Isolation and characterization of a cDNA encoding an ACC oxidase from Cicer arietinum and its expression during embryogenesis and seed germination

1998 ◽  
Vol 25 (6) ◽  
pp. 765 ◽  
Author(s):  
M.C. Gómez-Jiménez ◽  
A.J. Matilla ◽  
D. Garrido
Keyword(s):  
Molecular Weight ◽  
Cicer Arietinum ◽  
Acc Oxidase ◽  
Protein Product ◽  
Transcriptional Level ◽  
Mrna Levels ◽  
Embryonic Axes ◽  
Chick Pea ◽  
Isolation And Characterization ◽  
Genes Encoding

A full length cDNA (caaco1) encoding a putative ACC-oxidase (ACCO) was isolated and sequenced from embryonic axes of chick-pea (Cicer arietinum L.) seeds, which depend on ethylene synthesis for germination. The deduced protein for caaco1 has a molecular weight of 36 kDa, a high homology with other ACCOs and is apparently found in the cytosolic fraction of the cell. Heterologous expression of this cDNA confirmed that the protein product exhibits ACCO activity and a molecular weight close to 38 kDa. Southern blot analysis shows that there are at least two genes encoding ACCO in the chick-pea genome. The caaco1 mRNA levels in seeds remained constant during the initial stages of embryogenesis decreasing in the latest stages. During germination, caaco1 mRNA levels increase, reaching a maximum at 24 h, coinciding with the maximum percentage of germination (when all seeds are germinated), ACCO activity and ethylene production. It is interesting that there is a shift in the tissue source of the caaco1 mRNA during embryogenesis and germination. While the bulk of the expression was detected in cotyledons during embryogenesis, it was the embryonic axis that provided most of the expression detected during germination. Our data suggest that during embryogenesis ACCO is regulated at the translational level, but during germination at the transcriptional level.

scholarly journals Key Function for the CCAAT-Binding Factor Php4 To Regulate Gene Expression in Response to Iron Deficiency in Fission Yeast

2008 ◽  
Vol 7 (3) ◽  
pp. 493-508 ◽  
Author(s):  
Alexandre Mercier ◽  
Stephen Watt ◽  
Jürg Bähler ◽  
Simon Labbé
Keyword(s):  
Iron Deficiency ◽  
Fission Yeast ◽  
Tricarboxylic Acid Cycle ◽  
Transcriptional Level ◽  
Mrna Levels ◽  
Gata Factor ◽  
Iron Starvation ◽  
A Genome ◽  
Binding Factor ◽  
Genes Encoding

ABSTRACT The fission yeast Schizosaccharomyces pombe responds to the deprivation of iron by inducing the expression of the php4 + gene, which encodes a negative regulatory subunit of the heteromeric CCAAT-binding factor. Once formed, the Php2/3/4/5 transcription complex is required to inactivate a subset of genes encoding iron-using proteins. Here, we used a pan-S. pombe microarray to study the transcriptional response to iron starvation and identified 86 genes that exhibit php4 + -dependent changes on a genome-wide scale. One of these genes encodes the iron-responsive transcriptional repressor Fep1, whose mRNA levels were decreased after treatment with the permeant iron chelator 2,2′-dipyridyl. In addition, several genes encoding the components of iron-dependent biochemical pathways, including the tricarboxylic acid cycle, mitochondrial respiration, amino acid biosynthesis, and oxidative stress defense, were downregulated in response to iron deficiency. Furthermore, Php4 repressed transcription when brought to a promoter using a yeast DNA-binding domain, and iron deprivation was required for this repression. On the other hand, Php4 was constitutively active when glutathione levels were depleted within the cell. Based on these and previous results, we propose that iron-dependent inactivation of Php4 is regulated at two distinct levels: first, at the transcriptional level by the iron-responsive GATA factor Fep1 and second, at the posttranscriptional level by a mechanism yet to be identified, which inhibits Php4-mediated repressive function when iron is abundant.

Altered development of polysomal RNA activity in chick-pea (Cicer arietinum L.) embryonic axes. Effects of abscisic acid and temperature

Planta ◽  
1985 ◽  
Vol 164 (4) ◽  
pp. 517-523 ◽  
Author(s):  
D. Rodriguez ◽  
G. Nicol�s ◽  
J. J. Aldasoro ◽  
J. Hern�ndez-Nistal ◽  
M. J. Babiano ◽  
...  
Keyword(s):  
Abscisic Acid ◽  
Cicer Arietinum ◽  
Embryonic Axes ◽  
Chick Pea ◽  
Cicer Arietinum L

scholarly journals Proteomic and Transcriptomic Analysis of Extracellular Proteins and mRNA Levels in Thermobifida fusca Grown on Cellobiose and Glucose

2007 ◽  
Vol 189 (17) ◽  
pp. 6260-6265 ◽  
Author(s):  
Shaolin Chen ◽  
David B. Wilson
Keyword(s):  
Cell Wall ◽  
Plant Cell Wall ◽  
Extracellular Proteins ◽  
Transcriptional Analysis ◽  
Thermobifida Fusca ◽  
Transcriptional Level ◽  
Mrna Levels ◽  
Egg White Lysozyme ◽  
Extracellular Proteome ◽  
Genes Encoding

ABSTRACT Thermobifida fusca secretes proteins that carry out plant cell wall degradation. Using two-dimensional electrophoresis, the extracellular proteome of T. fusca grown on cellobiose was compared to that of cells grown on glucose. Extracellular proteins, the expression of which is induced by cellobiose, mainly are cellulases and cellulose-binding proteins. Other major extracellular proteins induced by cellobiose include a xylanase (Xyl10A) and two unknown proteins, the C-terminal regions of which are homologous to a lytic transglycosylase goose egg white lysozyme domain and an NLPC_P60 domain (which defines a family of cell wall peptidases), respectively. Transcriptional analysis of genes encoding cellobiose-induced proteins suggests that their expression is controlled at the transcriptional level and that their expression also is induced by cellulose. Some other major extracellular proteins produced by T. fusca grown on both cellobiose and glucose include Lam81A and three unknown proteins that are homologous to aminopeptidases and xylanases or that contain a putative NLPC_P60 domain.

Alleviation of Thermoinhibition in Chickpea Seeds by Putrescine Involves the Ethylene Pathway

1996 ◽  
Vol 23 (4) ◽  
pp. 479 ◽  
Author(s):  
M Gallardo ◽  
I Sanchez-Calle ◽  
PMD Rueda ◽  
AJ Matilla
Keyword(s):  
Molecular Weight ◽  
Carboxylic Acid ◽  
Cicer Arietinum ◽  
Ethylene Production ◽  
Acc Oxidase ◽  
Sharp Decrease ◽  
Acc Synthase ◽  
Cicer Arietinum L ◽  
Adenosyl Methionine ◽  
Stimulation Of

Germination of chickpea (Cicer arietinum L.) was inhibited by supraoptimal temperatures of 30 or 35�C, but the inhibition was alleviated by a relatively low concentration (1 mM) of putrescine (Put). This allevation may be due to (a) stimulation of the 1-aminocyclopropane-1-carboxylate (ACC) synthase and ACC oxidase activities; (b) increased levels of ACC and decreased levels of 1-(malonylamino)cyclopropane-1-carboxylic acid (MACC); or (c) strongly increased ethylene production. Put at 10 mM did not alleviate thermoinhibition, although, as with Put at 1 mM, it did inhibit adenosyl-methionine (AdoMet) decarboxylase. Alleviation conditions resulted in: (a) an induced accumulation of free Put (S) and Put conjugated to substances of low (HS) and high (HP) molecular weight; (b) a decrease in spermidine (Spd) and spermine (Spm) (S and HP); and (c) no alteration in the levels of Spd and Spm (HS) with respect to the absence of Put (1 mM) at 30�C. In the presence of Put (10 mM), increased accumulation of Put (S, HS and HP) was detected, but with a sharp decrease of Spd and Spm (S and HS).

Involvement of calcium in ACC-oxidase activity from Cicer arietinum seed embryonic axes

1999 ◽  
Vol 50 (3) ◽  
pp. 373-376 ◽  
Author(s):  
M Gallardo ◽  
M del Carmen Gómez-Jiménez ◽  
A Matilla
Keyword(s):  
Cicer Arietinum ◽  
Oxidase Activity ◽  
Acc Oxidase ◽  
Embryonic Axes

scholarly journals Differential Influence of Inositol Hexaphosphate on the Expression of Genes Encoding TGF-βIsoforms and Their Receptors in Intestinal Epithelial Cells Stimulated with Proinflammatory Agents

2013 ◽  
Vol 2013 ◽  
pp. 1-10
Author(s):  
Małgorzata Kapral ◽  
Joanna Wawszczyk ◽  
Stanisław Sośnicki ◽  
Ludmiła Węglarz
Keyword(s):  
Mrna Expression ◽  
Transforming Growth Factor ◽  
Inflammatory Responses ◽  
Transcriptional Level ◽  
Mrna Levels ◽  
Dependent Manner ◽  
Inositol Hexaphosphate ◽  
Inflammatory Conditions ◽  
Expression Of Genes ◽  
Genes Encoding

Transforming growth factorβ(TGF-β) is a multifunctional cytokine recognized as an important regulator of inflammatory responses. The effect of inositol hexaphosphate (IP6), a naturally occurring phytochemical, on the mRNA expression of TGF-β1, TGF-β2, TGF-β3 and TβRI, TβRII, and TβRIII receptors stimulated with bacterial lipopolysaccharides (Escherichia coliandSalmonella typhimurium) and IL-1βin intestinal cells Caco-2 for 3 and 12 h was investigated. Real-time qRT-PCR was used to validate mRNAs level of examined genes. Bacterial endotoxin promoted differential expression of TGF-βs and their receptors in a time-dependent manner. IL-1βupregulated mRNA levels of all TGF-βs and receptors at both 3 h and 12 h. IP6 elicited the opposed to LPS effect by increasing downregulated transcription of the examined genes and suppressing the expression of TGF-β1 at 12 h. IP6 counteracted the stimulatory effect of IL-1βon TGF-β1 and receptors expression by decreasing their mRNA levels. IP6 enhanced LPS- and IL-1β-stimulated mRNA expression of TGF-β2 and -β3. Based on these studies it may be concluded that IP6 present in the intestinal milieu may exert immunoregulatory effects and chemopreventive activity on colonic epithelium under inflammatory conditions or during microbe-induced infection/inflammation by modulating the expression of genes encoding TGF-βs and their receptors at transcriptional level.

scholarly journals Pioglitazone increases secretion of high-molecular-weight adiponectin from adipocytes

2006 ◽  
Vol 291 (5) ◽  
pp. E1100-E1105 ◽  
Author(s):  
Angela M. Bodles ◽  
Anannya Banga ◽  
Neda Rasouli ◽  
Fumiyo Ono ◽  
Philip A. Kern ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Adipose Tissue ◽  
High Molecular Weight ◽  
Human Adipose Tissue ◽  
Transcriptional Level ◽  
Mrna Levels ◽  
Primary Mouse ◽  
Mouse Adipocytes ◽  
Pioglitazone Treatment

Adiponectin is an adipocyte-derived serum protein that plays important roles in energy homeostasis, obesity, and insulin sensitivity. Using sucrose gradients and Western blotting of nondenaturing gels, we examined the adiponectin isoforms secreted from human adipose tissue, human and mouse adipocytes, and cell lines in response to pioglitazone added in vitro. The predominant form secreted from adipose tissue in vitro was the high-molecular-weight (HMW) isoform, with small amounts of low-molecular-weight (LMW) forms present. The addition of pioglitazone (1–3 μM) in vitro increased the secretion of the HMW isoform, with no significant effect on the other isoforms. Human adipose tissue was also examined for changes in adiponectin mRNA levels upon pioglitazone treatment. No difference was detected, suggesting that the effect of pioglitazone is not at the transcriptional level but, rather, at a posttranscriptional phase of the secretory pathway. Additional experiments were conducted to determine whether adiponectin expression was mechanistically similar in other adipose cells. Examination of primary human adipocytes revealed an increase in intracellular HMW isoform with a decline in LMW forms following pioglitazone treatment, with a corresponding increase in the secreted HMW form. Similar results were observed with primary mouse adipocytes, 3T3-F422A cells, and SGBS human adipocyte cells, although differences in the distribution of HMW and LMW isoforms were apparent between cell types. Although there are differences in isoforms between species, in all cases pioglitazone served to increase the secretion of the HMW form of adiponectin.

Effect of short-chain fatty acids on the ethylene pathway in embryonic axes of Cicer arietinum during germination

1994 ◽  
Vol 92 (4) ◽  
pp. 629-635 ◽  
Author(s):  
Mercedes Gallardo ◽  
Paloma Munoz De Rueda ◽  
Angel Jesus Matilla ◽  
Isabel Maria Sanchez-Calle
Keyword(s):  
Fatty Acids ◽  
Cicer Arietinum ◽  
Short Chain Fatty Acids ◽  
Short Chain ◽  
Embryonic Axes ◽  
Chain Fatty Acids

Endotoxin-Induced Tissue Factor in Human Monocytes is Dependent upon Protein Kinase C Activation

1993 ◽  
Vol 70 (05) ◽  
pp. 800-806 ◽  
Author(s):  
C Ternisien ◽  
M Ramani ◽  
V Ollivier ◽  
F Khechai ◽  
T Vu ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Tissue Factor ◽  
Factor Ix ◽  
Transcriptional Level ◽  
Mrna Levels ◽  
Dependent Manner ◽  
Human Monocytes ◽  
Kinase C ◽  
Pkc Activation

SummaryTissue factor (TF) is a transmembrane receptor which, in association with factors VII and Vila, activates factor IX and X, thereby activating the coagulation protease cascades. In response to bacterial lipopolysaccharide (LPS) monocytes transcribe, synthesize and express TF on their surface. We investigated whether LPS-induced TF in human monocytes is mediated by protein kinase C (PKC) activation. The PKC agonists phorbol 12- myristate 13-acetate (PMA) and phorbol 12, 13 dibutyrate (PdBu) were both potent inducers of TF in human monocytes, whereas 4 alpha-12, 13 didecanoate (4 a-Pdd) had no such effect. Both LPS- and PMA-induced TF activity were inhibited, in a concentration dependent manner, by three different PKC inhibitors: H7, staurosporine and calphostin C. TF antigen determination confirmed that LPS-induced cell-surface TF protein levels decreased in parallel to TF functional activity under staurosporine treatment. Moreover, Northern blot analysis of total RNA from LPS- or PMA-stimulated monocytes showed a concentration-dependent decrease in TF mRNA levels in response to H7 and staurosporine. The decay rate of LPS-induced TF mRNA evaluated after the arrest of transcription by actinomycin D was not affected by the addition of staurosporine, suggesting that its inhibitory effect occurred at a transcriptional level. We conclude that LPS-induced production of TF and its mRNA by human monocytes are dependent on PKC activation.

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