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At least 631 records · Page 35Linked to original sources
PubMed2000

Recombinant carboxyltransferase responsive to redox of pea plastidic acetyl-CoA carboxylase.

Acetyl-CoA carboxylase regulates the rate of fatty acid synthesis. This enzyme in plants is localized in plastids and is believed to be composed of biotin carboxyl carrier protein, biotin carboxylase, and carboxyltransferase made up of alpha and beta polypeptides, although the enzyme has not been purified yet. Accumulated evidence shows that pea plastidic acetyl-CoA carboxylase is activated by light and the activation is caused by light-dependent reduction of carboxyltransferase, but not of biotin carboxylase, via a redox cascade. To understand the reductive activation of carboxyltransferase at the molecular level here, we obtained the active enzyme composed of decahistidine-tagged (His tag) alpha and beta polypeptides through the expression of the pea plastidic carboxyltransferase gene in Escherichia coli. Gel filtration showed that the molecular size of the recombinant carboxyltransferase is in agreement with that of partially purified carboxyltransferase from pea chloroplasts. The catalytic activity of the recombinant enzyme was similar to that of native carboxyltransferase. These results indicate that the molecular structure and conformation of recombinant carboxyltransferase resemble those of its native counterpart and that native carboxyltransferase is indeed composed of alpha and beta polypeptides. This recombinant enzyme was activated by dithiothreitol, a known reductant of S-S bonds, with a profile similar to that of its native counterpart. The recombinant enzyme was activated by reduced thioredoxin-f, a signal transducer of redox potential in chloroplasts under irradiation. Thus, this enzyme was redox-regulated, like that of the native carboxyltransferase.

Acetyl-CoA Carboxylase↗
PubMed2001

Basic calcium phosphate crystals induce matrix metalloproteinase-1 through the Ras/mitogen-activated protein kinase/c-Fos/AP-1/metalloproteinase 1 pathway. Involvement of transcription factor binding sites AP-1 and PEA-3.

Synovial fluid basic calcium phosphate (BCP) crystals are common in osteoarthritis and are associated with severe degenerative arthropathy. Besides stimulating synovial fibroblast-like cells to proliferate, BCP crystals are a potent inducer of human matrix metalloproteinases (hMMPs), which can speed up the articular joint tissue degeneration of osteoarthritis patients. Here, we report that transfections with hMMP1 luciferase reporter plasmids in fibroblast-like synoviocytes revealed that the induction of hMMP1 promoter by BCP crystals was mainly mediated through the -72AP-1 element. Elimination of the -72AP-1 element either by mutation or deletion abolished the induction of hMMP1 promoter activity by BCP crystals almost completely. Interestingly, a mutation at the -88PEA-3 site also abolished the induction of hMMP1 promoter. Further mutation at the -181AP-1 site resumed the induction, indicating that the -181AP-1 element had an effect opposite to the -72AP-1 element. The effect of -181AP-1 could be inactivated either by a mutation at this -181AP-1 site or by the -88PEA-3 element. In addition, dominant negative Ras, Raf, and MEK1/2 could block the induction of hMMP1, and a MEK1/2-specific inhibitor (UO126) could block the induction of hMMP1 and c-Fos by BCP crystals. Taken together, these data indicate that multiple elements, including at least AP-1 and PEA-3, are involved in the induction of hMMP1 gene expression by BCP crystals and that the induction follows the Ras/MAPK/c-Fos/AP-1/MMP1 signaling pathway.

Animals↗
PubMed2004

PEA-15 is inhibited by adenovirus E1A and plays a role in ERK nuclear export and Ras-induced senescence.

Oncogenic ras activates multiple signaling pathways to enforce cell proliferation in tumor cells. The ERK1/2 mitogen-activated protein kinase pathway is required for the transforming effects of ras, and its activation is often sufficient to convey mitogenic stimulation. However, in some settings oncogenic ras triggers a permanent cell cycle arrest with features of cellular senescence. How the Ras/ERK1/2 pathway activates different cellular programs is not well understood. Here we show that ERK1/2 localize predominantly in the cytoplasm during ras-induced senescence. This cytoplasmic localization seems to be dependent on an active nuclear export mechanism and can be rescued by the viral oncoprotein E1A. Consistent with this hypothesis, we showed that E1A dramatically down-regulated the expression of the ERK1/2 nuclear export factor PEA-15. Also, RNA interference against PEA-15 restored the nuclear localization of phospho-ERK1/2 in Ras-expressing primary murine embryo fibroblasts and stimulated their escape from senescence. Because senescence prevents the transforming effect of oncogenic ras, our results suggest a tumor suppressor function for PEA-15 that operates by means of controlling the localization of phospho-ERK1/2.

Active Transport, Cell Nucleus↗
PubMed2005

The importance of antennae for pea aphid wing induction in the presence of natural enemies.

The pea aphid Acyrthosiphon pisum Harris has been shown to produce an increasing proportion of winged morphs among its offspring when exposed to natural enemies, in particular hoverfly larvae, lacewing larvae, adult and larval ladybirds and aphidiid parasitoids. While these results suggest that wing induction in the presence of predators and parasitoids is a general response of the pea aphid, the cues and mechanisms underlying this response are still unclear. Tactile stimuli and the perception of chemical signals as well as visual signals are candidates for suitable cues in the presence of natural enemies. In this paper the hypothesis that the aphids' antennae are crucial for the wing induction in the presence of natural enemies is tested. Antennae of pea aphids were ablated and morph production was scored when aphids were reared either in the presence or the absence of predatory lacewing larvae over a six-day period. Ablation of antennae resulted in a drastic drop in the proportion of winged morphs among the offspring, both in the presence and the absence of a predator whereas predator presence increased wing induction in aphids with intact antennae, as reported in previous experiments. The results show that antennae are necessary for wing induction in the presence of natural enemies. Critical re-examination of early work on the importance of aphid antennae and tactile stimuli for wing induction suggests that a combination of tactile and chemical cues is likely to be involved not only in predator-induced wing formation but also for wing induction in response to factors such as crowding in the aphid colony.

Analysis of Variance↗
PubMed1996

Does chronic supplementation of the diet with dietary fibre extracted from pea or carrot affect colonic motility in man?

The aim of the present study was to assess, in healthy volunteers and under physiological conditions, the acceptability, clinical tolerance and effects on colonic motility of chronic supplementation of the usual diet with new dietary fibre sources. Three studies were carried out, one after a period of habitual diet, and two after randomized 3-week periods of supplementation with fibre extracted either from pea hulls or carrots, added to the meals as a fine powder. The 24 h motility was recorded on an unprepared colon at five levels to determine the initiation site and the number of high amplitude propagated contractions (HAPC) and to quantify motor activity every 30 min, particularly in the two periods following lunch and breakfast. With the habitual diet the motility pattern was an irregular alternation of quiescence and sporadic non-propagated contractions. HAPC always started from the ascending colon and occurred mainly after breakfast. With either type of fibre the 24 h motor profiles, the 24 h variations and the number of HAPC were not significantly modified but a more distal initiation of HAPC was found. The colonic postprandial motor response was more diffuse after dietary enrichment with carrot fibre than after enrichment with pea-hull fibre. In healthy volunteers the long-term addition of fibre extracted from pea hulls and carrots to the usual diet was easy and well-tolerated without clinical side-effects, but with limited colonic motor effects. However, the more distal initiation of HAPC observed could be deleterious.

Adult↗
PubMed1990

Test for linkage between the eumelanin dilution blue (B1), the extended black (E) allele at the E-locus and the linked pea comb (P) and eumelanin extension (M1) genes in the domestic fowl.

1. A mating was made between a Blue Andalusian bantam male and a pea comb striped necked bantam female to produce a quadruple heterozygote of the linked pea comb (P) and eumelanin extension (Ml) genes and of the eunmelanin dilution blue (Bl) gene and the extended black (E) allele at the E-locus. 2. Two pea comb blue females so produced were mated to a single comb striped necked bantam male, thus providing a backcross to the quadruple recessive. 3. Bl segregated independently with each of the other three genes whilst 25 crossovers occurred amongst the 55 progeny assessed for linkage between P and Ml, confirming loose linkage between P and Ml which had previously been shown to be approximately 46 units. Linkage of 0.3% had been previously reported (Crawford, 1986) between P and a "melanotic" gene isolated from a segregating gene pool. Evidence is presented to demonstrate that two different "melanotic" genes were being considered, thus explaining the apparently contradictory reports. Charcoal (cha) is suggested for the recessive gene linked with P by 0.3%. 4. Thirty-four crossovers occurred among the 97 progeny between P and E suggesting linkage of approximately 35 units. A further mating was made from among segregants in the backcross which confirmed P-E linkage with 17 crossovers in 55 gametes. Combining the tests produced a linkage value of approximately 34 units.

Alleles↗
PubMed2005

In vitro intestinal transport and antihypertensive activity of ACE inhibitory pea and whey digests.

Angiotensin I converting enzyme (ACE) inhibitory peptides cause an antihypertensive effect if they reach the systemic circulation. This was investigated for the high ACE inhibitory activity present in peas and whey in vitro gastrointestinal digests. The samples retained high ACE inhibitory activity when incubated in Caco-2 homogenates or rat intestinal acetone powder, both sources of small intestine peptidases. Only little ACE inhibitory activity was transported through Caco-2 cell monolayers in 1 h. As the Caco-2 model is tighter than intestinal mammalian tissue, sufficient absorption of these peptides might occur in vivo. After intravenous administration of 50 mg protein kg(-1) BW in spontaneously hypertensive rats (SHR), pea digest exerted a transient, but strong antihypertensive effect of 44.4 mmHg. Whey digest exerted no effect at this dose. These results suggest that pea digest could be a promising source of ACE inhibitory peptides for use in the prevention and treatment of hypertension.

Acetone↗
PubMedDate not supplied

Structural modulation of calmodulin and calmodulin-dependent protein kinase II by pea protein hydrolysates.

The effects of two fractions of pea protein hydrolysate with high levels of positively charged amino acids on the structural conformations of calmodulin (CaM) and CaM-dependent protein kinase II (CaMKII) were determined using fluorescence and circular dichroism methods. In the presence of Ca2 + , addition of the protein hydrolysates to CaM and CaM/CaMKII complex led to increased exposure of aromatic groups as measured by intrinsic and extrinsic fluorescence spectroscopy. Near-UV circular dichroism data revealed an increase in the tertiary structure of CaM in the presence of pea protein hydrolysates. Effect of the protein hydrolysates on the CaM structure was greater with the fraction that contained higher contents of arginine and lysine when compared with the fraction with lower levels of these two amino acids. We concluded that the presence of the pea protein hydrolysates led to rearrangement of the native protein structure and exposure of buried hydrophobic groups of CaM and/or CaMKII.

Calcium-Calmodulin-Dependent Protein Kinase Type 2↗
PubMed2003

Peas-Mea1-Ppp2r5d overlapping gene complex: a transposon mediated-gene formation in mammals.

Human and mouse MEA1/Mea1 is flanked by two overlapping genes, a novel PEAS/Peas in a head-to-head orientation and PPP2R5D/Ppp2r5d in a tail-to-tail orientation making a Peas-Mea1-Ppp2r5d overlapping gene complex (PMP-complex). Genomic zoo blot analyses and database searching revealed that Mea1 exists only in mammals, while Peas and Ppp2r5d are conserved in eukaryotes. Mea1 and Peas are transcribed from a testis-expressed bidirectional promoter. Mea1-Ppp2r5d overlapping segment (MPOS) contains polyadenylation signals for both genes and shows marked conservation throughout mammals. Furthermore, the MPOS occupies 3'-region of transcripts of both genes is expected to form a clover-like intramolecular structure. Mouse genomic library Screening and database searches identified two MPOS-derived sequences in Odf2 gene and RP23-86H7 cosmid clone, respectively, in which MPOS might be a core segment for the retropositions. Thus, a key role of MPOS, a short transposable element containing polyadenylation signals on both strands, in the formation of the Mea1 during mammalian evolution is suggested.

Animals↗
PubMed2000

A plasma membrane-enriched fraction isolated from the coats of developing pea seeds contains H(+)-symporters for amino acids and sucrose.

Aqueous polymer two-phase partitioning was used to obtain a plasma membrane-enriched fraction from coats of developing pea (Pisum sativum L.) seeds in the filling stage. Uptake of amino acids and sucrose by vesicles from this fraction was determined after imposition of gradients of proton concentration (DeltapH, inside alkaline) and electrical potential (Deltapsi, inside negative) across the vesicle membrane. The uptake of sucrose and the amino acids L-valine, L-lysine, and L-glutamic acid was stimulated by the imposition of DeltapH. The imposition of Deltapsi, either in the presence or in the absence of DeltapH, stimulated the uptake of L-valine and L-lysine, but had no detectable effect on the uptake of sucrose and L-glutamic acid. The proton-motive-force-driven uptake of all four substrates was abolished by the protonophore carbonylcyanide m-chlorophenyl-hydrazone (CCCP). The results demonstrate the presence of H(+)-symporters for sucrose and amino acids in pea seed coats. This is running counter to the previously reported finding that their uptake by isolated pea seed coats was insensitive to CCCP, and that the uptake of sucrose, L-valine, and L-glutamic acid displayed linear kinetics. Possible causes of this discrepancy will be discussed.

Amino Acids↗
PubMed2001

Specific flavonoids induced nod gene expression and pre-activated nod genes of Rhizobium leguminosarum increased pea (Pisum sativum L.) and lentil (Lens culinaris L.) nodulation in controlled growth chamber environments.

The gram-negative soil bacteria Rhizobium spp. infect and establish a nitrogen-fixing symbiosis with legume crops which involves the mutual exchange of diffusable signal molecules. In this study, Rhizobium leguminosarum containing a nod-lacZ gene fusion was used to screen the most effective plant-to-bacteria signal molecules for pea and lentil and the induction conditions. Out of a number of signal compounds including apigenin, daidzein, genistein, hesperetin, kaempferol, luteolin, naringenin, and rutin, hesperetin and naringenin were found to be the most effective plant-to-bacteria signal molecules. The induction of nod genes was temperature-dependent, where nod gene induction was decreased with dropping incubation temperature. The combination of hesperetin at 7 microM and naringenin at 3 microM resulted in better induction of nod gene activities compared to either hesperetin or naringenin alone. Nodulation and plant dry matter accumulation of pea and lentil plants receiving preinduced R. leguminosarum were higher than those of plants receiving uninduced R. leguminosarum cells in controlled environment growth chamber conditions. Preinduced Rhizobium with hesperetin at a concentration of 10 microM increased nodule number on average by 60.5% and dry matter accumulation by 14% in field pea at 17 degrees C, while it was 32% and 9% at 24 degrees C, respectively. Similarly, averaged over two rhizobial strains, a 59% and 6% increase in nodule number and biomass production at 17 degrees C, and a 39% and 27% at 24 degrees C, were obtained from lentil inoculated with hesperetin-induced R. leguminosarum, respectively.

Environment, Controlled↗
PubMed2002

Regulation of pectic polysaccharide domains in relation to cell development and cell properties in the pea testa.

The occurrence of pectic polysaccharide epitopes in cells and tissues of the pea testa during late stages of seed development have been examined in relation to anatomy and cell properties. Homogalacturonan, in a highly methyl-esterified form, was present throughout late development in all pea testa cell walls, including the thickened cell walls of the outer macrosclereid layer. Two epitopes, characteristic of the side-chains of the rhamnogalacturonan-I domain of pectic polysaccharides, occurred in restricted and separate cell layers of the pea testa. A (1-->4)-beta-D-galactan epitope was restricted to regions of the outer cell wall of the testa and to inner regions of the macrosclereid layer at 20 DAA and was absent from the osteosclereid and parenchyma cell walls. By 25 DAA the (1-->4)-beta-D-galactan epitope occurred only in the outer epidermal cell walls. A (1-->5)-alpha-L-arabinan epitope was also dependent on the developmental stage of the seed and was found with greatest abundance in the walls of the inner parenchyma cells. Cell separation studies indicated that, although calcium cross-links were involved in the maintenance of the link between the macrosclereid layer and proximal cell layers, most cell-to-cell adhesion in the testa was not due to calcium- or ester-based bonds.

Antibodies, Monoclonal↗
PubMed2003

A Tudor protein with multiple SNc domains from pea seedlings: cellular localization, partial characterization, sequence analysis, and phylogenetic relationships.

A major high molecular weight protein (HMP) in the cytoskeletal fraction from pea has been purified. A combination of chromatographic techniques and protease fragment analysis also facilitated the isolation of the encoding cDNA, disclosing the sequence of the complete open reading frame. The protein possesses four complete N-terminal Staphylococcal nuclease (SNc) domains, a central Tudor domain and a partial SNc domain at the C-terminus, which may act as a coiled-coil cytoskeleton interaction motif. Cell fractionation studies showed that the protein was abundant in the cytoskeleton fraction in dark-grown pea seedlings, but essentially was absent from the nucleus. Gel filtration column chromatography indicated that the native protein exists as a dimer, while isoelectric focusing suggested that there were at least four HMP isotypes. The protein co-eluted with ribosomes from a heparin affinity column in vitro, consistent with ribosome/polysome interactions in vivo. Significantly, sequence analysis of the C-terminal SNc motif may accurately predict nuclear versus cytoplasmic localization resulting in potentially very different functional roles for this protein family in different organisms. An antibody to HMP from peas was also raised and an HMP with a similar molecular mass was detected in the cytoskeleton fractions and to a lesser extent in the nuclear fraction (250 g pellet) from rice and wheat seedlings.

Amino Acid Sequence↗
PubMed2004

Activity and protein level of AO isoforms in pea plants (Pisum sativum L.) during vegetative development and in response to stress conditions.

Among three AO isoforms detected in pea plants, the activity of PAO-1 was dominant in leaves of seedlings and young leaves of mature plants, while PAO-3 revealed the highest band intensity in old leaves and roots. PAO-1 and PAO-3 are homodimers consisting of 145 kDa and 140 kDa subunits, respectively, while PAO-2 is a heterodimer of one 145 kDa and one 140 kDa subunit. In leaves, the activity of PAO-1 disappeared gradually with leaf ageing, while in roots it was present only in seedlings but not in mature pea plants. PAO-3 could oxidize abscisic aldehyde, a precursor of abscisic acid, indicating the possible involvement of this isoform in ABA synthesis in pea. The ability of PAO-3 to oxidize abscisic aldehyde was higher in old leaves than in young ones and increased significantly both in roots and leaves of plants exposed to salinity and ammonium treatments. A marked increase of the AO protein level was observed after ammonium application but not under salinity. Interestingly, the activity of PAO isoforms may be transcriptionally and post-transcriptionally regulated during vegetative growth and in response to stress conditions, and such a regulation might be particularly important to adjust ABA levels to the recent requirements of the plant. The observations suggest that the AO isoforms have different metabolic roles and that the activity and protein level of each isoform is regulated not only by environmental conditions but also through plant developmental stages.

Abscisic Acid↗
PubMed2006

Antioxidative enzymes from chloroplasts, mitochondria, and peroxisomes during leaf senescence of nodulated pea plants.

In this work the influence of the nodulation of pea (Pisum sativum L.) plants on the oxidative metabolism of different leaf organelles from young and senescent plants was studied. Chloroplasts, mitochondria, and peroxisomes were purified from leaves of nitrate-fed and Rhizobium leguminosarum-nodulated pea plants at two developmental stages (young and senescent plants). In these cell organelles, the activity of the ascorbate-glutathione cycle enzymes ascorbate peroxidase (APX), monodehydroascorbate reductase (MDHAR), dehydroascorbate reductase (DHAR), and glutathione reductase (GR), and the ascorbate and glutathione contents were determined. In addition, the total superoxide dismutase (SOD) activity, the pattern of mitochondrial and peroxisomal NADPH-generating dehydrogenases, some of the peroxisomal photorespiratory enzymes, the glyoxylate cycle and oxidative metabolism enzymes were also analysed in these organelles. Results obtained on the metabolism of cell organelles indicate that nodulation with Rhizobium accelerates senescence in pea leaves. A considerable decrease of the ascorbate content of chloroplasts, mitochondria, and peroxisomes was found, and in these conditions a metabolic conversion of leaf peroxisomes into glyoxysomes, characteristic of leaf senescence, took place.

Aging↗
PubMed2006

Respiratory potential and Se compounds in pea (Pisum sativum L.) plants grown from Se-enriched seeds.

Selenium (Se) has been proved to be an essential element for humans and animals. However, less is known about its effects on plants. Pea plants were treated foliarly once (OT) and twice (TT) with Se solution during their flowering period. Seeds obtained from these plants contained 383 and 743 ng Se g(-1), respectively, and, together with control seeds from untreated plants (UT) containing 21 ng Se g(-1), were sown in soil in a greenhouse. Se content and its chemical form in young plants were studied, and its impact on plant respiratory potential, measured as terminal electron transport system (ETS) activity, determined. ETS activity was highest in young pea leaves with the highest Se content. Higher ETS activity possibly reflected increased glutathione peroxidase (GSH-Px) activity in mitochondria. The Se content of leaves and stems of plants grown from control seeds was similar to that in the seed, being around 40 ng Se g(-1). Se concentration in leaves of young plants grown from OT and TT seeds was 605%, and 1340% higher, respectively, than the control, and in their stems 355%, and 680% higher, respectively. The ratio of Se concentrations in OT and TT seeds was the same as in the leaves and stems in the young plants grown from them. SeMet was the major Se compound in Se-rich pea seeds and leaves, comprising 49% and 67% of the total Se content in OT and TT seeds, respectively, and 85% and 79% in the corresponding leaves.

Electron Transport↗
PubMed1985

Sequence of a pseudogene in the legumin gene family of pea (Pisum sativum L.).

A second legumin gene, denoted psi Leg D, has been located on the pea genomic clone lambda Leg 1, approx. 1.3 Kbases 3' of Leg A, in the same orientation. The complete sequence of psi Leg D shows that it is a pseudogene, having two stop codons near the 5' end of its predicted coding sequence, as well as deletions and frame shift errors when compared to Leg A. No transcripts from this gene could be detected in developing pea seeds. Leg A and psi Leg D are homologous over their coding sequences, and partially homologous in the intron sequences and the immediate 5' flanking sequences. Other flanking sequences of the two genes show no significant homology, apart from the presence of polyadenylation signals 3' to both coding sequences. The introns in the two genes occur in corresponding positions in the sequences, but a deletion in psi Leg D affects the 3' boundary of IVS-2. Hybridisation of psi Leg D to pea genomic DNA suggests that it does not represent a hitherto undetected sub-family of legumin genes.

Amino Acid Sequence↗
PubMed1991

cDNA cloning of U1, U2, U4 and U5 snRNA families expressed in pea nuclei.

Differences observed between plant and animal pre-mRNA splicing may be the result of primary or secondary structure differences in small nuclear RNAs (snRNAs). A cDNA library of pea snRNAs was constructed from anti-trimethylguanosine (m3(2,2,7)G immunoprecipitated pea nuclear RNA. The cDNA library was screened using oligo-deoxyribonucleotide probes specific for the U1, U2, U4 and U5 snRNAs. cDNA clones representing U1, U2, U4 and U5 snRNAs expressed in seedling tissue have been isolated and sequenced. Comparison of the pea snRNA variants with other organisms suggest that functionally important primary sequences are conserved phylogenetically even though the overall sequences have diverged substantially. Structural variations in U1 snRNA occur in regions required for U1-specific protein binding. In light of this sequence analysis, it is clear that the dicot snRNA variants do not differ in sequences implicated in RNA:RNA interactions with pre-mRNA. Instead, sequence differences occur in regions implicated in the binding of small ribonucleoproteins (snRNPs) to snRNAs and may result in the formation of unique snRNP particles.

Base Sequence↗