Characterization of an AtCCX5 gene from Arabidopsis thaliana that involves in high-affinity K+ uptake and Na+ transport in yeast

2011 ◽  
Vol 414 (1) ◽  
pp. 96-100 ◽  
Author(s):  
Xinxin Zhang ◽  
Min Zhang ◽  
Tetsuo Takano ◽  
Shenkui Liu
Keyword(s):  
Arabidopsis Thaliana ◽  
Na Transport ◽  
K Uptake ◽  
High Affinity

scholarly journals Characterization of the high-affinity phosphate transporter PHT1;4 gene promoter of Arabidopsis thaliana in transgenic wheat

2017 ◽  
Vol 61 (3) ◽  
pp. 453-462 ◽  
Author(s):  
E. Penaloza ◽  
M. Santiago ◽  
S. Cabrera ◽  
G. Munoz ◽  
L. J. Corcuera ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Gene Promoter ◽  
Transgenic Wheat ◽  
Phosphate Transporter ◽  
High Affinity

scholarly journals The Effect of AtHKT1;1 or AtSOS1 Mutation on the Expressions of Na+ or K+ Transporter Genes and Ion Homeostasis in Arabidopsis thaliana under Salt Stress

2019 ◽  
Vol 20 (5) ◽  
pp. 1085 ◽  
Author(s):  
Qian Wang ◽  
Chao Guan ◽  
Pei Wang ◽  
Qing Ma ◽  
Ai-Ke Bao ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Salt Stress ◽  
Plant Growth ◽  
Expression Profiles ◽  
Ion Homeostasis ◽  
Wild Type ◽  
Na Transport ◽  
K Uptake ◽  
Selective Transport ◽  
K Transport

HKT1 and SOS1 are two key Na+ transporters that modulate salt tolerance in plants. Although much is known about the respective functions of HKT1 and SOS1 under salt conditions, few studies have examined the effects of HKT1 and SOS1 mutations on the expression of other important Na+ and K+ transporter genes. This study investigated the physiological parameters and expression profiles of AtHKT1;1, AtSOS1, AtHAK5, AtAKT1, AtSKOR, AtNHX1, and AtAVP1 in wild-type (WT) and athkt1;1 and atsos1 mutants of Arabidopsis thaliana under 25 mM NaCl. We found that AtSOS1 mutation induced a significant decrease in transcripts of AtHKT1;1 (by 56–62% at 6–24 h), AtSKOR (by 36–78% at 6–24 h), and AtAKT1 (by 31–53% at 6–24 h) in the roots compared with WT. This led to an increase in Na+ accumulation in the roots, a decrease in K+ uptake and transportation, and finally resulted in suppression of plant growth. AtHKT1;1 loss induced a 39–76% (6–24 h) decrease and a 27–32% (6–24 h) increase in transcripts of AtSKOR and AtHAK5, respectively, in the roots compared with WT. At the same time, 25 mM NaCl decreased the net selective transport capacity for K+ over Na+ by 92% in the athkt1;1 roots compared with the WT roots. Consequently, Na+ was loaded into the xylem and delivered to the shoots, whereas K+ transport was restricted. The results indicate that AtHKT1;1 and AtSOS1 not only mediate Na+ transport but also control ion uptake and the spatial distribution of Na+ and K+ by cooperatively regulating the expression levels of relevant Na+ and K+ transporter genes, ultimately regulating plant growth under salt stress.

scholarly journals Electrophysiological characterization of AtAMT1;4, an extraordinarily high affinity ammonium transporter from Arabidopsis thaliana

2019 ◽  
Author(s):  
Nino Bindel ◽  
Benjamin Neuhäuser
Keyword(s):  
Arabidopsis Thaliana ◽  
Pollen Tube ◽  
Pollen Grains ◽  
Transport Proteins ◽  
Ammonium Transporter ◽  
High Affinity ◽  
Electrode Voltage ◽  
Electrophysiological Characterization ◽  
Unique Expression Pattern

In plants high affinity transport proteins mediate the essential transport of ammonium across membranes. In Arabidopsis thaliana six of these AMmonium Transporters (AMTs) are encoded on the genome. All of these show a unique expression pattern. While most AMTs are highly expressed in the root, AtAMT1;4 expression is limited to the pollen grains and the pollen tube. Here, we addressed the transport characteristics of AtAMT1;4 in the heterologous Xenopus laevis oocytes system. Two electrode voltage clamp measurements tagged AtAMT1;4 as an electrogenic high affinity ammonium transporter. The transport was saturable and showed extraordinarily high affinity for ammonium with a Km value lower than 10 µM.

Characterization of a Mode of Specific Binding of Fibrin Monomer through its Amino-Terminal Domain by Macrophages and Macrophage Cell-Lines

1990 ◽  
Vol 63 (02) ◽  
pp. 193-203 ◽  
Author(s):  
John R Shainoff ◽  
Deborah J Stearns ◽  
Patricia M DiBello ◽  
Youko Hishikawa-Itoh
Keyword(s):  
Peritoneal Macrophages ◽  
Affinity Binding ◽  
Macrophage Cell ◽  
High Affinity Binding ◽  
Amino Terminal ◽  
High Affinity ◽  
Terminal Domain ◽  
Weak Binding ◽  
Amino Terminal Domain

SummaryThe studies reported here probe the existence of a receptor-mediated mode of fibrin-binding by macrophages that is associated with the chemical change underlying the fibrinogen-fibrin conversion (the release of fibrinopeptides from the amino-terminal domain) without depending on fibrin-aggregation. The question is pursued by 1) characterization of binding in relation to fibrinopeptide content of both the intact protein and the CNBr-fragment comprising the amino-terminal domain known as the NDSK of the protein, 2) tests of competition for binding sites, and 3) photo-affinity labeling of macrophage surface proteins. The binding of intact monomers of types lacking either fibrinopeptide A alone (α-fibrin) or both fibrinopeptides A and B (αβ-fibrin) by peritoneal macrophages is characterized as proceeding through both a fibrin-specific low density/high affinity (BMAX ≃ 200–800 molecules/cell, KD ≃ 10−12 M) interaction that is not duplicated with fibrinogen, and a non-specific high density/low affinity (BMAX ≥ 105 molecules/cell, KD ≥ 10−6 M) interaction equivalent to the weak binding of fibrinogen. Similar binding characteristics are displayed by monocyte/macrophage cell lines (J774A.1 and U937) as well as peritoneal macrophages towards the NDSK preparations of these proteins, except for a slightly weaker (KD ≃ 10−10 M) high-affinity binding. The high affinity binding of intact monomer is inhibitable by fibrin-NDSK, but not fibrinogen-NDSK. This binding appears principally dependent on release of fibrinopeptide-A, because a species of fibrin (β-fibrin) lacking fibrinopeptide-B alone undergoes only weak binding similar to that of fibrinogen. Synthetic Gly-Pro-Arg and Gly-His-Arg-Pro corresponding to the N-termini of to the α- and the β-chains of fibrin both inhibit the high affinity binding of the fibrin-NDSKs, and the cell-adhesion peptide Arg-Gly-Asp does not. Photoaffinity-labeling experiments indicate that polypeptides with elec-trophoretically estimated masses of 124 and 187 kDa are the principal membrane components associated with specifically bound fibrin-NDSK. The binding could not be up-regulated with either phorbol myristyl acetate, interferon gamma or ADP, but was abolished by EDTA and by lipopolysaccharide. Because of the low BMAX, it is suggested that the high-affinity mode of binding characterized here would be too limited to function by itself in scavenging much fibrin, but may act cooperatively with other, less limited modes of fibrin binding.

Acid-Sensing Ion Channels

2020 ◽  
Author(s):  
Stefan Gründer
Keyword(s):  
Nervous System ◽  
Ion Channels ◽  
Excitatory Synapses ◽  
Detailed Characterization ◽  
High Affinity ◽  
Acid Sensing Ion Channels ◽  
Long Time ◽  
Pathological Pain

Acid-sensing ion channels (ASICs) are proton-gated Na+ channels. Being almost ubiquitously present in neurons of the vertebrate nervous system, their precise function remained obscure for a long time. Various animal toxins that bind to ASICs with high affinity and specificity have been tremendously helpful in uncovering the role of ASICs. We now know that they contribute to synaptic transmission at excitatory synapses as well as to sensing metabolic acidosis and nociception. Moreover, detailed characterization of mouse models uncovered an unanticipated role of ASICs in disorders of the nervous system like stroke, multiple sclerosis, and pathological pain. This review provides an overview on the expression, structure, and pharmacology of ASICs plus a summary of what is known and what is still unknown about their physiological functions and their roles in diseases.

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