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PubMed1998

Endothelin induces a calcium-dependent phosphorylation of PEA-15 in intact astrocytes: identification of Ser104 and Ser116 phosphorylated, respectively, by protein kinase C and calcium/calmodulin kinase II in vitro.

PEA-15 (phosphoprotein enriched in astrocytes, Mr = 15,000) is an acidic serine-phosphorylated protein highly expressed in the CNS, where it can play a protective role against cytokine-induced apoptosis. PEA-15 is a major substrate for protein kinase C. Endothelins, which are known to exert pleiotropic effects on astrocytes, were used to analyze further the processes involved in PEA-15 phosphorylation. Endothelin-1 or endothelin-3 (0.1 microM) induced a robust phosphorylation of PEA-15 that was abolished by the removal of extracellular calcium, but only diminished by inhibitors of protein kinase C. Microsequencing of phosphopeptides generated by digestion of PEA-15 following endothelin-1 treatment identified two phosphorylated residues: Ser104, previously recognized as the protein kinase C site, and a novel phosphoserine, Ser116, located in a consensus motif for either protein kinase casein kinase II or calcium/calmodulin-dependent protein kinase II (CaMKII). Partly purified PEA-15 was a substrate in vitro for CaMKII, but not for casein kinase II. Two-dimensional phosphopeptide mapping demonstrated that the site phosphorylated in vitro by CaMKII was also phosphorylated in intact astrocytes in response to endothelin. CaMKII phosphorylated selectively Ser116 and had no effect on Ser104, but in vitro phosphorylation by CaMKII appeared to facilitate further phosphorylation by protein kinase C. Treatment of intact astrocytes with okadaic acid enhanced the phosphorylation of the CaMKII site. These results demonstrate that PEA-15 is phosphorylated in astrocytes by CaMKII (or a related kinase) and by protein kinase C in response to endothelin.

Amino Acid Sequence↗

PubMed1986

Efficient in vitro import of a cytosolic heat shock protein into pea chloroplasts.

In order to further our understanding of the targeting of nuclear-encoded proteins into intracellular organelles, we have investigated the import of chimeric precursor proteins into pea chloroplasts. Two different chimeric precursor proteins were produced by in vitro expression of chimeric genes. One chimeric precursor contained the transit peptide of the small subunit of soybean ribulose 1,5-bisphosphate carboxylase and the mature peptide of the same protein from pea. The second contained the same transit peptide plus 13 amino acids of the pea mature peptide fused to a cytosolic heat shock protein. The extent of import and binding of the two chimeric proteins was examined by using quantitative assays and was compared to the import of pea small subunit precursor. Both precursor proteins imported well into pea chloroplasts, although the extent of import observed with the chimeric small-subunit-heat shock precursor was less than that observed with the soybean-pea small subunit precursor. The heat shock protein alone did not import into nor bind to chloroplasts. The binding of both the chimeric small-subunit-heat shock protein and the soybean-pea small subunit precursor to chloroplasts was physiologically significant, as shown by the fact that when chloroplasts with bound precursors were isolated, these bound precursors could subsequently be imported.

Journal Article↗

PubMed1994

The effect of heat on amino acids for growing pigs. 1. A comparison of ileal and faecal digestibilities of amino acids in raw and heat-treated field peas (Pisum sativum cultivar Dundale).

Three experiments were conducted to examine the effect of heating field peas (Pisum sativum cultivar Dundale) on (1) proximate analysis and total amino acid composition, (2) ileal and faecal digestibilities of amino acids, and (3) digestible energy content. Alternative techniques for assessing ileal and faecal digestibilities and digestible energy respectively, were also investigated. Forced-air dehydrators were used to heat field peas at temperatures of 110 degrees, 135 degrees, 150 degrees or 165 degrees. In the first experiment the apparent ileal and faecal digestibilities of amino acids and the faecal digestibility of energy in the raw and heated field peas were determined using pigs fitted with 'T'-shaped cannulas. In the second, apparent ileal digestibility of amino acids and the faecal digestibility of energy were determined using the direct ileal and rectal sampling technique. This involved a single collection of digesta and faeces from the digestive tract of the pig while it was anaesthetized. The faecal digestibilities of amino acids and energy were determined using total faeces collection in the third experiment. In all experiments the respective field-pea treatments comprised 400 g/kg sugar-based diets and were the only source of amino acids. Heat significantly decreased the lysine (14.6-8.7 g/kg; P < 0.001), cystine (3.2-2.6 g/kg; P < 0.01) and arginine (16.7-14.5 g/kg; P < 0.05) contents of the heated peas. The 'reactive' lysine content of the field peas, as measured using the Silcock technique, was decreased by 0.11 and 0.30 with the application of heat at 150 degrees and 165 degrees respectively. Heat treatments did not alter the ileal digestibility of most amino acids. Only aspartic acid (0.72-0.58), glutamic acid (0.80-0.65) and the basic amino acids, lysine (0.79-0.56) and arginine (0.85-0.75), showed a significant linear decrease (P < 0.05) in ileal digestibility over the heat treatments, determined using the ileal cannulation procedure. Heating significantly (P < 0.05) decreased faecal digestibility for all amino acids. Faecal digestibility was consistently greater than ileal digestibility for the raw field peas; however, this difference decreased with heat application until faecal digestibility was equal or less than ileal digestibility at the 165 degrees treatment. Heat linearly depressed digestible energy, diet dry-matter digestibility and diet energy digestibility. Losses in lysine, cystine and arginine are likely to be due to early and advanced Maillard reactions. Considerable binding of the remaining lysine also occurred as indicated by a decline in Silcock-reactive lysine.(ABSTRACT TRUNCATED AT 400 WORDS)

Amino Acids↗

PubMed1987

Effect of pelleting and associations with maize or wheat on the nutritive value of smooth pea (Pisum sativum) seeds in adult cockerels.

Four types of diet were tested: 960 g maize/kg (M), 960 g wheat/kg (W), 463 g maize added to 497 g of smooth peas/kg (PM) and 463 g wheat added to 497 g smooth peas/kg (PW). Three treatments were applied to each of these 4 diets: grinding (OP), one steam pelleting (1 P) and two successive steam pelleting (2 P). The pelleted diets were ground before feeding. Adult cockerels received all the diets whereas rats received only W and PW diets. Apparent metabolisable energy values corrected for N-equilibrium (AMEn), protein and starch digestibilities were measured in adult cockerels. Digestible energy (DE) values were measured in rats. The AMEn values of cereals remained practically unchanged by pelleting, whereas that of smooth peas was increased by between 1.8-4.6% after pelleting. Pelleting also induced 3.5 and 5.4% increases respectively in the digestibilities of pea protein and starch. Pelleting did not change the DE values measured in rats. The AMEn values of smooth peas mixed with maize were 4.6% higher than those of smooth peas mixed with wheat. The true digestibility of pea protein was 8.4% higher in the former mixture, whereas the pea starch digestibility remained unchanged. Calculation showed that most of the pea AMEn variations could be explained in terms of variations in protein and starch digestibilities.

Animal Feed↗

PubMed2002

Production of 13C labelled pea flour for use in human digestion and fermentation studies.

Stable isotope breath tests offer a new approach to the study of digestion and fermentation of carbohydrates in man. In this study, 13C labelled peas were grown by pulsing 250 ml 13CO2 into a sealed growth chamber. A second pulse was added to a portion of the peas to increase the 13C enrichment. This generated pea flour with an enrichment of 2.36 at.% excess (range 2.09-2.71 n = 3) and 8.64 atom % excess (range 7.37-9.78 n = 3) respectively. This represented incorporation of an absolute yield of 3.8% of the 13CO2 into peas in the 'once-labelled' treatment and 7.5% in the 'twice-labelled' treatment. Ingestion of a mixture of the labelled pea flour (300 mg) by two volunteers generated measurable 13CO2 excretion for breath test analysis. The profile of breath 13CO2 enrichment increased to a maximum within three hours after consuming the pea flour followed by a decrease almost back to baseline by 13 hours. Breath 13CO2 appeared to rise again after this apparent nadir at 13 hours until the end of the sampling period. Mathematical analysis of the data suggested that two peaks best described the profile of breath 13CO2 up to 13 hours. A third peak was necessary to describe the late rise in breath 13CO2 enrichment. This use of 13C enriched pea flour may provide a useful non invasive method for measurement of digestion and fermentation in vivo.

Adult↗

PubMed2006

Akt down-regulates ERK1/2 nuclear localization and angiotensin II-induced cell proliferation through PEA-15.

Angiotensin II (AngII) type 1 receptors (AT1) regulate cell growth through the extracellular signal-regulated kinase (ERK)1/2 and phosphatidylinositol 3-kinase (PI3K) pathways. ERK1/2 and Akt/protein kinase B, downstream of PI3K, are independently activated but both required for mediating AngII-induced proliferation when expressed at endogenous levels. We investigate the effect of an increase in the expression of wild-type Akt1 by using Chinese hamster ovary (CHO)-AT1 cells. Unexpectedly, Akt overexpression inhibits the AT1-mediated proliferation. This effect could be generated by a cross-talk between the PI3K and ERK1/2 pathways. A functional partner is the phosphoprotein enriched in astrocytes of 15 kDa (PEA-15), an Akt substrate known to bind ERK1/2 and to regulate their nuclear translocation. We report that Akt binds to PEA-15 and that Akt activation leads to PEA-15 stabilization, independently of PEA-15 interaction with ERK1/2. Akt cross-talk with PEA-15 does not affect ERK1/2 activation but decreases their nuclear activity as a result of the blockade of ERK1/2 nuclear accumulation. In response to AngII, PEA-15 overexpression displays the same functional consequences on ERK1/2 signaling as Akt overactivation. Thus, Akt overactivation prevents the nuclear translocation of ERK1/2 and the AngII-induced proliferation through interaction with and stabilization of endogenous PEA-15.

Angiotensin II↗

PubMed2006

Effects of hydrophilic and hydrophobic kaolin-based particle films on pea aphid (Homoptera: Aphididae) and its entomopathogen Pandora neoaphidis (Entomophthorales: Entomophthoraceae).

Hydrophobic and hydrophilic kaolin-based particle films are effective for control of insect pests in certain agricultural crops. How these products interact with potential biological control agents is not well documented. This study was conducted to evaluate the effects of the hydrophobic (M96-018) and hydrophilic (Surround WP) kaolin-based particle films (Engelhard Corporation, Iselin, NJ) on pea aphid, Acyrthosiphon pisum (Harris), on peas (Pisum spp.), and on the fungal aphid pathogen Pandora neoaphidis (Remaudière and Hennebert) Humber. Over two field seasons (2001 and 2002) in northern Idaho, applications of M96-018 significantly reduced the rate of pea aphid increase on pea, but Surround WP, tested only in 2001, did not reduce aphid population growth rate. Neither particle film treatment was as effective as a standard application of esfenvalerate (DuPont Asana). In the laboratory, particle films suppressed pea aphid populations by up to 30%. M96-018 seemed to have some repellent activity based on aphid distributions after treating plants. When applied along with P. neoaphidis conidia, M96-018 but not Surround WP caused higher percentage of infection mortality of pea aphids by P. neoaphidis than occurred on controls treated only with P. neoaphidis conidia. P. neoaphidis conidia deposited on glass slides coated with M96-018, produced more germ tubes and secondary conidia than those deposited on untreated glass slides or slides treated with Surround WP. This result suggests that greater infection of pea aphids on plants treated with M96-018 is in part a result of a direct enhancement of fungal germination by the particle film.

Analysis of Variance↗

PubMed2000

Heterologous rhizobial lipochitin oligosaccharides and chitin oligomers induce cortical cell divisions in red clover roots, transformed with the pea lectin gene.

Division of cortical cells in roots of leguminous plants is triggered by lipochitin oligosaccharides (LCOs) secreted by the rhizobial microsymbiont. Previously, we have shown that presence of pea lectin in transgenic white clover hairy roots renders these roots susceptible to induction of root nodule formation by pea-specific rhizobia (C. L. Díaz, L. S. Melchers, P. J. J. Hooykaas, B. J. J. Lugtenberg, and J. W. Kijne, Nature 338:579-581, 1989). Here, we report that pea lectin-transformed red clover hairy roots form nodule primordium-like structures after inoculation with pea-, alfalfa-, and Lotus-specific rhizobia, which normally do not nodulate red clover. External application of a broad range of purified LCOs showed all of them to be active in induction of cortical cell divisions and cell expansion in a radial direction, resulting in formation of structures that resemble nodule primordia induced by clover-specific rhizobia. This activity was obvious in about 50% of the red clover plants carrying hairy roots transformed with the pea lectin gene. Also, chitopentaose, chitotetraose, chitotriose, and chitobiose were able to induce cortical cell divisions and cell expansion in a radial direction in transgenic roots, but not in control roots. Sugar-binding activity of pea lectin was essential for its effect. These results show that transformation of red clover roots with pea lectin results in a broadened response of legume root cortical cells to externally applied potentially mitogenic oligochitin signals.

Cell Division↗

PubMed1983

Influence of adenosine phosphates and magnesium on photosynthesis in chloroplasts from peas, sedum, and spinach.

(14)CO(2) photoassimilation in the presence of MgATP, MgADP, and MgAMP was investigated using intact chloroplasts from Sedum praealtum, a Crassulacean acid metabolism plant, and two C(3) plants: spinach and peas. Inasmuch as free ATP, ADP, AMP, and uncomplexed Mg(2+) were present in the assays, their influence upon CO(2) assimilation was also examined. Free Mg(2+) was inhibitory with all chloroplasts, as were ADP and AMP in chloroplasts from Sedum and peas. With Sedum chloroplasts in the presence of ADP, the time course of assimilation was linear. However, with pea chloroplasts, ADP inhibition became progressively more severe, resulting in a curved time course. ATP stimulated assimilation only in pea chloroplasts. MgATP and MgADP stimulated assimilation in all chloroplasts. ADP inhibition of CO(2) assimilation was maximal at optimum orthophosphate concentrations in Sedum chloroplasts, while MgATP stimulation was maximal at optimum or below optimum concentrations of orthophosphate. MgATP stimulation in peas and Sedum and ADP inhibition in Sedum were not sensitive to the addition of glycerate 3-phosphate (PGA).PGA-supported O(2) evolution by pea chloroplasts was not inhibited immediately by ADP; the rate of O(2) evolution slowed as time passed, corresponding to the effect of ADP on CO(2) assimilation, and indicating that glycerate 3-phosphate kinase was a site of inhibition. Likewise, upon the addition of AMP, inhibition of PGA-dependent O(2) evolution became more severe with time. This did not mirror CO(2) assimilation, which was inhibited immediately by AMP. In Sedum chloroplasts, PGA-dependent O(2) evolution was not inhibited by ADP and AMP. In chloroplasts from peas and Sedum, the magnitude of MgADP and MgATP stimulation of PGA-dependent O(2) evolution was not much larger than that given by ATP, and it was much smaller than MgATP stimulation of CO(2) assimilation. Analysis of stromal metabolite levels by anion exchange chromatography indicated that ribulose 1,5-bisphosphate carboxylase was inhibited by ADP and stimulated by MgADP in Sedum chloroplasts.The appearance of label in the medium was measured when [U-(14)C] ADP-loaded Sedum chloroplasts were challenged with ATP, ADP, or AMP and their Mg(2+) complexes. The rate of back exchange was stimulated by the presence of Mg(2+). This suggests that ATP, ADP, and AMP penetrate the chloroplast slower than their Mg(2+) complexes. A portion of the CO(2) assimilation and O(2) evolution data could be explained by differential penetration rates, and other proposals were made to explain the remainder of the observations.

Journal Article↗

PubMed1990

Purification and Characterization of Pea Epicotyl beta-Amylase.

The most abundant beta-amylase (EC 3.2.1.2) in pea (Pisum sativum L.) was purified greater than 880-fold from epicotyls of etiolated germinating seedlings by anion exchange and gel filtration chromatography, glycogen precipitation, and preparative electrophoresis. The electrophoretic mobility and relative abundance of this beta-amylase are the same as that of an exoamylase previously reported to be primarily vacuolar. The enzyme was determined to be a beta-amylase by end product analysis and by its inability to hydrolyze beta-limit dextrin and to release dye from starch azure. Pea beta-amylase is an approximate 55 to 57 kilodalton monomer with a pl of 4.35, a pH optimum of 6.0 (soluble starch substrate), an Arrhenius energy of activation of 6.28 kilocalories per mole, and a K(m) of 1.67 milligrams per milliliter (soluble starch). The enzyme is strongly inhibited by heavy metals, p-chloromer-curiphenylsulfonic acid and N-ethylmaleimide, but much less strongly by iodoacetamide and iodoacetic acid, indicating cysteinyl sulfhydryls are not directly involved in catalysis. Pea beta-amylase is competitively inhibited by its end product, maltose, with a K(i) of 11.5 millimolar. The enzyme is partially inhibited by Schardinger maltodextrins, with alpha-cyclohexaamylose being a stronger inhibitor than beta-cycloheptaamylose. Moderately branched glucans (e.g. amylopectin) were better substrates for pea beta-amylase than less branched or non-branched (amyloses) or highly branched (glycogens) glucans. The enzyme failed to hydrolyze native starch grains from pea and glucans smaller than maltotetraose. The mechanism of pea beta-amylase is the multichain type. Possible roles of pea beta-amylase in cellular glucan metabolism are discussed.

Journal Article↗

PubMed1994

Comparison of electric and growth responses to excision in cucumber and pea seedlings. I. Short-distance effects are a result of wounding.

The local electric response to stem excision in both pea epicotyls and cucumber hypocotyls is a depolarization of the cells in the wound area. If we define wound area as the region of local depolarization, we find that it extends for approximately 10 mm from the cut or wound site in pea epicotyls, whereas it can reach up to 40 mm in cucumber hypocotyls. The wound-induced depolarization in pea cells is transient, reaching its maximal amplitude within 1-2 min, whereas in cucumber cells this depolarization is more sustained. A third difference between wound responses in pea and cucumber is the intermittent appearance of spikes, i.e. very short, rapidly reverted depolarizations which frequently accompany the basic depolarization in cucumber but not in pea cells. These spikes can propagate in both directions along the hypocotyl axis. The cause of the different responses of pea and cucumber cells is unknown. A possible explanation might be found in different degrees of electrical cell coupling in the two species. This possibility was investigated in cucumber hypocotyls by measuring the cell input resistance (R(in)) of epidermal cells at various axial distances from the cut. Shorter distances increase the likelihood of shunting the cell membrane resistance through the shortened symplastic path to the cut surface. With a series of cuts made at decreasing distances from the measured site, cell depolarization increased without comparable changes in R(in). Two conclusions were drawn. Firstly, wound-induced depolarizations are not brought about by shunting of the cell resistance in the wound area. Secondly, the depolarization is probably not carried by ion channels but may be caused by an inhibition of proton pump activity. Parallel to its depolarization effect on the membrane potential, excision led to a severe and sustained decline in the cucumber hypocotyl growth rate only when carried out sufficiently close to the growing region (45 mm from the hook). Similar excision in pea epicotyls failed to change the growth rate. Both electrical and growth data support the concept that the high and sustained responsiveness of cucumber seedlings to wounding is caused by a particular sensitivity of their proton pump mechanism.

Cell Polarity↗

PubMed2005

Neurolathyrism risk depends on type of grass pea preparation and on mixing with cereals and antioxidants.

OBJECTIVE: To study an array of household individual and dietary risk factors for neurolathyrism. METHOD: Case-control study using recent cases in a district highly affected by the recent neurolathyrism epidemic in Ethiopia: 108 households with cases and 104 households with no cases; 170 neurolathyrism cases, 370 intra-family controls and 170 community controls frequency matched for age and sex. RESULTS: A history of acute illness was associated with a two- and threefold increased risk of paralysis in community and intra-family controls, respectively. Soaking grass pea in water before cooking roughly halved the risk of neurolathyrism but cooking in clay utensils more than quadrupled it. Consumption of grass pea in the green unripe and boiled forms increased the risk 10 times or more. Mixing the food with gravy that contains condiments with antioxidant activity reduced it by a factor of 4. The consumption of grass pea mixed with cereals rich in sulphur amino acids was also highly protective, but the magnitude of the effect depended on the grass pea preparation consumed. CONCLUSION: Consumption of pure grass pea, especially in the green unripe and boiled forms, should be avoided. Communities at risk of neurolathyrism during famine crises should be encouraged to combine and use grass pea with cereals before the household cereal stock is fully depleted. Breeding programmes, alongside traditional attempts to reduce the toxin content, should enhance the content of sulphur amino acids and antioxidants in grass pea.

Adolescent↗

PubMed1990

Intraorganelle localization and substrate specificities of the mitochondrial acyl-CoA: sn-glycerol-3-phosphate O-acyltransferase and acyl-CoA: 1-acyl-sn-glycerol-3-phosphate O-acyltransferase from potato tubers and pea leaves.

The mitochondrial sn-glycerol-3-phosphate and 1-acyl-sn-glycerol-3-phosphate O-acyltransferases from potato tubers and pea leaves were investigated with respect to their intraorganelle localization, their positional and substrate specificities, and their fatty acid selectivities. In mitochondria from potato tubers both enzymes were found to be located in the outer membrane. The 1-acyl-sn-glycerol-3-phosphate O-acyltransferase of pea mitochondria showed the same intraorganelle localization whereas the sn-glycerol-3-phosphate O-acyltransferase behaved like a soluble protein of the intermembrane space. The sn-glycerol-3-phosphate O-acyltransferase of both potato and pea mitochondria used sn-glycerol-3-phosphate but not dihydroxyacetone phosphate as acyl acceptor and exclusively catalyzed the formation of 1-acyl-sn-glycerol-3-phosphate which subsequently served as substrate for the second acylation reaction at its C-2 position. Both acyltransferases of potato as well as pea mitochondria showed higher activities with acyl-CoA than with the corresponding acyl-(acyl carrier protein) thioesters. When different acyl-CoA thioesters were offered separately, the sn-glycerol-3-phosphate O-acyltransferase of potato mitochondria displayed no fatty acid specificity whereas the enzyme of pea mitochondria revealed one for saturated acyl groups. On the other hand, the mitochondrial 1-acyl-sn-glycerol-3-phosphate O-acyltransferases from both potato tubers and pea leaves were more active on unsaturated than on saturated acyl-CoA thioesters. Furthermore, these enzymes preferentially used oleoyl- and linoleoyl-CoA when they were offered in a mixture with saturated ones, although the fatty acid selectivity of the pea enzyme was less pronounced than that of the potato enzyme. The sn-glycerol-3-phosphate O-acyltransferase of potato mitochondria displayed a slight preference for saturated acyl groups.

1-Acylglycerol-3-Phosphate O-Acyltransferase↗

PubMed1998

Peak endocardial acceleration-based clinical testing of the "BEST" DDDR pacemaker. European PEA Clinical Investigation Group.

The peak endocardial acceleration (PEA, unit g) shows a near correlation with myocardial contractility during the isometric systolic contraction of the heart (dP/dtmax), with sympathetic activity and, thus, with physiological heart rate modulation. The (Biomechanical Endocardial Sorin Transducer (BEST) sensor is incorporated in the tip of a pacing lead and measures PEA directly near the myocardium. In an international study, the lead was implanted with the dual chamber pacemaker Living-1 (Sorin) in 105 patients. The behavior of the PEA signal was tested under conditions of physical and mental stress and during daily life activities by 24-hour recordings of PEA (PEA Holter) at 1 to 2 months and approximately 1 year after implantation. Implantation of the BEST lead was performed without complications in all patients. The sensor functioned properly in the short- and long-term in 98% of patients. Although PEA values differed from patient to patient, the values closely reflected the variations in sympathetic activity due to physical and mental stress in each patient. During exercise and during daily life activities a close correlation between PEA and heart rate was observed among patients with normal sinus rhythm. Peak endocardial acceleration allows a nearly physiological control of the pacing rate.

Activities of Daily Living↗

PubMed1998

Dual chamber rate responsive pacing system driven by contractility: final assessment after 1-year follow-up. The European PEA Clinical Investigation Group.

The aim of this study was to assess the long-term performance of a new dual chamber rate responsive pacing system based on the dynamic measurement of the peak endocardial acceleration (PEA) index of cardiac contractility. Seventy patients who participated in the Multicenter European Clinical Evaluation were studied 1 year after implantation by continuously recording the PEA and the heart rate (HR) during exercise stress testing and during 24 hours of usual activities. A complete examination of standard parameters was also performed to assess the pacing/sensing lead characteristics. Statistical comparisons were performed with the data recorded with the same protocol at 1 month after implant for each patient. A linear correlation coefficient was calculated between PEA and sinus rate when the patient showed predominant atrial tracked rhythm. There were no significant differences between PEA values measured at 1 month and 1 year (PEA = 0.41 +/- 0.26 g vs 0.45 +/- 0.29 g at rest and PEA = 1.63 +/- 0.77 g vs 1.72 +/- 0.83 g during peak exercise). The correlation coefficient remained stable (0.67 +/- 0.15 vs 0.65 +/- 0.14 during daily life and 0.74 +/- 0.14 vs 0.77 +/- 0.11 during exercise). The PEA signal detected by the sensor was reliable and stable. No long-term complications or adverse effects were observed, and the lead performance was comparable to that of a standard lead.

Activities of Daily Living↗

PubMed2000

Specific IgE levels to Cicer arietinum (Chick pea) in tolerant and nontolerant children: evaluation of boiled and raw extracts.

The chick pea, Cicer arietinum, is a legume commonly consumed in Spain and other Mediterranean countries. The sera of 29 children (mean age: 8.4 years) with a current or past history of allergic reactions after ingestion of chick pea, and positive skin tests to this legume, were used to study the allergenic composition of raw and boiled chick pea extracts. The patient population was divided into 2 groups: group 1 consisted of 19 patients with clinical sensitivity confirmed by either positive oral challenges or a convincing recent history of anaphylaxis after eating chick peas, and group 2 consisted of 10 patients with clinical sensitivity in the past, but tolerant at the time of blood extraction. Six atopic children, not allergic to legumes, were included as controls. Specific IgE to the raw and boiled extracts was measured by ELISA. The allergenic composition of both extracts was analyzed by SDS-PAGE and immunoblots. There were no significant differences between specific IgE levels to the raw and boiled extracts (p = 0.23). The mean levels in group 1 were significantly higher than in group 2 and controls (p = 0.0001). Multiple IgE binding proteins/peptides were detected in both extracts in the molecular weight range of 10-106 kD. Only nontolerant patients recognized a similar number of bands in both extracts. Chick pea extracts contain a majority of heat-stable allergens, which could be responsible for the clinical sensitivity to chick pea. Patients with a current clinical allergy to chick pea have statistically higher specific IgE levels than tolerant patients and controls.

Adolescent↗

PubMed2006

Effects of phytoestrogen extracts isolated from rye, green and yellow pea seeds on hormone production and proliferation of trophoblast tumor cells Jeg3.

BACKGROUND: Phytoestrogens are a diverse group of non-steroidal plant compounds. Because they have chemical structures similar to estrogens they are able to bind on estrogen receptors in humans. OBJECTIVES: In this study, we tested the effects of crude phytoestrogen extracts from rye (Secale cereale), green pea (Pisum sativum) and yellow pea seeds (Pisum sativum cv.) on cell proliferation and the production of progesterone in trophoblast tumor cells of the cell line Jeg3. METHODS: Isoflavone extracts from green and yellow pea seeds and lignan extracts from rye seeds were obtained, using different extraction methods. Isolated extracts were incubated in different concentrations with trophoblast tumor cells. Untreated cells were used as controls. At designated times, aliquots were removed and tested for estradiol and progesterone production. In addition, we tested the effects of the phytoestrogen extracts on cell proliferation. RESULTS: Cell proliferation is significantly inhibited by potential phytoestrogens isolated from rye, green and yellow pea seeds in trophoblast tumor cells of the cell line Jeg3. We found a correlation between the effects of proliferation and production of estradiol in isoflavone extracts from green and yellow pea seeds in Jeg3 cells. In addition, higher concentrations of isoflavones isolated from green pea seeds and lignans from rye showed also a inhibition of progesterone production whereas higher concentrations of rye lignans elevated estradiol production in Jeg3 cells. CONCLUSION: A useful indicator test system for potential phytoestrogens could be established. Based on the obtained results it is proposed that green and yellow pea seeds contain measurable concentrations of isoflavones and rye seeds contain lignans which can be isolated and used for special human diet programs.

Cell Line, Tumor↗

PubMed1992

Evaluation of pearl millet and field peas plus triticale silages for midlactation dairy cows.

A mixture of field peas and triticale was planted in spring, harvested as silage, and followed by a double crop of pearl millet, which also was harvested as silage. Eighteen Holstein cows were fed diets based on pea with triticale, pearl millet, or alfalfa plus corn silages. Dry matter digestibility of the pea with triticale diet was higher than for control (71.1 vs. 66.9%), but DM digestibility was not different between control and pearl millet diets. Milk production was not affected by diets containing pea with triticale or pearl millet compared with control diets (25.2, 23.2, and 24.5 kg/d). Cows fed pea with triticale produced milk with a higher concentration of fat (4.59 vs. 3.35%) and more FCM (27.3 vs. 22.1 kg/d) than those fed the control diet. However, cows fed the control diet gained more BW than those receiving pea with triticale or pearl millet diets. Partitioning of energy between body stores and milk production was different between cows fed pea with triticale and control diets; however, total energy use was not different (32.4 vs. 30.5 Mcal of NE(L)/d). Differences in energy partitioning may have been caused partly by differences in ruminal fermentation of the respective diets.

Animal Feed↗