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Article ; Online: Amino Acid Transporters Proteins Involved in the Glutamate-Glutamine Cycle and Their Alterations in Murine Models of Alzheimer's Disease.

Vázquez-Durán, Diana Laura / Ortega, Arturo / Rodríguez, Angelina

2024

Abstract: The brain's ability to integrate external stimuli and generate responses is highly complex. While these mechanisms are not completely understood, current evidence suggests that alterations in cellular metabolism and microenvironment are involved in some ... ...

Abstract	The brain's ability to integrate external stimuli and generate responses is highly complex. While these mechanisms are not completely understood, current evidence suggests that alterations in cellular metabolism and microenvironment are involved in some dysfunctions as complex as Alzheimer's disease. This pathology courses with defects in the establishment of chemical synapses, which is dependent on the production and supply of neurotransmitters like glutamate and its recycling through the glutamate-glutamine cycle. Alterations in the expression and function of the amino acid transporters proteins involved in this cycle have recently been reported in different stages of Alzheimer's disease. Most of these data come from patients in advanced stages of the disease or post-mortem, due to the ethical and technical limitations of human studies. Therefore, genetically modified mouse models have been an excellent tool to analyze metabolic and even behavioral parameters that are very similar to those that develop in Alzheimer's disease, even at presymptomatic stages. Hence, this paper analyzes the role of glutamate metabolism and its intercellular trafficking in excitatory synapses from different approaches using transgenic mouse models; such an analysis will contribute to our present understanding of AD.
Language	English
Publishing date	2024-01-26
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	645020-9
ISSN	1559-1182 ; 0893-7648
ISSN (online)	1559-1182
ISSN	0893-7648
DOI	10.1007/s12035-024-03966-3
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Article: Glutamine/Glutamate Transporters in Glial Cells: Much More Than Participants of a Metabolic Shuttle.

Rodríguez, Angelina / Ortega, Arturo

Advances in neurobiology

2017 Volume 16, Page(s) 169–183

Abstract: Glial glutamine and glutamate transporters play an important role in glial/neuronal interactions. An excellent model to establish the role of these membrane proteins is the cerebellum. The most abundant glutamatergic synapse in the central nervous system ...

Abstract	Glial glutamine and glutamate transporters play an important role in glial/neuronal interactions. An excellent model to establish the role of these membrane proteins is the cerebellum. The most abundant glutamatergic synapse in the central nervous system is present in the molecular layer of the cerebellar cortex, and it is entirely wrapped by Bergmann glial cells. The recycling of glutamate involves glutamate and glutamine transporters enriched in these radial glial processes. The functional properties of amino acid glial transporters allow, in an activity-dependent manner, the conformation of protein complexes important for the adequate support of glutamatergic neurotransmission. A detailed description of the most important features of glial glutamate and glutamine transporters follows, and a working model of the molecular mechanisms by which these glutamate and glutamine binding proteins interact, and by these means might modulate cerebellar glutamatergic transactions, is presented.
MeSH term(s)	Amino Acid Transport System X-AG/metabolism ; Animals ; Carrier Proteins/metabolism ; Cerebellum/metabolism ; Humans ; Models, Neurological ; Neuroglia/metabolism
Chemical Substances	Amino Acid Transport System X-AG ; Carrier Proteins ; glutamine transport proteins
Language	English
Publishing date	2017-08-05
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ISSN	2190-5215
ISSN	2190-5215
DOI	10.1007/978-3-319-55769-4_8
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Article ; Online: Effect of an Electronic Order Set on Newborn Hepatitis B Immunization Rates.

Pedersen, Daniel / Rodriguez, Angelina / Oyesanmi, Olu / Schramm, Heather / King, Michael

HCA healthcare journal of medicine

2020 Volume 1, Issue 6, Page(s) 507–512

Abstract: Objective: Hepatitis B is an infectious deoxyribonucleic acid virus which can cause significant morbidity and mortality. There is no current definitive treatment, however in the United States immunization is widely available. A paper published by the ... ...

Abstract	Objective: Hepatitis B is an infectious deoxyribonucleic acid virus which can cause significant morbidity and mortality. There is no current definitive treatment, however in the United States immunization is widely available. A paper published by the Advisory Committee on Immunization Practices/Centers for Disease Control (ACIP/CDC) in 2018 made updated recommendations regarding vaccination practices in the United States. The most notable change made was that all healthy newborns weighing ≥2000 g with a negative hepatitis B-status mother should receive hepatitis B immunization within 24 hours of birth. This quality improvement project studied the effect of the electronic medical record newborn admission order set, altered to reflect current societal recommendations, and the resulting newborn hepatitis B immunization rates. Methods: The electronic medical record admission order set was modified to reflect the most recent recommendations made by ACIP/CDC. Hepatitis B immunization rates were then analyzed prior to and following the order set changes. Results: The most significant effect was seen in the overall rate of hepatitis B immunization achieved prior to hospital discharge. In the 12 months before order set modifications were implemented the rate was 9.5%. Following electronic medical record changes it improved to over 90%. In addition, the immunization rate performed within the first 24 hours increased from 74.1% to 91.1%. Finally, these records were made accessible to outpatient providers via a statewide immunization database. Conclusions: This project serves as an example of how modifying order sets can have a dramatic effect on ordering practices and therefore allows for quality improvement.
Language	English
Publishing date	2020-12-29
Publishing country	United States
Document type	Journal Article
ISSN	2689-0216
ISSN (online)	2689-0216
DOI	10.36518/2689-0216.1152
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Article ; Online: Getting the hypertension Dx right: Patient positioning matters.

Morcos, Roy N / Carter, Kimbroe J / Castro, Frank / Yu, Nathan / Jordan, Cary / Macabobby, Thomas D / Rodriguez, Angelina

The Journal of family practice

2018 Volume 67, Issue 4, Page(s) 199;201;206;207

Abstract: Taking blood pressure with the patient seated on the edge of an exam table led to misclassification of prehypertension or hypertension in 13.2% of patients. ...

Abstract	Taking blood pressure with the patient seated on the edge of an exam table led to misclassification of prehypertension or hypertension in 13.2% of patients.
MeSH term(s)	Adult ; Aged ; Aged, 80 and over ; Antihypertensive Agents/therapeutic use ; Blood Pressure Determination/methods ; Diagnostic Errors/statistics & numerical data ; Female ; Humans ; Hypertension/diagnosis ; Male ; Middle Aged ; Patient Positioning/methods ; Risk Factors ; Sitting Position
Chemical Substances	Antihypertensive Agents
Language	English
Publishing date	2018-04-03
Publishing country	United States
Document type	Comparative Study ; Journal Article
ZDB-ID	197883-4
ISSN	1533-7294 ; 0094-3509
ISSN (online)	1533-7294
ISSN	0094-3509
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Article ; Online: Serotonin receptors in hippocampus.

Berumen, Laura Cristina / Rodríguez, Angelina / Miledi, Ricardo / García-Alcocer, Guadalupe

TheScientificWorldJournal

2012 Volume 2012, Page(s) 823493

Abstract: Serotonin is an ancient molecular signal and a recognized neurotransmitter brainwide distributed with particular presence in hippocampus. Almost all serotonin receptor subtypes are expressed in hippocampus, which implicates an intricate modulating system, ...

Abstract	Serotonin is an ancient molecular signal and a recognized neurotransmitter brainwide distributed with particular presence in hippocampus. Almost all serotonin receptor subtypes are expressed in hippocampus, which implicates an intricate modulating system, considering that they can be localized as autosynaptic, presynaptic, and postsynaptic receptors, even colocalized within the same cell and being target of homo- and heterodimerization. Neurons and glia, including immune cells, integrate a functional network that uses several serotonin receptors to regulate their roles in this particular part of the limbic system.
MeSH term(s)	Animals ; Hippocampus/physiology ; Humans ; Receptors, Serotonin/metabolism ; Serotonin/metabolism ; Synaptic Transmission/physiology
Chemical Substances	Receptors, Serotonin ; Serotonin (333DO1RDJY)
Language	English
Publishing date	2012-05-02
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	2075968-X
ISSN	1537-744X ; 1537-744X
ISSN (online)	1537-744X
ISSN	1537-744X
DOI	10.1100/2012/823493
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Article ; Online: RON2, a novel gene in

Mosqueda, Juan / Hidalgo-Ruiz, Mario / Calvo-Olvera, Diana Alexandra / Hernandez-Silva, Diego Josimar / Ueti, Massaro Wilson / Mercado-Uriostegui, Miguel Angel / Rodriguez, Angelina / Ramos-Aragon, Juan Alberto / Hernandez-Ortiz, Ruben / Kawazu, Shin-Ichiro / Igarashi, Ikuo

Parasitology

2019 Volume 146, Issue 13, Page(s) 1646–1654

Abstract: Bovine babesiosis is the most important protozoan disease transmitted by ticks. In Plasmodium falciparum, another Apicomplexa protozoan, the interaction of rhoptry neck protein 2 (RON2) with apical membrane antigen-1 (AMA-1) has been described to have a ... ...

Abstract	Bovine babesiosis is the most important protozoan disease transmitted by ticks. In Plasmodium falciparum, another Apicomplexa protozoan, the interaction of rhoptry neck protein 2 (RON2) with apical membrane antigen-1 (AMA-1) has been described to have a key role in the invasion process. To date, RON2 has not been described in Babesia bigemina, the causal agent of bovine babesiosis in the Americas. In this work, we found a ron2 gene in the B. bigemina genome. RON2 encodes a protein that is 1351 amino acids long, has an identity of 64% (98% coverage) with RON2 of B. bovis and contains the CLAG domain, a conserved domain in Apicomplexa. B. bigemina ron2 is a single copy gene and it is transcribed and expressed in blood stages as determined by RT-PCR, Western blot, and confocal microscopy. Serum samples from B. bigemina-infected bovines were screened for the presence of RON2-specific antibodies, showing the recognition of conserved B-cell epitopes. Importantly, in vitro neutralization assays showed an inhibitory effect of RON2-specific antibodies on the red blood cell invasion by B. bigemina. Therefore, RON2 is a novel antigen in B. bigemina and contains conserved B-cell epitopes, which induce antibodies that inhibit merozoite invasion.
MeSH term(s)	Animals ; Antibodies, Protozoan/blood ; Babesia/genetics ; Babesia/immunology ; Babesiosis/parasitology ; Cattle ; DNA, Protozoan/immunology ; Epitopes, B-Lymphocyte/immunology ; Erythrocytes/parasitology ; Genome, Protozoan ; Male ; Merozoites/genetics ; Merozoites/immunology ; Neutralization Tests ; Protozoan Proteins/genetics ; Protozoan Proteins/immunology
Chemical Substances	Antibodies, Protozoan ; DNA, Protozoan ; Epitopes, B-Lymphocyte ; Protozoan Proteins
Language	English
Publishing date	2019-09-13
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	207627-5
ISSN	1469-8161 ; 0031-1820
ISSN (online)	1469-8161
ISSN	0031-1820
DOI	10.1017/S0031182019001161
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Article ; Online: Expression of the System N transporter (SNAT5/SN2) during development indicates its plausible role in glutamatergic neurotransmission.

Rodríguez, Angelina / Ortega, Arturo / Berumen, Laura C / García-Alcocer, María G / Giménez, Cecilio / Zafra, Francisco

Neurochemistry international

2014 Volume 73, Page(s) 166–171

Abstract: Solute neutral amino acid transporter 5 (SNAT5/SN2) is a member of the System N family, expressed in glial cells in the adult brain, able to transport glutamine, histidine or glycine among other substrates. Its tight association with synapses and its ... ...

Abstract	Solute neutral amino acid transporter 5 (SNAT5/SN2) is a member of the System N family, expressed in glial cells in the adult brain, able to transport glutamine, histidine or glycine among other substrates. Its tight association with synapses and its electroneutral mode of operation that allows the bidirectional movement of substrates, supports the idea that this transporter participates in the function of the glutamine-glutamate cycle between neurons and glia. Moreover, SNAT5/SN2 might contribute to the regulation of glycine concentration in glutamatergic synapses and, therefore, to the functioning of the N-methyl-d-aspartate (NMDA) subtype of glutamate receptors. Ontogenic maturation of these synapses occurs postnatally through the coordinate expression of a large number of receptors, transporters, structural and regulatory proteins that ensure the correct operation of the excitatory pathways in the central nervous system. Since the temporal pattern of expression of SNAT5/SN2 is unknown, we analyzed it by immunoblot and immunohistochemical techniques. Results indicate that the expression of SNAT5/SN2 is triggered between the second and third postnatal week in the cerebral cortex, in parallel to the expression of the vesicular glutamate transporter vGLUT1 and the glial glutamate transporter GLT1/EAAT2. In the cerebellum, this process occurs about one week later than in the cerebral cortex. Immunohistochemical staining of cortical sections shows that from postnatal day 14 to adulthood the transporter was expressed exclusively in glial cells. Our results are consistent with the idea that SNAT5/SN2 expression is coordinated with that of other proteins necessary for the operation of glutamatergic synapses and reinforce the existence of a regulatory cross-talk between neurons and glia that orchestrates the building up of these synapses.
MeSH term(s)	Amino Acid Transport System X-AG/metabolism ; Amino Acid Transport Systems, Neutral/genetics ; Amino Acid Transport Systems, Neutral/physiology ; Animals ; Excitatory Amino Acid Transporter 2/biosynthesis ; Excitatory Amino Acid Transporter 2/genetics ; Female ; Glucose Transporter Type 1/biosynthesis ; Glucose Transporter Type 1/genetics ; Glutamic Acid/physiology ; Male ; Neuroglia/physiology ; Pregnancy ; Rats ; Rats, Wistar ; Synaptic Transmission/genetics ; Synaptic Transmission/physiology
Chemical Substances	Amino Acid Transport System X-AG ; Amino Acid Transport Systems, Neutral ; Excitatory Amino Acid Transporter 2 ; Glucose Transporter Type 1 ; Slc1a2 protein, rat ; Slc2a1 protein, rat ; Slc38a5 protein, rat ; Glutamic Acid (3KX376GY7L)
Language	English
Publishing date	2014-07
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	283190-9
ISSN	1872-9754 ; 0197-0186
ISSN (online)	1872-9754
ISSN	0197-0186
DOI	10.1016/j.neuint.2013.11.011
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Article: RON2, a novel gene in Babesia bigemina, contains conserved, immunodominant B-cell epitopes that induce antibodies that block merozoite invasion

Parasitology. 2019 Nov., v. 146, no. 13

2019

Abstract	Bovine babesiosis is the most important protozoan disease transmitted by ticks. In Plasmodium falciparum, another Apicomplexa protozoan, the interaction of rhoptry neck protein 2 (RON2) with apical membrane antigen-1 (AMA-1) has been described to have a key role in the invasion process. To date, RON2 has not been described in Babesia bigemina, the causal agent of bovine babesiosis in the Americas. In this work, we found a ron2 gene in the B. bigemina genome. RON2 encodes a protein that is 1351 amino acids long, has an identity of 64% (98% coverage) with RON2 of B. bovis and contains the CLAG domain, a conserved domain in Apicomplexa. B. bigemina ron2 is a single copy gene and it is transcribed and expressed in blood stages as determined by RT-PCR, Western blot, and confocal microscopy. Serum samples from B. bigemina-infected bovines were screened for the presence of RON2-specific antibodies, showing the recognition of conserved B-cell epitopes. Importantly, in vitro neutralization assays showed an inhibitory effect of RON2-specific antibodies on the red blood cell invasion by B. bigemina. Therefore, RON2 is a novel antigen in B. bigemina and contains conserved B-cell epitopes, which induce antibodies that inhibit merozoite invasion.
Keywords	B-lymphocytes ; Babesia bigemina ; Babesia bovis ; Plasmodium falciparum ; Protozoa ; Western blotting ; amino acids ; antibodies ; babesiosis ; blood serum ; cattle ; confocal microscopy ; epitopes ; erythrocytes ; genes ; merozoites ; neutralization tests ; protozoal infections ; reverse transcriptase polymerase chain reaction ; rhoptry proteins ; ticks ; transcription (genetics) ; North America ; South America
Language	English
Dates of publication	2019-11
Size	p. 1646-1654.
Publishing place	Cambridge University Press
Document type	Article
ZDB-ID	207627-5
ISSN	1469-8161 ; 0031-1820
ISSN (online)	1469-8161
ISSN	0031-1820
DOI	10.1017/S0031182019001161
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Distribution of the purinegic receptors P2X(4) and P2X(6) during rat gut development.

García-Alcocer, Guadalupe / Padilla, Karla / Rodríguez, Angelina / Miledi, Ricardo / Berumen, Laura C

Neuroscience letters

2012 Volume 509, Issue 2, Page(s) 92–95

Abstract: The purinergic receptors P2X(4) and P2X(6) are ion channels activated by ATP. These receptors are present in the gastrointestinal tract, and they are involved in synaptic transmission, taste sensation, and pain, among other functions. In this work, we ... ...

Abstract	The purinergic receptors P2X(4) and P2X(6) are ion channels activated by ATP. These receptors are present in the gastrointestinal tract, and they are involved in synaptic transmission, taste sensation, and pain, among other functions. In this work, we studied the distribution of P2X(4) and P2X(6) receptors in proximal and distal regions of the gut newborn and adult rats. Using immunohistochemistry, purinergic receptors were found in gut epithelial cells and capillary vessels. In both proximal and distal regions of newborn rats, we observed P2X(4) signal in epithelial cells, whereas P2X(6) was present in capillary vessels in the proximal region and to a lesser extent in the distal region. In both regions of adult gut, we observed P2X(4) and P2X(6) immunostain in the capillary vessels. Semi-quantification indicated a significant difference in the amount of P2X(4) between proximal regions, whereas the P2X(6) content of both newborn regions differed from that in adult proximal gut. We conclude that P2X(4) and P2X(6) purinoreceptors are present in the gut from birth and that they are differentially distributed among regions.
MeSH term(s)	Aging/metabolism ; Animals ; Animals, Newborn ; Gastrointestinal Tract/blood supply ; Gastrointestinal Tract/growth & development ; Gastrointestinal Tract/metabolism ; Organ Specificity ; Rats ; Rats, Sprague-Dawley ; Receptors, Purinergic P2/metabolism ; Receptors, Purinergic P2X4/metabolism
Chemical Substances	Receptors, Purinergic P2 ; Receptors, Purinergic P2X4 ; purinoceptor P2X6
Language	English
Publishing date	2012-02-16
Publishing country	Ireland
Document type	Journal Article
ZDB-ID	194929-9
ISSN	1872-7972 ; 0304-3940
ISSN (online)	1872-7972
ISSN	0304-3940
DOI	10.1016/j.neulet.2011.12.044
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Article ; Online: Expression of the SNAT2 amino acid transporter during the development of rat cerebral cortex.

Rodríguez, Angelina / Angelina, Rodríguez / Berumen, Laura C / Francisco, Zafra / Giménez, Cecilio / Cecilio, Giménez / García-Alcocer, María Guadalupe / Guadalupe, García-Alcocer María

International journal of developmental neuroscience : the official journal of the International Society for Developmental Neuroscience

2011 Volume 29, Issue 7, Page(s) 743–748

Abstract: The sodium-coupled neutral amino acid transporter 2 (SNAT2) is a protein that is expressed ubiquitously in mammalian tissues and that displays Na(+), voltage and pH dependent activity. This transporter mediates the passage of small zwitterionic amino ... ...

Abstract	The sodium-coupled neutral amino acid transporter 2 (SNAT2) is a protein that is expressed ubiquitously in mammalian tissues and that displays Na(+), voltage and pH dependent activity. This transporter mediates the passage of small zwitterionic amino acids across the cell membrane and regulates the cell homeostasis and its volume. We have examined the expression of SNAT2 mRNA and protein during the development of the rat cerebral cortex, from gestation through the postnatal stages to adulthood. Our data reveal that SNAT2 mRNA and protein expression is higher during embryogenesis, while it subsequently diminishes during postnatal development. Moreover, during embryonic period SNAT2 colocalizes with the radial glial cells marker GLAST, while in postnatal period it is mainly detected in neuronal dendrites. These findings suggest a relevant role for amino acid transport through SNAT2 in the developing embryonic brain.
MeSH term(s)	Amino Acid Transport System A/metabolism ; Amino Acid Transport Systems/genetics ; Amino Acid Transport Systems/metabolism ; Animals ; Cerebral Cortex/anatomy & histology ; Cerebral Cortex/embryology ; Cerebral Cortex/growth & development ; Cerebral Cortex/metabolism ; Excitatory Amino Acid Transporter 1/metabolism ; Female ; Gene Expression Regulation, Developmental ; Pregnancy ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; Rats ; Rats, Sprague-Dawley ; Sodium/metabolism
Chemical Substances	Amino Acid Transport System A ; Amino Acid Transport Systems ; Excitatory Amino Acid Transporter 1 ; RNA, Messenger ; Slc1a3 protein, rat ; Slc38a1 protein, rat ; Slc38a2 protein, rat ; Sodium (9NEZ333N27)
Language	English
Publishing date	2011-06-22
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	605533-3
ISSN	1873-474X ; 0736-5748
ISSN (online)	1873-474X
ISSN	0736-5748
DOI	10.1016/j.ijdevneu.2011.05.010
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