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PubMed2005

Peanut- and cow's milk-specific IgE, Th2 cells and local anaphylactic reaction are induced in Balb/c mice orally sensitized with cholera toxin.

BACKGROUND: The development of animal models developing specific immunoglobulin (Ig)E presenting the same specificity as human IgE and similar clinical symptoms as those observed in allergic patients are of great interest for the understanding of mechanisms involved in the induction and regulation of food allergy. METHODS: Balb/c female mice were sensitized with whole peanut protein extract (WPPE) by means of intraperitoneal (i.p.) injections with alum or gavages with cholera toxin (CT). The WPPE specific IgE, IgG1 and IgG2a were monitored. Th2 cells activation was analysed assaying interleukin (IL)-4 and IL-5 vs IFNgamma on reactivated splenocytes. Local anaphylactic reaction was evaluated by assaying histamine in faecal samples. The oral sensitization protocol was further extended to cow's milk proteins (CMP). RESULTS: Balb/c mice developed high peanut-specific IgE and IgG1 responses either after i.p. or oral sensitizations. In both cases, antibodies were specific to polymer of glycinin fragments, containing polypeptides from Ara h3/4, and to a lesser extent to Ara h1 and Ara h2. Interleukin-4 and IL-5 production were evidenced. Balb/c mice could also be sensitized to CMP, as demonstrated by CMP-specific IL-4 and IL-5 secretions and induction of IgE specific for whole caseins, beta-lactoglobulin, serum bovine albumin and lactoferrin. Of interest was the occurrence of a local anaphylactic reaction in the peanut and CM models. CONCLUSIONS: In contrast with previous authors, Balb/c mice were sensitized and evidenced an allergic reaction after oral administrations of peanut or CMP plus CT, providing an interesting model for further studies on immunopathogenic mechanisms.

Anaphylaxis↗
PubMed2001

Mutagenicity and identification of mutagenic compounds of fumes obtained from heating peanut oil.

Since the fume of cooking oil has been reported to increase the risk of lung cancer, the objectives of this study were to evaluate the mutagenicity and to find the mutagens in the fumes of peanut oil heated to the smoke point. Peanut oil prepared from roasted peanut kernel showed a lower smoke point, less unsaturated fatty acids, more fume formation, and stronger mutagenicity than that from unroasted kernel. Further investigation of mutagenic compounds was performed by the Ames test and gas chromatography/mass spectrometry analysis. Among the 12 compounds identified from the neutral fraction of methanol extract, four compounds at a dose of 10 microg per plate were mutagenic to Salmonella Typhimurium TA98 and TA100 in the order of trans-trans-2,4-decadienal > trans-trans-2,4-nonadienal > trans-2-decenal > trans-2-undecenal. Results report the enal compounds formed as the mutagens in the fumes of peanut oil and indicate that inhaling cooking fumes might cause carcinogenic risk.

Gas Chromatography-Mass Spectrometry↗
PubMed2000

[Contamination by aflatoxins of local peanut oils prepared in Senegal].

Aflatoxins are mycotoxins produced by certain strains of fungus (Aspergillus) which develop in peanut seeds. Peanut oil and peanut meal are widely used in Senegal. The risk of intoxication is quite real. We determined aflatoxin contamination levels in peanut oil and food prepared by small scale production plants in the Kaolack and Diourbel regions of Senegal. High performance liquid chromatography (HPLC) of the different samples showed that 80% of them were contaminated. Aflatoxin B(1), B(2), G(1) and G(2) were detected. The pattern of contamination was similar for the two regions. Aflatoxin B(1) was prevalent and found in over 85% of the samples. The mean content of this mycotoxin (the most dangerous toxin) was about 40 ppb, a value which largely exceeds specifications for allowable levels.

Aflatoxins↗
PubMed2001

Development and characterization of edible peanut protein films.

In this work, novel edible films were developed from peanut protein with sorbitol as a plasticizer. The peanut protein was extracted from peanut flour. Two groups of films were prepared. One group contained 10% in weight of natural oil/fat of the peanuts, while the other group contained no oil/fat. Six types of films with 37.5%, 44.5%, and 50% sorbitol content by weight, with and without fat, were chosen for mechanical properties characterization and microscopic observations. It was found that with the increase of sorbitol content, higher tensile strength and higher Young's modulus were achieved for the films without fat. However, films with fat exhibited maximum strength and modulus at 44.5% sorbitol content. Relationships between the mechanical properties and the microscopic features of these films were established. It was found that the higher the content of the sorbitol, the more evident the crystalline structure. Grant numbers: NCC9-51.

Arachis↗
PubMed2002

Peanut allergy in-flight.

An unknown but probably significant number of airline passengers are allergic to peanuts. Reactions can be mild, moderate, or severe (life threatening). Because peanuts are sometimes dispensed by flight attendants on commercial flights, there is public concern that passengers are at risk of an in-flight allergic reaction. Although there is little in the medical literature to substantiate this concern, there are anecdotal cases of inflight allergic reactions to peanuts from ingestion, dermal contact, and inhalation of airborne peanut particles. Consequently, there are several options among which the airlines must choose in order to satisfy passenger concerns.

Aerospace Medicine↗
PubMed2000

[Aflatoxin contamination level in artisanal and industrial peanut butter food in Dakar (Senegal)].

Aflatoxins are mycotoxins produced by some strains of fungus (Aspergillus) which develop in peanut seeds. Peanut oil and past are very used up in Senegal, then the aflatoxin poisoning risk is very actual. The aim of this study was to determinate the aflatoxin level in artisanal and industrial peanut pastry food from Dakar (Sénégal). High Performance Liquid Chromatography (HPLC) analysis of the different samples showed that the most contaminated by aflatoxins are artisanal pastry sold in different market of Dakar (Sénégal). Indeed, 40% of these samples contained mean values of aflatoxin B1 (the most dangerous) widely over allowable EEC specifications (5ppb). Furthermore, most of industrial and domestic peanut pastry were cleaned and could be consumed without risk.

Aflatoxin B1↗
PubMedDate not supplied

Clinical pearls and pitfalls: peanut allergy.

A case of pediatric peanut allergy is presented. Pathophysiology, clinical characteristics, diagnostic test, case management, and natural history are reviewed. Clinical Pearls and Pitfalls include: (1) About 20% of young infants will outgrow peanut allergy, especially if IgE levels measured by ImmunoCAP RAST are less than SkU/L. (2) Cases of resensitization have been documented after negative peanut oral challenges. (3) Only a negative food challenge can provide convincing evidence that the patient has outgrown his or her peanut allergy.

Child↗
PubMed1988

Cholesterol vehicle in experimental atherosclerosis. A brief review with special reference to peanut oil.

In general, the level of unsaturation of a fat determines its effect on plasma cholesterol level-the level being lower with more unsaturated fat. However, some exceptions do exist. One such exception is cocoa butter, which is not as cholesterolemic or atherogenic for rabbits as would be expected from its level of saturation. The reason for this anomaly is believed to be the high level of stearic acid present in cocoa butter. Peanut oil is also anaomalous, being unexpectedly atherogenic for monkeys, rabbits, and rats. Randomization of peanut oil reduces its atherogenicity, suggesting that the structure of the triglyceride comprising peanut oil may affect its atherogenic potential. Another possibility is that a lectin present in peanut oil may be responsible for its atherogenic capacity.

Animals↗
PubMed1982

Peanut lectin-binding sites in large bowel carcinoma.

Peanut lectin is known to bind to B-D-Gal-(1 leads to 3)-D-GalNac which provides antigenic determination for the T (TAg) blood group antigen. We examined 33 rectosigmoid carcinomas and 15 corresponding controls for their ability to express peanut lectin-binding sites. In controls one could localize TAg to the supranuclear portion of the cell, however, in cancers one noticed a cytostructural relocalization of TAg with the following two major patterns: localization to the region of the glycocalyx and localization intracytoplasmically in the apical portion of the cell. These two patterns were associated with glandular differentiation. Less frequently noted or in association with the above was a mucin glob-like pattern and/or a fine diffuse intracytoplasmic pattern associated with solid, nonglandular areas. The more poorly differentiated cancers less frequently expressed peanut lectin-binding sites. Benign (nontransitional zone) epithelium in those patients whose tumor expressed TAg was negative for peanut lectin-binding sites in 66 per cent of the cases. Reduced tumoral glycosyltransferases may explain this increased synthesis of TAg in cancers as compared with controls, if one considers TAg to be an incomplete glycoprotein of the MN blood group system.

Adenocarcinoma↗
PubMed1982

Lymphocyte cell surface glycoproteins which bind to soybean and peanut lectins.

In cellular immunology, peanut (Arachis hypogaea) lectin has been used to selectively agglutinate immature lymphoid cells and soybean (Glycine max-lectin to agglutinate B lymphocytes. We have used affinity chromatography to study the surface glycoproteins of rat and mouse lymphoid cells which bind to these lectins. Thymocyte and T and B lymphocyte glycoproteins were analysed either without modification (native) or after the removal of sialic acid with neuraminidase (asialo). The only native glycoprotein which was seen to bind to peanut lectin was the 95,000 mol. wt sialoglycoprotein from thymocytes. The equivalent molecules from T lymphocytes bound to peanut lectin only after neuraminidase digestion. Thus the selective agglutination of thymocytes by peanut lectin would seem to be due to a partial lack of sialic acid residues on the O-glycosidically-linked oligosaccharides of the thymocyte sialoglycoprotein. The B lymphocyte form of the leucocyte-common antigen was the only prominent native glycoprotein which was seen to bind to soybean lectin and this probably accounts for the specific binding of this lectin to B cells. The leucocyte-common antigens, in their asialo forms, from thymocytes and B and T lymphocytes differed in their binding to the lectins and this establishes that these glycoproteins which share antigenic determinants differ in their carbohydrate structures.

Animals↗
PubMed1994

[Experimental study of peanut sensitization in guinea pigs].

An experimental study of sensitization to peanut has shown that this can be induced in guinea pigs by crushed peanuts ingested daily for three weeks although peanut oil, which is found in some preparations of vitamin D, did not sensitize the guinea pigs, when compared with a control group and a group of guinea pigs that had received only a "flash" dose of 1 ml peanut oil by the oral route.

Administration, Oral↗
PubMed1994

Changing patterns of peanut agglutinin labelling in the dorsal cochlear nucleus correspond to axonal ingrowth.

Various studies have suggested that glycoconjugates may influence connectivity and lamination in the developing central nervous system and may function as barriers to neuritic extension. It has been proposed that the peanut agglutinin lectin labels a glycoconjugate subserving a barrier function. We chose to investigate the distribution of this peanut-agglutinin-labelled glycoconjugate in the dorsal cochlear nucleus of the developing hamster since the development of the dorsal cochlear nucleus is well characterised and its axons obey laminar boundaries. The distribution of peanut agglutinin label throughout the cochlear nucleus delineated zones that cochlear axons fail to invade. In the dorsal cochlear nucleus, laminar differences were reduced on postnatal d 13 and virtually disappearing by postnatal d 23. Label in the molecular layer dissipated as axons and dendrites grew into this layer. These patterns of peanut agglutinin binding correspond to axonal ingrowth and are consistent with a barrier function for glycoconjugates in the molecular layer.

Animals↗
PubMed1997

Influence of partial replacement of butter fat with peanut oil (in infant formula) on erythrocyte fatty acids in infants.

Erythrocyte fatty acid composition was studied in infants fed with three different formulae: formula I containing 20% butter fat; formula II containing 10% butter fat and 10% peanut oil; and formula III containing 10% butter fat and 5% peanut oil with a fat content itself reduced to 15%. The linoleic acid levels were 2.5, 18 and 13% in formula I-III, respectively. Analysis of fatty acids at the time of birth, and 3 and 6 months thereafter, indicated that linoleic acid levels could be improved by supplementation with peanut oil. Arachidonic acid levels (20:4, n-6) did not show a proportional relationship with respect to linoleic acid intake. The other ratio such as triene/tetraene, oleic/linoleic, linoleic/arachidonic and arachidonic/linoleic were all within the normal range, indicating normal desaturase and elongase activity. Thus, our present study suggests that peanut oils could be used for enhancing the linoleic acid levels in infants.

Arachis↗
PubMed2002

Nut and peanut butter consumption and risk of type 2 diabetes in women.

CONTEXT: Nuts are high in unsaturated (polyunsaturated and monounsaturated) fat and other nutrients that may improve glucose and insulin homeostasis. OBJECTIVE: To examine prospectively the relationship between nut consumption and risk of type 2 diabetes. DESIGN, SETTING, AND PARTICIPANTS: Prospective cohort study of 83 818 women from 11 states in the Nurses' Health Study. The women were aged 34 to 59 years, had no history of diabetes, cardiovascular disease, or cancer, completed a validated dietary questionnaire at baseline in 1980, and were followed up for 16 years. MAIN OUTCOME MEASURE: Incident cases of type 2 diabetes. RESULTS: We documented 3206 new cases of type 2 diabetes. Nut consumption was inversely associated with risk of type 2 diabetes after adjustment for age, body mass index (BMI), family history of diabetes, physical activity, smoking, alcohol use, and total energy intake. The multivariate relative risks (RRs) across categories of nut consumption (never/almost never, or =5 times/week) for a 28-g (1 oz) serving size were 1.0, 0.92 (95% confidence interval [CI], 0.85-1.00), 0.84 (0.95% CI, 0.76-0.93), and 0.73 (95% CI, 0.60-0.89) (P for trend <.001). Further adjustment for intakes of dietary fats, cereal fiber, and other dietary factors did not appreciably change the results. The inverse association persisted within strata defined by levels of BMI, smoking, alcohol use, and other diabetes risk factors. Consumption of peanut butter was also inversely associated with type 2 diabetes. The multivariate RR was 0.79 (95% CI, 0.68-0.91; P for trend <.001) in women consuming peanut butter 5 times or more a week (equivalent to > or =140 g [5 oz] of peanuts/week) compared with those who never/almost never ate peanut butter. CONCLUSIONS: Our findings suggest potential benefits of higher nut and peanut butter consumption in lowering risk of type 2 diabetes in women. To avoid increasing caloric intake, regular nut consumption can be recommended as a replacement for consumption of refined grain products or red or processed meats.

Adult↗
PubMed2005

Proteolytic processing of the peanut allergen Ara h 3.

The allergen Ara h 3 has been purified recently from peanuts. In contrast to recombinant Ara h 3, a 60 kDa single-chain polypeptide, the allergen isolated from its native source is extensively proteolytically processed. The characteristic proteolytic processing for 11S plant storage proteins of the glycinin family is observed for Ara h 3 yielding an acidic and a basic subunit, bound by a disulfide bridge. In addition to this, proteolytic truncation is observed for the acidic subunit but not for the basic subunit of Ara h 3. A series of Ara h 3 polypeptides ranging from 13-45 kDa was separated by sodium dodecylsulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and each band was digested by trypsin. Peptides related to the bands were identified and a scheme positioning the different polypeptides in the Ara h 3 sequence has been constructed. Peptide analysis showed sequence heterogeneity at two positions indicating the presence of multiple genes encoding variant, but highly homologous Ara h 3 proteins. The pool of Ara h 3 polypeptides from its native source illustrated that allergen from the peanut is much more complex than the recombinant protein used for epitope mapping experiments. From several Ara h 3 truncation products one or more immunoglobulin E (IgE) binding sites had been removed. Characterization of the allergenicity of Ara h 3 should therefore also include IgE-binding studies with peanut-derived Ara h 3, providing the high degree of variation in the Ara h 3 protein structure, as this is what peanut-allergic individuals are confronted with.

Allergens↗
PubMed1999

Changes in auxin patterns in developing gynophores of the peanut plant (Arachis hypogaea L.).

The peanut plant (Arachis hypogaea L.) produces flowers aerially, but buries the recently fertilized ovules in the soil in order for the fruit and seeds to mature underground. The organ that carries the seeds into the soil is called the gynophore. The growth of the peanut gynophore is regulated primarily by indole-3-acetic acid (IAA). A monoclonal antibody raised against IAA was used to successfully detect and localize this growth substance in the tissues of developing peanut gynophores. Five different stages of development were analysed: (1) before fertilization; (2) after fertilization; (3) during downwards growth; (4) at soil penetration; and (5) at the early stages of fruit formation. While no auxin signal is visible in the unfertilized ovules and ovary region, an asymmetric signal is observed in the gynophore wall after fertilization. During downwards growth, the auxin signal is located in both the meristematic region and in the area encircling the seeds, as well as in the cortex and epidermis region of the elongation zone. Upon soil penetration, the auxin signal in the meristematic region disappears, and most of the signal is detected in the gynophore wall near the tip. At the early stages of peanut fruit development, auxin signal is found at the lowermost area of the bending fruit, which eventually causes the fruit to be positioned horizontally. The results of this study suggest that the possible source of auxin within the gynophore may be the area of the gynophore wall close to the tip.

Arachis↗
PubMed1996

Characterization of two class II chitinase genes from peanut and expression studies in transgenic tobacco plants.

Two different genes encoding class II chitinases from peanut (Arachis hypogaea L. cv. NC4), A.h.Chi2;1 and A.h.Chi2;2, have been cloned. In peanut cell suspension cultures, mRNA levels of A.h.Chi2;2 increased after ethylene or salicylate treatment and in the presence of conidia from Botrytis cinerea. The second gene, A.h.Chi2;1, was only expressed after treatment with the fungal spores. Transgenic tobacco plants containing the complete peanut A.h.Chi2;1 gene exhibited essentially the same expression pattern in leaves as observed in peanut cell cultures. Expression characteristics of transgenic tobacco carrying a promoter-GUS fusion of A.h.Chi2;1 are described.

Amino Acid Sequence↗
PubMed1984

Effect of soil temperature and drought on peanut pod and stem temperatures relative to Aspergillus flavus invasion and aflatoxin contamination.

Peanut stem and pod temperatures of plants growing in irrigated, drought, drought-heated soil, and drought-cooled soil treatments were determined near the end of the growing season. Mean soil temperatures of the treatments during this period were 21.5 degrees, 25.5 degrees, 30 degrees and 20 degrees C, respectively. Peanut stem temperatures in all drought treatments reached a maximum of ca. 40 degrees C and for 6-7 h each day were as much as 10 degrees C warmer than irrigated peanut stems. Pod temperatures in drought-heated soil and drought treatments were ca. 34 degrees C and 30 degrees C, respectively, for several hours each day. As pod temperatures approached the optimum for A. flavus growth (ca. 35 degrees C), the proportion of kernels colonized and aflatoxin concentrations increased. Increased plant temperature without accompanying pod temperature increases (drought-cooled soil) resulted in colonization percentages and aflatoxin concentrations only slightly higher than those of the irrigated peanuts.

Aflatoxins↗