement membranes of several tissues. A kappa isotype restriction and an unusual frequency of a variable region subgroup (VkappaIV) suggest that precise structural features govern the propensity of pathogenic light chains to precipitate in extracellular spaces. We studied primary structures of light chains from six patients with light chain deposition disease in comparison with light chains from other pathological conditions. Sequence alignment revealed the presence of certain amino acids only in light chain deposition disease, in particular non-polar replacing hydrophilic residues. To determine the role of these residues, structures of the variable domain from four kappa chains belonging to VkappaI and VkappaIV subgroups responsible for deposition disease were modeled using known immunoglobulins as templates. The most evident structural features shared by all pathogenic light chains were hydrophobic residues exposed to the solvent in complementarity determining regions 1 or 3. In contrast to immunoglobulin light chain- related amyloidosis, where deposition of organized material might be due to electrostatic interactions between light chain dimers, hydrophobic interactions could enhance amorphous precipitation in non- amyloid light chain deposition disease.      

DEHYDRATION BY DESORPTION AND BY SPRAY DRYING OF DAIRY PROTEINS: INFLUENCE OF THE MINERAL ENVIRONMENT

A drying method by desorption in a water activity meter was used to simulate the conditions of spray drying and to determine the water transfer inside dairy concentrates towards the surface and from the surface to the drying air. The concentrates were also spray dried and solubility index of powders were determined during reconstitution. Whey protein concentrates (WPC) and native phosphocaseinate suspensions (NPCS) were used to study the effect of NaCl (420 mM), CaCl₂ (222 raM), sodium phosphate (173 mM) and sodium citrate (238 mM) on the water transfers. The decrease in water transfer during drying was explained by the high hygroscopicity of added mineral salts to WPC. NaCl addition to NPCS decreased the water transfer during drying, but increased the solubility index. Citrate and phosphate addition to NPCS increased the water transfer during drying and reconstitution. CaCl₂ increased the water transfer during drying but the solubility index was always low. Results are discussed as a function of the aqueous environment, of the nature of mineral salts, of the structure of dairy proteins and of protein solvation.     

Ovohemerythrin, a major 14-kDa yolk protein distinct from vitellogenin in leech

A 14-kDa protein was identified as a major component of mature oocytes of the leech Theromyzon tessulatum. This protein was, like vitellin, detected in the content of yolk granules and was purified by gel-permeation and ion-exchange chromatography. The yolk protein corresponded to an iron-binding protein which exists in a monomeric unglycosylated form and had no similarities to vitellin. However, a strong resemblance between this protein and sipunculid hemerythrin, a non-heme iron-binding protein, was observed on the basis of its characteristics including molecular mass, iron content, ultraviolet/visible spectrum, amino acid composition and N-terminal sequence. These similarities with hemerythrin and the accumulation of the protein in the oocyte justify the name ovohemerythrin given to the molecule. A coelomic-fluid protein immunologically related to ovohemerythrin was detected in vitellogenic animals. The protein was purified with the chromatographic procedure used to isolate ovohemerythrin from oocytes and was found to be similar to the oocyte protein. This circulating ovohemerythrin was present in large amounts in the coelomic fluid while gametogenesis is in progress, i.e. after the third and last blood meal of the animal (stage 3), except at the time of oocyte enlargement when its concentration decreases dramatically. However, in contrast to vitellogenin, which is detected specifically in the coelomic fluid of leeches at stage 3, circulating ovohemerythrin is also observed after the first (stage 1) and second (stage 2) blood meal. This observation suggests a more complex function for ovohemerythrin than being merely a yolk nutrient for the embryo.     

The National Cancer Data Base report on the relationship of race and national origin to the histology of nasopharyngeal carcinoma

This study was undertaken to clarify several aspects of morphological and taxonomic characters of Physaloptera bispiculata Vaz and Pereira, 1935, a parasite of the water rat, Nectomys squamipes. The cephalic structures (including lips, papillae, teeth, amphids, and porous areas) and details of the posterior end of male and female adult worms were examined by scanning electron microscopy, leading to the addition of new taxonomic characters for this species. We consider P. bispiculata a valid species, based on a comparative analysis of the specific characters for P. bispiculata and P. getula Seurat, 1917, including the morphology and morphometry of body structures as well as number and disposition of caudal papillae of the males.