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PubMed1990

Behavioral sensitization to beta-phenylethylamine (PEA): enduring modifications of specific dopaminergic neuron systems in the rat.

Repeated daily administration of an endogenous trace amine, beta-phenylethylamine (PEA), produces behavioral sensitization such that the intensity of PEA-induced stereotyped behaviors in rats increases gradually during the treatment, and a challenge injection with PEA reinstates the enhanced stereotypy even long after withdrawal. In the present study, we examined the neurochemical changes in the central dopaminergic neurons systems in the rat for 7 drug-free days after repeated treatment with PEA (50 mg/kg, IP day for 14 or 28 days). During withdrawal, a decrease in steady-state levels of tissue dopamine (DA) and its metabolite, dihydroxyphenylacetic acid (DOPAC), was found in the mesolimbic DA nerve terminal areas of the rat brain receiving repeated PEA treatment. Fifteen minutes after challenge administration of PEA at varying doses from 6.3 to 75 mg/kg, the rats with repeated PEA treatment required smaller doses of PEA challenge than the rats with acute PEA treatment in order to obtain a significant decrease in striatal DOPAC content compared to the saline control in each treatment group. These results imply that the behavioral sensitization to PEA is accompanied by enduring modifications of the specific dopaminergic neuron systems in the rat brain. This suggestion was strongly supported by the results of the study using in vivo intracerebral dialysis, which indicated that 25 mg/kg PEA challenge elicited a remarkable increase in the extracellular DA concentrations in striatal perfusates collected from the PEA-pretreated rats, in accordance with the intensity of stereotyped behaviors. These findings argue that the hyper-responsiveness to PEA of the striatal dopaminergic neuron systems persists long after withdrawal from repeated treatment with PEA.

3,4-Dihydroxyphenylacetic Acid↗

PubMed1997

Correct blue-light regulation of pea Lhcb genes in an Arabidopsis background.

Irradiation of etiolated Arabidopsis or pea, or dim-red-light-grown pea seedling with a single, short (under 10 s) pulse of blue light (threshold at 0.1 mumol/m2) is sufficient to induce the expression of specific members of the Lhcb gene family including the pea Lhcb1*4 gene and the Arabidopsis Lhcb1*3 gene. Other Lhcb genes, such as the pea Lhcb1*3 gene and the Arabidopsis Lhcb1*1 and 1*2 genes are unaffected by this blue-light treatment. Transgenic Arabidopsis bearing pea Lhcb1*3::Gus (beta-glucuronidase), pea Lhcb1*4::Gus or Arabidopsis Lhcb1*3::Gus constructs were used to determine if pea and Arabidopsis employ a similar mechanism to achieve blue-light induced Lhcb expression. Examination of the respective Gus expression patterns in white-light-grown seedlings indicates that the pea promoters are active and properly expressed in the Arabidopsis background. Irradiation of dark-grown Arabidopsis with a 20 s pulse of blue light with a total fluence of 100 mumol/m-2 results in expression of the pea Lhcb1*4::Gus (beta-glucuronidase) construct, but not of the pea Lhcb1*3::Gus construct indicating that the pea promoters respond correctly to blue light in the Arabidopsis background. Fluence-response, time-course and reciprocity characteristics for the blue-light-induced expression of the pea Lhcb1*4::Gus construct closely resemble those of the endogenous Arabidopsis Lhcb genes, confirming the proper interpretation of the Arabidopsis blue-light-signaling mechanism by the pea Lhcb1*4 promoter and suggesting that the signaling mechanisms in the two plants are very similar, if not identical. Fluence response data for the steady-state level of transcript derived from an Arabidopsis Lhcb1*3::Gus construct extending 200 bp upstream of the site of transcription indicate that the blue light responsive elements(s) are contained within this 200 bp region.

Arabidopsis↗

PubMed2003

RSK2 activity is regulated by its interaction with PEA-15.

The ERK MAP (mitogen-activated protein) kinase cascade modulates many cellular processes including transcription, adhesion, growth, survival, and proliferation. One target substrate of ERK involved in regulating transcription is the p90 ribosomal S6 kinase (RSK) isozyme, RSK2. Here we demonstrate that a small death effector domain-containing protein called PEA-15 binds RSK2. RSK2 and PEA-15 (phosphoprotein enriched in astrocytes, 15 kDa) co-precipitated from cells and were colocalized in the cytoplasm. Furthermore, purified PEA-15 bound in vitro translated RSK2, suggesting that these proteins interact directly. PEA-15 does not bind to RSK1 and therefore exhibits some binding specificity. RSK2 binds the COOH terminus of PEA-15 and does not interact with its NH2-terminal death effector domain. We show that this interaction has functional consequences including the inhibition of RSK2-dependent CREB transcription. PEA-15 expression also blocks histone H3 phosphorylation, an RSK2-dependent event that may contribute to effects on gene expression. These results can be attributed to two effects of PEA-15 on RSK2. First, PEA-15 blocks nuclear accumulation of RSK2 after epidermal growth factor stimulation. Second, PEA-15 inhibits RSK2 kinase activity by 50%. A mutant of PEA-15 that binds RSK2 but is localized to the nucleus had no effect on RSK2-dependent transcription. Interestingly, this mutant also did not affect RSK2 kinase activity. This may indicate that cytoplasmic retention of RSK2 is also required for PEA-15 to impair kinase activity. PEA-15 does not alter ERK phosphorylation of RSK2 and is not itself a substrate of RSK2. Hence the effects of PEA-15 on RSK2 represent a novel mechanism for the regulation of RSK2-mediated signaling.

Animals↗

PubMed1995

The effect of heat on amino acids for growing pigs. 4. Nitrogen balance and urine, serum and plasma composition of growing pigs fed on raw or heat-treated field peas (Pisum sativum).

Experiments were conducted to determine the effect of heating field peas (Pisum sativum) on the N balance and urine, serum and plasma composition of growing pigs. In the first experiment, four diets containing raw field peas (cv. Wirrega) or field peas heated to 150 degrees (cv. Wirrega), 165 degrees (cv. Wirrega) or 150 degrees (cv. Dundale) for 15 min respectively were formulated to contain 1.15 g ileal digestible N/MJ digestible energy (DE) and 0.36 g ileal digestible lysine/MJ DE in a sugar-based diet. Digestibility estimates were based on those for the Dundale cultivar of field peas used in previous experiments. Total urine and faeces collection from eight pigs was conducted over two 7 d collection periods with a 7 d diet change-over period. Serial blood sampling from the external jugular vein was conducted on the final day of each collection period. There was no significant difference (P > 0.05) in the N balance or apparent biological value of the field-pea treatments. Pigs fed on diets containing peas heated to 150 degrees (cv. Wirrega) or 165 degrees (cv. Wirrega) had a significantly lower (P < 0.01) daily output of urea and uric acid in the urine, and depressed serum protein and serum urea concentrations. Plasma lysine concentration and daily urine lysine output were not significantly different (P > 0.05) in pigs fed on heated peas. Protein excretion in the urine of pigs fed on diets containing peas heated to 165 degrees increased 3-7 times (depending on estimation technique) the level observed in pigs fed on diets containing raw peas. A second experiment was conducted to determine the apparent ileal digestibility of N and amino acids in cv. Wirrega field peas. This study revealed that N digestibility (0.44) and lysine digestibility (0.35) in peas heated to 165 degrees were significantly lower than the cv. Dundale estimates (0.57 and 0.62 respectively) used in diet formulations. The depressed serum and urine variables in pigs fed on heated peas were attributed to overestimation of digestibility. The results exemplify the fact that it is not possible to draw general conclusions as to the effects of heat on any particular protein concentrate. Variability in N balance experiments and problems associated with urine analysis are suggested as likely reasons for the current study not reflecting poor utilization of ileal digestible lysine from heat-treated field peas.(ABSTRACT TRUNCATED AT 400 WORDS)

Amino Acids↗

PubMed2004

Arthropod diversity in peas with normal or reduced waxy bloom.

Crop traits can alter economically important interactions between plants, pests, and biological control agents. For example, a reduced waxy bloom on the surface of pea plants alters interactions between pea aphids and their natural enemies. In this study, we assess whether the effect of wax reduction extends beyond the 2 or 3 arthropod species closely associated with the plants and into the structure of the broader arthropod community of over 200 taxa at our site. We sampled arthropods on lines of peas with normal and reduced wax in Latah Co., Idaho using pitfall traps within randomly assigned pairs of 5 x 5 meter plots. During the 1998 and 1999 growing seasons, we collected 12,113 individual arthropods from 221 unambiguously identified morphospecies. The number of individuals collected from each morphospecies responded idiosyncratically to the reduced wax peas. To test whether arthropod community structure differed between the collections from plots having peas with normal or reduced wax, we performed a randomization test. The collection from peas with reduced wax had higher species evenness and thus higher community diversity despite having lower species richness. Our results demonstrate the potential of a single plant trait, epicuticular wax, to affect a community of arthropods. Two pests of peas had opposite responses to peas with reduced wax. The number of pea aphids collected was greater from peas with normal wax peas than those with reduced wax. In contrast, the number of pea leaf weevils collected was greater from peas with reduced wax.

Animals↗

PubMed2004

The expression of PEA-15 (phosphoprotein enriched in astrocytes of 15 kDa) defines subpopulations of astrocytes and neurons throughout the adult mouse brain.

Phosphoprotein enriched in astrocytes of 15 kDa (PEA-15) is an abundant phosphoprotein in primary cultures of mouse brain astrocytes. Its capability to interact with members of the apoptotic and mitogen activated protein (MAP) kinase cascades endows PEA-15 with anti-apoptotic and anti-proliferative properties. We analyzed the in vivo cellular sources of PEA-15 in the normal adult mouse brain using a novel polyclonal antibody. Immunohistochemical assays revealed numerous PEA-15-immunoreactive cells throughout the brain of wild-type adult mice while no immunoreactive signal was observed in the brain of PEA-15 -/- mice. Cell morphology and double immunofluorescent staining showed that both astrocytes and neurons could be cellular sources of PEA-15. Closer examination revealed that in a given area only part of the astrocytes expressed the protein. The hippocampus was the most striking example of this heterogeneity, a spatial segregation restricting PEA-15 positive astrocytes to the CA1 and CA3 regions. A PEA-15 immunoreactive signal was also observed in a few cells within the subventricular zone and the rostral migratory stream. In vivo analysis of an eventual PEA-15 regulation in astrocytes was performed using a model of astrogliosis occurring along motor neurons degeneration, the transgenic mouse expressing the mutant G93A human superoxyde-dismutase-1, a model of amyotrophic lateral sclerosis. We observed a marked up-regulation of PEA-15 in reactive astrocytes that had developed throughout the ventral horn of the lumbar spinal cord of the transgenic mice. The heterogeneous cellular expression of the protein and its increased expression in pathological situations, combined with the known properties of PEA-15, suggest that PEA-15 expression is associated with a particular metabolic status of cells challenged with potentially apoptotic and/or proliferative signals.

3T3 Cells↗

PubMed1994

The effect of heat on amino acids for growing pigs. 2. Utilization of ileal-digestible lysine from heat-treated field peas (Pisum sativum cultivar Dundale).

Two growth experiments were conducted to determine the effect of heat on the utilization of ileal-digestible lysine from field peas (Pisum sativum cultivar Dundale) fed to growing pigs. Five lysine-deficient diets (0.36 g ileal-digestible lysine/MJ digestible energy (DE)) were formulated using raw field peas, and field peas heated to either 110 degrees, 135 degrees, 150 degrees, or 165 degrees for 15 min respectively in a forced-air dehydrator. Additional diets were formulated with supplements of free lysine to verify that lysine was limiting in the diets containing the raw peas, and peas heated to 150 degrees or 165 degrees. The growth performance and retention of ileal-digestible lysine by pigs given the diets was determined over the 20-45 kg growth phase. Heat had a significant quadratic effect (P < 0.01) on growth rate, with responses declining from 543 g/d with pigs given the raw peas, to 407 g/d for those given the peas heated to 165 degrees. Similarly, crude protein deposition declined in a quadratic manner (P < 0.001) from 76 to 36 g/d for pigs fed on raw peas and peas heated to 165 degrees respectively. Retention of ileal-digestible lysine was 0.85 in the pigs given the raw field peas and declined in a quadratic manner (P < 0.001) with the application of heat to 0.48 in those pigs given the peas heated to 165 degrees. Pigs fed on field peas heated to 165 degrees had increased (P < 0.05) liver weights. The results indicate that heat applied to protein concentrates, even at mild temperatures, renders lysine in a form that is apparently absorbed but inefficiently utilized by the growing pig. Consequently, ileal digestibility values for lysine in heat-processed meals are unsuitable for diet formulations.

Amino Acids↗

PubMed1987

Digestion of starch and fibre carbohydrates in peas by adult cockerels.

The digestion of starch and fibre by adult cockerels fed peas which were whole, ground, autoclaved, heated, dehulled, cooked or supplemented with a cellulose degrading enzyme was studied. The starch in ground peas that had been autoclaved, heated or dehulled was slightly, though not significantly, better digested than the starch in peas that had been ground only. Feeding peas whole greatly reduced starch digestibility. Cooking failed to improve starch digestibility as retrograded starch produced in the cooking process was not digested. The more finely ground the foodstuff, the better the in vitro enzymatic hydrolysis of starch. Starch digestibility correlated well (r2 = 0.80) with the true metabolisable energy values obtained for the different pea treatments. In experiment 1 cockerels digested on average 0.22 of the pea fibre from the different forms of peas. A significant decrease in xylose digestion was observed when birds were fed dehulled peas, birds excreting more xylose than they ingested. In experiment 2, cockerels digested on average 0.38 of the pea fibre from different forms of peas. A reduction in fibre digestion was observed when birds were fed cooked peas as a consequence of a decreased digestibility of all monosaccharide residues. A slight increase in fibre digestion was observed when peas were augmented with 'cellulase', entirely because of an increase in xylose digestion.

Animals↗

PubMed1999

Expression of the insecticidal bean alpha-amylase inhibitor transgene has minimal detrimental effect on the nutritional value of peas fed to rats at 30% of the diet.

The effect of expression of bean alpha-amylase inhibitor (alpha-AI) transgene on the nutritional value of peas has been evaluated by pair-feeding rats diets containing transgenic or parent peas at 300 and 650 g/kg, respectively, and at 150 g protein/kg diet, supplemented with essential amino acids to target requirements. The results were also compared with the effects of diets containing lactalbumin with or without 0.9 or 2.0 mg bean alpha-AI, levels equivalent to those in transgenic pea diets. When 300 and 650 g peas/kg diet were fed, the daily intake of alpha-AI was 11.5 or 26.3 mg alpha-AI, respectively. At the 300 g/kg level, the nutritional value of the transgenic and parent line peas was not significantly different. The weight gain and tissue weights of rats fed either of the two pea diets were not significantly different from each other or from those of rats given the lactalbumin diet even when this was supplemented with 0.9 g alpha-AI/kg. The digestibilities of protein and dry matter of the pea diets were slightly but significantly lower than those of the lactalbumin diet, probably due to the presence of naturally occurring antinutrients in peas. The nutritional value of diets containing peas at the higher (650 g) inclusion level was less than that of the lactalbumin diet. However, the differences between transgenic and parent pea lines were small, possibly because neither the purified recombinant alpha-AI nor that in transgenic peas inhibited starch digestion in the rat small intestine in vivo to the same extent as did bean alpha-AI. This was the case even though both forms of alpha-AI equally inhibited alpha-amylase in vitro. Thus, this short-term study indicated that transgenic peas expressing bean alpha-AI gene could be used in rat diets at 300 g/kg level without major harmful effects on their growth, metabolism and health, raising the possibility that transgenic peas may also be used at this level in the diet of farm animals.

Animals↗

PubMed2004

Assessment of the feeding value of South Dakota-grown field peas (Pisum sativum l.) for growing pigs.

Four experiments were conducted to investigate the feeding value of South Dakota-grown field peas (Pisum sativum L.) for growing pigs. In Exp. 1, 96 pigs (initial BW = 22 +/- 3.35 kg) were allotted to four treatment groups (four pigs per pen, six replicate pens per treatment) and fed growing (0.95% Lys) and finishing (0.68% Lys) diets containing 0, 12, 24, or 36% field peas (as-fed basis). There were no differences among the treatment groups in ADG, ADFI, or G:F. Likewise, there were no differences in backfat thickness or lean meat percent among treatment groups, but pigs fed diets containing 12, 24, or 36% field peas had greater (P < 0.05) loin depths than pigs fed the control diet. In Exp. 2, 120 pigs (initial BW = 7.8 +/- 1.04 kg) were allotted to four treatment groups 2 wk after weaning. Pigs were then fed diets containing 0, 6, 12, or 18% field peas (as-fed basis) during the following 4 wk. There were five pigs per pen and six replicate pens per treatment. Results of the experiment showed no differences in ADG, ADFI, or G:F among treatment groups. In Exp. 3, apparent (AID) and standardized (SID) ileal digestibility coefficients of CP and AA in field peas and soybean meal were measured using six individually penned growing pigs (initial BW = 36.5 +/- 2.1 kg) arranged in a repeated 3 x 3 Latin square design. The AID for Met, Trp, Cys, and Ser, and the SID for Met, Trp, and Cys were lower (P < 0.05) in field peas than in soybean meal; but for CP and all other AA, no differences in AID or SID were observed between the two feed ingredients. Experiment 4 was an energy balance experiment conducted to measure the DE and ME concentrations in field peas and corn. Six growing pigs (initial BW = 85.5 +/- 6.5 kg) were placed in metabolism cages and fed diets based on field peas or corn and arranged in a two-period switch-back design. The DE values for field peas and corn (3,864 and 3,879 kcal/kg DM, respectively) were similar, but the ME of corn was higher (P < 0.05) than the ME of field peas (3,825 vs. 3,741 kcal ME/kg DM). The results from the current experiments demonstrate that the nutrients in South Dakota-grown field peas are highly digestible by growing pigs. Therefore, such field peas may be included in diets for nursery pigs and growing-finishing pigs in amounts of at least 18 and 36%, respectively, without negatively affecting pig performance.

Animal Feed↗

PubMed2001

Repellent effect of pea (Pisum sativum) fractions against stored-product insects.

Peas (Pisum sativum) are toxic to some stored-product insects. The repellent effect of fractions of pea seed to stored-product insects was evaluated in multiple-choice tests in which wheat kernels were dusted with fractions rich in either protein, fibre or starch at 0.001 to 10% (wt:wt). There was a negative correlation between pea protein concentration and the number of adults found in grain for Cryptolestes ferrugineus and Sitophilus oryzae, but not for Tribolium castaneum. Pea fibre repelled C. ferrugineus adults but not S. oryzae and T. castaneum. Pea starch did not repel any of the insects. One-week old and 6-week old C. ferrugineus were equally repelled by pea protein. Repellency was detectable 1h after exposure. Cryptolestes ferrugineus and S. oryzae did not become habituated to the repellent action of pea protein even after 4 weeks of exposure. Habituation was observed, however, when C. ferrugineus was exposed to pea fibre for 4 weeks. In a two-choice bioassay (0 vs. 0.1% and 0 vs. 1% pea protein), the pea-protein-treated grain had significantly fewer insects (C. ferrugineus, S. oryzae, Sitophilus zeamais, T. castaneum, and Tribolium confusum) than untreated grain. The properties of the pea protein fractions seem well suited for developing a natural stored grain protectant.

Journal Article↗

PubMed2001

Antioxidant systems and O(2)(.-)/H(2)O(2) production in the apoplast of pea leaves. Its relation with salt-induced necrotic lesions in minor veins.

The present work describes, for the first time, the changes that take place in the leaf apoplastic antioxidant defenses in response to NaCl stress in two pea (Pisum sativum) cultivars (cv Lincoln and cv Puget) showing different degrees of sensitivity to high NaCl concentrations. The results showed that only superoxide dismutase, and probably dehydroascorbate reductase (DHAR), were present in the leaf apoplastic space, whereas ascorbate (ASC) peroxidase, monodehydroascorbate reductase (MDHAR), and glutathione (GSH) reductase (GR) seemed to be absent. Both ASC and GSH were detected in the leaf apoplastic space and although their absolute levels did not change in response to salt stress, the ASC/dehydroascorbate and GSH to GSH oxidized form ratios decreased progressively with the severity of the stress. Apoplastic superoxide dismutase activity was induced in NaCl-treated pea cv Puget but decreased in NaCl-treated pea cv Lincoln. An increase in DHAR and GR and a decrease in ASC peroxidase, MDHAR, ASC, and GSH levels was observed in the symplast from NaCl-treated pea cv Lincoln, whereas in pea cv Puget an increase in DHAR, GR, and MDHAR occurred. The results suggest a strong interaction between both cell compartments in the control of the apoplastic ASC content in pea leaves. However, this anti-oxidative response does not seem to be sufficient to remove the harmful effects of high salinity. This finding is more evident in pea cv Lincoln, which is characterized by a greater inhibition of the growth response and by a higher rise in the apoplastic hydrogen peroxide content, O(2)(.-) production and thiobarbituric acid-reactive substances, and CO protein levels. This NaCl-induced oxidative stress in the apoplasts might be related to the appearance of highly localized O(2)(.-)/H(2)O(2)-induced necrotic lesions in the minor veins in NaCl-treated pea plants. It is possible that both the different anti-oxidative capacity and the NaCl-induced response in the apoplast and in the symplast from pea cv Puget in comparison with pea cv Lincoln contributes to a better protection of pea cv Puget against salt stress.

Adaptation, Physiological↗

PubMed1997

High-yield expression of pea thioredoxin m and assessment of its efficiency in chloroplast fructose-1,6-bisphosphatase activation.

A cDNA clone encoding pea (Pisum sativum L.) chloroplast thioredoxin (Trx) m and its transit peptide were isolated from a pea cDNA library. Its deduced amino acid sequence showed 70% homology with spinach (Spinacia oleracea L.) Trx m and 25% homology with Trx f from pea and spinach. After subcloning in the Ndel-BamHI sites of pET-12a, the recombinant supplied 20 mg Trx m/L. Escherichia coli culture. This protein had 108 amino acids and was 12,000 D, which is identical to the pea leaf native protein. Unlike pea Trx f, pea Trx m showed a hyperbolic saturation of pea chloroplast fructose-1,6-bisphosphatase (FBPase), with a Trx m/ FBPase molar saturation ratio of about 60, compared with 4 for the Trx f/FBPase quotient. Cross-experiments have shown the ability of pea Trx m to activate the spinach chloroplast FBPase, results that are in contrast with those in spinach found by P. Schürmann, K. Maeda, and A. Tsugita ([1981] Eur J Biochem 116: 37-45), who did not find Trx m efficiency in FBPase activation. This higher efficiency of pea Trx m could be related to the presence of four basic residues (arginine-37, lysine-70, arginine-74, and lysine-97) flanking the regulatory cluster; spinach Trx m lacks the positive charge corresponding to lysine-70 of pea Trx m. This has been confirmed by K70E mutagenesis of pea Trx m, which leads to a 50% decrease in FBPase activation.

Amino Acid Sequence↗

PubMed1992

Molecular characterization of a pea beta-1,3-glucanase induced by Fusarium solani and chitosan challenge.

beta-glucanases are prominent proteins in pea endocarp tissue responding to fungal infection. We have cloned and sequenced a partial pea cDNA clone, pPIG312, corresponding to a beta-1,3-glucanase in pea pods challenged with the incompatible pathogen Fusarium solani f. sp. phaseoli. The insert from the partial pea cDNA was used to probe a genomic library derived from pea leaves of the same cultivar. One of the genomic clones, pPIG4-3, contained the complete coding sequence for a mature beta-1,3-glucanase protein. The predicted amino acid sequence of the pea beta-1,3-glucanase has 78% identity to bean beta-1,3-glucanase, 62% and 60% to two tobacco beta-1,3-glucanases, 57% to soybean beta-1,3-glucanase, 51% to barley beta-1,3-glucanase, and 48% to barley beta-1,3-1,4-glucanase. Genomic Southern analysis indicates that the pea genome contains only one beta-1,3-glucanase gene corresponding to the probe used in this study. Accumulation of beta-1,3-glucanase mRNA homologous with the pPIG312 probe was detected in pea pods within 4 to 8 h after challenge with F. solani f. sp. phaseoli, f. sp. pisi, a compatible strain, or the elicitor, chitosan. In the incompatible reaction, mRNA accumulation remained high for 48h, whereas it rapidly decreased in the compatible reaction. After fungal inoculation of whole pea seedlings, the enhanced mRNA accumulation occurred mainly in the basal region (lower stem and root). This beta-1,3-glucanase mRNA was constitutively expressed in the roots of pea seedlings.(ABSTRACT TRUNCATED AT 250 WORDS)

Amino Acid Sequence↗

PubMed1980

Effects of 2-(2-pyridyl)ethylamine (PEA) on the isolated guinea-pig heart.

The effect of 2-(2-pyridyl)ethylamine (PEA) on the rate and force of contraction of cardiac tissues from untreated and reserpine-pretreated guinea-pigs was examined. PEA produced changes in rate of spontaneously beating right atria without activation of H1 or H2-receptors. The positive chronotropic effect of PEA was eliminated when atria from reserpine-pretreated animals were used, indicating an entirely indirect mode of action of PEA in the right atrium. The positive inotropic effect of low doses of PEA in left atria was antagonized by promethazine, whereas the inotropic effect of higher doses of PEA was reduced either by propranolol or following reserpine pretreatment. In the right ventricle strip, the inotropic effect of high doses of PEA was blocked equally by propranolol and promethazine. The results obtained indicate that in the guinea-pig heart, PEA either produces it effects through catecholamine release (right atrium) or through a combination of both H1-receptor stimulation and catecholamine release (left atrium and right ventricle strip). The direct inotropic effects of PEA produced only small increases in force of contraction. The study indicates that caution should be used in ascribing all of the effects of PEA to histamine receptor stimulation.

Animals↗

PubMed2005

Phosphorylation of PEA-15 switches its binding specificity from ERK/MAPK to FADD.

Cell signalling pathways that regulate proliferation and those that regulate programmed cell death (apoptosis) are co-ordinated. The proteins and mechanisms that mediate the integration of these pathways are not yet fully described. The phosphoprotein PEA-15 (phosphoprotein enriched in astrocytes) can regulate both the ERK (extracellular-signal-regulated kinase)/MAPK (mitogen-activated protein kinase) pathway and the death receptor-initiated apoptosis pathway. This is the result of PEA-15 binding to the ERK/MAPK or the proapoptotic protein FADD (Fas-activated death domain protein) respectively. The mechanism by which binding of PEA-15 to these proteins is controlled has not been elucidated. PEA-15 is a phosphoprotein containing a Ser-104 phosphorylated by protein kinase C and a Ser-116 phosphorylated by CamKII (calcium/calmodulin-dependent protein kinase II) or AKT. Phosphorylation of Ser-104 is implicated in the regulation of glucose metabolism, while phosphorylation at Ser-116 is required for PEA-15 recruitment to the DISC (death-initiation signalling complex). Moreover, PEA-15 must be phosphorylated at Ser-116 to inhibit apoptosis. In the present study, we report that phosphorylation at Ser-104 blocks ERK binding to PEA-15 in vitro and in vivo, whereas phosphorylation at Ser-116 promotes its binding to FADD. We further characterize phospho-epitope-binding antibodies to these sites. We report that phosphorylation does not influence the distribution of PEA-15 between the cytoplasm and nucleus of the cell since all phosphorylated states are found predominantly in the cytoplasm. We propose that phosphorylation of PEA-15 acts as the switch that controls whether PEA-15 influences proliferation or apoptosis.

Adaptor Proteins, Signal Transducing↗

PubMed2000

Regulation of expression of phospholipase D1 and D2 by PEA-15, a novel protein that interacts with them.

Phospholipase D (PLD), a signal-transducing membrane-associated enzyme, is implicated in diverse processes including apoptosis, ERK activation, and glucose transport. Prior studies have identified specific PLD activators and repressors that directly regulate its enzymatic activity. Using two-hybrid screens, we have identified PEA-15 as a PLD interactor that unexpectedly functions to alter its level of expression. PEA-15 is a widely expressed death effector domain-containing phosphoprotein involved in signal transduction, apoptosis, ERK activation, and glucose transport. The PLD1-interacting site on PEA-15 consists of part of the death effector domain domain plus additional C-terminal flanking sequences, whereas the PEA-15-interacting site on PLD1 overlaps the previously identified RhoA-interacting site. PEA-15 did not affect basal or stimulated in vitro PLD1 enzymatic activation. However, co-expression of PEA-15 increased levels of PLD1 activity. This increased activation correlated with higher PLD1 protein expression levels, as marked by faster accumulation and longer persistence of PLD1 when PEA-15 was present. PEA-15 similarly increased protein expressions level of PLD2 and co-immunoprecipitated with it. These results suggest that PEA-15 may stabilize PLD or act as a PLD chaperone. The common involvement of PEA-15 and PLD in apoptosis, ERK activation, and glucose transport additionally suggests functional significance.

Alleles↗

PubMed2005

Variation in precaecal amino acid and energy digestibility between pea (Pisum sativum) cultivars determined using a linear regression approach.

An experiment was conducted to study the variation in the precaecal amino acid (AA) and energy digestibility of 4 cultivars of white-flowering peas (Pisum sativum) for broiler chickens. The 4 cultivars were grown and harvested under the same agronomic and environmental conditions. One basal diet and 8 diets including each pea cultivar at inclusion rates of either 150 or 300 g/kg were used. Peas were included at the expense of starch. Hence, the differences in dietary crude protein and AA concentrations resulted only from the inclusion of peas. Titanium dioxide was included as an indigestible marker. Crude protein concentrations in the complete diets ranged from 164 to 244 g/kg. All diets were fed ad libitum to broiler chickens between 14 and 21 d of age. Seven pens of 12 chickens were allocated to each treatment. Digesta were sampled on a pen basis from the section of the gastrointestinal tract between Meckel's diverticulum and 2 cm anterior to the ileo-caeco-colonic junction. The proportions of crude protein and AAs digested responded linearly to increased intake and the relationships between quantitative intake and digested amounts of AAs were described by multiple linear regressions. The slope determined for each pea cultivar was taken as a measure of AA digestibility without the need for consideration of basal endogenous crude protein and AA secretions. Digestibility of AAs in peas ranged from 0.60 to 0.91. One cultivar had significantly lower AA digestibilities than the other three cultivars. This could be explained neither by the trypsin inhibitor activity nor by tannin levels. The AAs with the highest digestibilities in all cultivars were arginine > glutamic acid > lysine > methionine > phenylalanine > leucine. The AAs with the consistently lowest digestibilities were cystine < threonine. The ranking of the remaining AAs varied slightly between cultivars. The multiple linear regression approach is suitable to study differences in AA digestibilities without the need for consideration of basal endogenous AA losses. Diets containing 300 g/kg of peas had significantly lower energy digestibilities than the pea-free basal diet. The pea cultivar with the lowest AA digestibility caused the lowest energy digestibility at both levels of pea inclusion.

Amino Acids↗