Functional characterization of Rat Plasma Membrane Monoamine Transporter in the Blood–Brain and Blood–Cerebrospinal Fluid Barriers

2011 ◽  
Vol 100 (9) ◽  
pp. 3924-3938 ◽  
Author(s):  
Takashi Okura ◽  
Sayaka Kato ◽  
Yusuke Takano ◽  
Takenori Sato ◽  
Atsushi Yamashita ◽  
...  
Keyword(s):  
Cerebrospinal Fluid ◽  
Plasma Membrane ◽  
Functional Characterization ◽  
Rat Plasma ◽  
Monoamine Transporter ◽  
Blood Brain

scholarly journals Functional characterization of a novel plasma membrane intrinsic protein2 in barley

2012 ◽  
Vol 7 (12) ◽  
pp. 1648-1652 ◽  
Author(s):  
Mineo Shibasaka ◽  
Sizuka Sasano ◽  
Sigeko Utsugi ◽  
Maki Katsuhara
Keyword(s):  
Plasma Membrane ◽  
Functional Characterization

Functional characterization of a plasma membrane Na+/H+ antiporter from alkali grass (Puccinellia tenuiflora)

2010 ◽  
Vol 38 (7) ◽  
pp. 4813-4822 ◽  
Author(s):  
Xin Wang ◽  
Ru Yang ◽  
Baichen Wang ◽  
Guifeng Liu ◽  
Chuanping Yang ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Functional Characterization ◽  
Puccinellia Tenuiflora

scholarly journals RsSOS1 Responding to Salt Stress Might Be Involved in Regulating Salt Tolerance by Maintaining Na+ Homeostasis in Radish (Raphanus sativus L.)

Horticulturae ◽  
2021 ◽  
Vol 7 (11) ◽  
pp. 458
Author(s):  
Wanting Zhang ◽  
Jingxue Li ◽  
Junhui Dong ◽  
Yan Wang ◽  
Liang Xu ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Salt Stress ◽  
Salt Tolerance ◽  
Functional Characterization ◽  
Vital Role ◽  
Salt Stress Response ◽  
Reading Frame ◽  
Yield And Quality

Radish is a kind of moderately salt-sensitive vegetable. Salt stress seriously decreases the yield and quality of radish. The plasma membrane Na+/H+ antiporter protein Salt Overly Sensitive 1 (SOS1) plays a crucial role in protecting plant cells against salt stress, but the biological function of the RsSOS1 gene in radish remains to be elucidated. In this study, the RsSOS1 gene was isolated from radish genotype ‘NAU-TR17’, and contains an open reading frame of 3414 bp encoding 1137 amino acids. Phylogenetic analysis showed that RsSOS1 had a high homology with BnSOS1, and clustered together with Arabidopsis plasma membrane Na+/H+ antiporter (AtNHX7). The result of subcellular localization indicated that the RsSOS1 was localized in the plasma membrane. Furthermore, RsSOS1 was strongly induced in roots of radish under 150 mmol/L NaCl treatment, and its expression level in salt-tolerant genotypes was significantly higher than that in salt-sensitive ones. In addition, overexpression of RsSOS1 in Arabidopsis could significantly improve the salt tolerance of transgenic plants. Meanwhile, the transformation of RsSOS1△999 could rescue Na+ efflux function of AXT3 yeast. In summary, the plasma membrane Na+/H+ antiporter RsSOS1 plays a vital role in regulating salt-tolerance of radish by controlling Na+ homeostasis. These results provided useful information for further functional characterization of RsSOS1 and facilitate clarifying the molecular mechanism underlying salt stress response in radish.

Characterization of the deafwaddler mutant of the rat plasma membrane calcium-ATPase 2

2001 ◽  
Vol 162 (1-2) ◽  
pp. 19-28 ◽  
Author(s):  
Alan R. Penheiter ◽  
Adelaida G. Filoteo ◽  
Cynthia L. Croy ◽  
John T. Penniston
Keyword(s):  
Plasma Membrane ◽  
Rat Plasma ◽  
Calcium Atpase ◽  
Plasma Membrane Calcium Atpase

scholarly journals Proteomic Characterization of Cerebrospinal Fluid from Ataxia-Telangiectasia (A-T) Patients Using a LC/MS-Based Label-Free Protein Quantification Technology

2011 ◽  
Vol 2011 ◽  
pp. 1-13 ◽  
Author(s):  
Monika Dzieciatkowska ◽  
Guihong Qi ◽  
Jinsam You ◽  
Kerry G. Bemis ◽  
Heather Sahm ◽  
...  
Keyword(s):  
Cerebrospinal Fluid ◽  
Biomarker Discovery ◽  
Functional Characterization ◽  
Therapeutic Targets ◽  
Bioinformatic Analysis ◽  
Protein Quantification ◽  
Label Free ◽  
Free Protein ◽  
Potential Biomarker

Cerebrospinal fluid (CSF) has been used for biomarker discovery of neurodegenerative diseases in humans since biological changes in the brain can be seen in this biofluid. Inactivation of A-T-mutated protein (ATM), a multifunctional protein kinase, is responsible for A-T, yet biochemical studies have not succeeded in conclusively identifying the molecular mechanism(s) underlying the neurodegeneration seen in A-T patients or the proteins that can be used as biomarkers for neurologic assessment of A-T or as potential therapeutic targets. In this study, we applied a high-throughput LC/MS-based label-free protein quantification technology to quantitatively characterize the proteins in CSF samples in order to identify differentially expressed proteins that can serve as potential biomarker candidates for A-T. Among 204 identified CSF proteins with high peptide-identification confidence, thirteen showed significant protein expression changes. Bioinformatic analysis revealed that these 13 proteins are either involved in neurodegenerative disorders or cancer. Future molecular and functional characterization of these proteins would provide more insights into the potential therapeutic targets for the treatment of A-T and the biomarkers that can be used to monitor or predict A-T disease progression. Clinical validation studies are required before any of these proteins can be developed into clinically useful biomarkers.

scholarly journals Two Novel Classes of Enzymes Are Required for the Biosynthesis of Aurofusarin in Fusarium graminearum

2011 ◽  
Vol 286 (12) ◽  
pp. 10419-10428 ◽  
Author(s):  
Rasmus J. N. Frandsen ◽  
Claes Schütt ◽  
Birgitte W. Lund ◽  
Dan Staerk ◽  
John Nielsen ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Fusarium Graminearum ◽  
Polyketide Synthase ◽  
Functional Characterization ◽  
Extracellular Enzyme ◽  
Gene Replacement ◽  
Orphan Genes ◽  
Pigment Biosynthesis ◽  
Targeted Gene Replacement

Previous studies have reported the functional characterization of 9 out of 11 genes found in the gene cluster responsible for biosynthesis of the polyketide pigment aurofusarin in Fusarium graminearum. Here we reanalyze the function of a putative aurofusarin pump (AurT) and the two remaining orphan genes, aurZ and aurS. Targeted gene replacement of aurZ resulted in the discovery that the compound YWA1, rather than nor-rubrofusarin, is the primary product of F. graminearum polyketide synthase 12 (FgPKS12). AurZ is the first representative of a novel class of dehydratases that act on hydroxylated γ-pyrones. Replacement of the aurS gene resulted in accumulation of rubrofusarin, an intermediate that also accumulates when the GIP1, aurF, or aurO genes in the aurofusarin cluster are deleted. Based on the shared phenotype and predicted subcellular localization, we propose that AurS is a member of an extracellular enzyme complex (GIP1-AurF-AurO-AurS) responsible for converting rubrofusarin into aurofusarin. This implies that rubrofusarin, rather than aurofusarin, is pumped across the plasma membrane. Replacement of the putative aurofusarin pump aurT increased the rubrofusarin-to- aurofusarin ratio, supporting that rubrofusarin is normally pumped across the plasma membrane. These results provide functional information on two novel classes of proteins and their contribution to polyketide pigment biosynthesis.

Functional characterization of a wheat plasma membrane Na+/H+ antiporter in yeast

2008 ◽  
Vol 473 (1) ◽  
pp. 8-15 ◽  
Author(s):  
Haixia Xu ◽  
Xingyu Jiang ◽  
Kehui Zhan ◽  
Xiyong Cheng ◽  
Xinjian Chen ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Functional Characterization

Neurochemical characterization of pathways expressing plasma membrane monoamine transporter in the rat brain

Neuroscience ◽  
2007 ◽  
Vol 144 (2) ◽  
pp. 616-622 ◽  
Author(s):  
V. Vialou ◽  
L. Balasse ◽  
S. Dumas ◽  
B. Giros ◽  
S. Gautron
Keyword(s):  
Plasma Membrane ◽  
Rat Brain ◽  
Monoamine Transporter

scholarly journals Electrophysiological Characterization of the Polyspecific Organic Cation Transporter Plasma Membrane Monoamine Transporter

2012 ◽  
Vol 40 (6) ◽  
pp. 1138-1143 ◽  
Author(s):  
Shiro Itagaki ◽  
Vadivel Ganapathy ◽  
Horace T. B. Ho ◽  
Mingyan Zhou ◽  
Ellappan Babu ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Organic Cation ◽  
Organic Cation Transporter ◽  
Monoamine Transporter ◽  
Electrophysiological Characterization

Functional characterization of NIPA2, a selective Mg2+ transporter

2008 ◽  
Vol 295 (4) ◽  
pp. C944-C953 ◽  
Author(s):  
Angela Goytain ◽  
Rochelle M. Hines ◽  
Gary A. Quamme
Keyword(s):  
Plasma Membrane ◽  
Functional Characterization ◽  
Affinity Constant ◽  
Fluorescence Studies ◽  
Low Magnesium ◽  
Early Endosomes ◽  
Electrode Voltage ◽  
Voltage Dependent ◽  
Transmembrane Regions

We used microarray analysis to identify renal cell transcripts that were upregulated with low magnesium. One transcript, identified as NIPA2 (nonimprinted in Prader-Willi/Angelman syndrome) subtype 2, was increased over twofold relative to cells cultured in normal magnesium. The deduced sequence comprises 129 amino acids with 8 predicted transmembrane regions. As the secondary structure of NIPA2 conformed to a membrane transport protein, we expressed it in Xenopus oocytes and determined that it mediated Mg2+ uptake with two-electrode voltage-clamp and fluorescence studies. Mg2+ transport was electrogenic, voltage dependent, and saturable, demonstrating a Michaelis affinity constant of 0.31 mM. Unlike other reported Mg2+ transporters, NIPA2 was very selective for the Mg2+ cation. NIPA2 mRNA is found in many tissues but particularly abundant in renal cells. With the use of immunofluorescence, it was shown that NIPA2 protein was normally localized to the early endosomes and plasma membrane and was recruited to the plasma membrane in response to low extracellular magnesium. We conclude that NIPA2 plays a role in magnesium metabolism and regulation of renal magnesium conservation.

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