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  1. Article ; Online: Salmonella

    Teafatiller, Trevor / Subramanya, Sandeep B / Lambrecht, Nils / Subramanian, Veedamali S

    Mediators of inflammation

    2023  Volume 2023, Page(s) 2629262

    Abstract: ... ...

    Abstract Salmonella
    MeSH term(s) Humans ; Animals ; Mice ; Ascorbic Acid/metabolism ; Ascorbic Acid/pharmacology ; Salmonella typhimurium/metabolism ; Caco-2 Cells ; NLR Family, Pyrin Domain-Containing 3 Protein ; Intestines ; Salmonella Infections ; Inflammasomes/metabolism ; Cytokines/pharmacology ; RNA, Messenger
    Chemical Substances Ascorbic Acid (PQ6CK8PD0R) ; NLR Family, Pyrin Domain-Containing 3 Protein ; Inflammasomes ; Cytokines ; RNA, Messenger
    Language English
    Publishing date 2023-01-17
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1137605-3
    ISSN 1466-1861 ; 0962-9351
    ISSN (online) 1466-1861
    ISSN 0962-9351
    DOI 10.1155/2023/2629262
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Nedd4-1 regulates human sodium-dependent vitamin C transporter-2 functional expression in neuronal and epithelial cells.

    Teafatiller, Trevor / Perez, Oasis / Kitazawa, Masashi / Agrawal, Anshu / Subramanian, Veedamali S

    The Journal of nutritional biochemistry

    2023  Volume 120, Page(s) 109413

    Abstract: The ubiquitin-proteasomal pathway regulates the functional expression of many membrane transporters in a variety of cellular systems. Nothing is currently known about the role of ubiquitin E3 ligase, neural precursor cell-expressed developmentally down- ... ...

    Abstract The ubiquitin-proteasomal pathway regulates the functional expression of many membrane transporters in a variety of cellular systems. Nothing is currently known about the role of ubiquitin E3 ligase, neural precursor cell-expressed developmentally down-regulated gene 4 (Nedd4-1) and the proteasomal degradation pathway in regulating human vitamin C transporter-2 (hSVCT2) in neuronal cells. hSVCT2 mediates the uptake of ascorbic acid (AA) and is the predominantly expressed vitamin C transporter isoform in neuronal systems. Therefore, we addressed this knowledge gap in our study. Analysis of mRNA revealed markedly higher expression of Nedd4-1 in neuronal samples than that of Nedd4-2. Interestingly, Nedd4-1 expression in the hippocampus was higher in patients with Alzheimer's disease (AD) and age-dependently increased in the J20 mouse model of AD. The interaction of Nedd4-1 and hSVCT2 was confirmed by coimmunoprecipitation and colocalization. While the coexpression of Nedd4-1 with hSVCT2 displayed a significant decrease in AA uptake, siRNA-mediated knockdown of Nedd4-1 expression up-regulated the AA uptake. Further, we mutated a classical Nedd4 protein interacting motif ("PPXY") within the hSVCT2 polypeptide and observed markedly decreased AA uptake due to the intracellular localization of the mutated hSVCT2. Also, we determined the role of the proteasomal degradation pathway in hSVCT2 functional expression in SH-SY5Y cells and the results indicated that the proteasomal inhibitor (MG132) significantly up-regulated the AA uptake and hSVCT2 protein expression level. Taken together, our findings show that the regulation of hSVCT2 functional expression is at least partly mediated by the Nedd4-1 dependent ubiquitination and proteasomal pathways.
    MeSH term(s) Animals ; Humans ; Mice ; Ascorbic Acid/pharmacology ; Ascorbic Acid/metabolism ; Endosomal Sorting Complexes Required for Transport/genetics ; Endosomal Sorting Complexes Required for Transport/metabolism ; Epithelial Cells/metabolism ; Nedd4 Ubiquitin Protein Ligases/genetics ; Nedd4 Ubiquitin Protein Ligases/metabolism ; Neuroblastoma ; Sodium-Coupled Vitamin C Transporters/genetics ; Sodium-Coupled Vitamin C Transporters/metabolism ; Ubiquitin/metabolism ; Ubiquitin-Protein Ligases/genetics ; Ubiquitin-Protein Ligases/metabolism ; Ubiquitination
    Chemical Substances Ascorbic Acid (PQ6CK8PD0R) ; Endosomal Sorting Complexes Required for Transport ; Nedd4 Ubiquitin Protein Ligases (EC 2.3.2.26) ; Sodium-Coupled Vitamin C Transporters ; Ubiquitin ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; SLC23A2 protein, human ; Nedd4 protein, human (EC 2.3.2.26) ; Nedd4 protein, mouse (EC 2.3.2.26)
    Language English
    Publishing date 2023-07-07
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 1014929-6
    ISSN 1873-4847 ; 0955-2863
    ISSN (online) 1873-4847
    ISSN 0955-2863
    DOI 10.1016/j.jnutbio.2023.109413
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Corrigendum to "Metabolites and growth factors produced by Airway epithelial cells induce tolerance in macrophages" [Life Sci. 302 (2022) 120659].

    Agrawal, Sudhanshu / Monteiro, Clarice / Baca, Christian Fredrick / Mohammadi, Rezaa / Subramanian, Veedamali S / de Melo Bento, Cleonice Alves / Agrawal, Anshu

    Life sciences

    2022  Volume 304, Page(s) 120702

    Language English
    Publishing date 2022-06-10
    Publishing country Netherlands
    Document type Published Erratum
    ZDB-ID 3378-9
    ISSN 1879-0631 ; 0024-3205
    ISSN (online) 1879-0631
    ISSN 0024-3205
    DOI 10.1016/j.lfs.2022.120702
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Vitamin C transport in neurons and epithelia is regulated by secretory carrier-associated membrane protein-2 (SCAMP2).

    Rashid, Mohammad A / Lin-Moshier, Yaping / Gunaratne, Gihan S / Subramanian, Sreya / Marchant, Jonathan S / Subramanian, Veedamali S

    International journal of biological macromolecules

    2023  Volume 230, Page(s) 123205

    Abstract: The human sodium-dependent vitamin C transporter-1 (hSVCT1) is localized at the apical membrane domain of polarized intestinal and renal epithelial cells to mediate ascorbic acid (AA) uptake. Currently, little is known about the array of interacting ... ...

    Abstract The human sodium-dependent vitamin C transporter-1 (hSVCT1) is localized at the apical membrane domain of polarized intestinal and renal epithelial cells to mediate ascorbic acid (AA) uptake. Currently, little is known about the array of interacting proteins that aid hSVCT1 trafficking and functional expression at the cell surface. Here we used an affinity tagging ('One-STrEP') and proteomic approach to identify hSVCT1 interacting proteins, which resolved secretory carrier-associated membrane protein-2 (SCAMP2) as a novel accessary protein partner. SCAMP2 was validated as an accessory protein by co-immunoprecipitation with hSVCT1. Co-expression of hSVCT1 and SCAMP2 in HEK-293 cells revealed both proteins co-localized in intracellular structures and at the plasma membrane. Functionally, over-expression of SCAMP2 potentiated
    MeSH term(s) Humans ; HEK293 Cells ; Proteomics ; Cell Membrane/metabolism ; Sodium-Coupled Vitamin C Transporters/genetics ; Sodium-Coupled Vitamin C Transporters/metabolism ; Ascorbic Acid/pharmacology ; Ascorbic Acid/metabolism ; Neurons/metabolism ; Protein Transport ; Carrier Proteins/metabolism ; Membrane Proteins/genetics ; Membrane Proteins/metabolism
    Chemical Substances Sodium-Coupled Vitamin C Transporters ; Ascorbic Acid (PQ6CK8PD0R) ; SCAMP2 protein, human ; Carrier Proteins ; Membrane Proteins
    Language English
    Publishing date 2023-01-09
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 282732-3
    ISSN 1879-0003 ; 0141-8130
    ISSN (online) 1879-0003
    ISSN 0141-8130
    DOI 10.1016/j.ijbiomac.2023.123205
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Vitamin C transport in neurons and epithelia is regulated by secretory carrier-associated membrane protein-2 (SCAMP2)

    Rashid, Mohammad A. / Lin-Moshier, Yaping / Gunaratne, Gihan S. / Subramanian, Sreya / Marchant, Jonathan S. / Subramanian, Veedamali S.

    International Journal of Biological Macromolecules. 2023 Mar., v. 230 p.123205-

    2023  

    Abstract: The human sodium-dependent vitamin C transporter-1 (hSVCT1) is localized at the apical membrane domain of polarized intestinal and renal epithelial cells to mediate ascorbic acid (AA) uptake. Currently, little is known about the array of interacting ... ...

    Abstract The human sodium-dependent vitamin C transporter-1 (hSVCT1) is localized at the apical membrane domain of polarized intestinal and renal epithelial cells to mediate ascorbic acid (AA) uptake. Currently, little is known about the array of interacting proteins that aid hSVCT1 trafficking and functional expression at the cell surface. Here we used an affinity tagging (‘One-STrEP’) and proteomic approach to identify hSVCT1 interacting proteins, which resolved secretory carrier-associated membrane protein-2 (SCAMP2) as a novel accessary protein partner. SCAMP2 was validated as an accessory protein by co-immunoprecipitation with hSVCT1. Co-expression of hSVCT1 and SCAMP2 in HEK-293 cells revealed both proteins co-localized in intracellular structures and at the plasma membrane. Functionally, over-expression of SCAMP2 potentiated ¹⁴C-AA uptake, and reciprocally silencing endogenous SCAMP2 decreased ¹⁴C-AA uptake. Finally, knockdown of endogenous hSVCT1 or SCAMP2 impaired differentiation of human-induced pluripotent stem cells (hiPSCs) toward a neuronal fate. These results establish SCAMP2 as a novel hSVCT1 accessary protein partner that regulates AA uptake in absorptive epithelia and during neurogenesis.
    Keywords ascorbic acid ; epithelium ; humans ; intestines ; neurogenesis ; neurons ; plasma membrane ; precipitin tests ; proteomics ; Vitamin C ; Protein-protein interaction ; Transporter ; hiPSC ; hSVCT1
    Language English
    Dates of publication 2023-03
    Publishing place Elsevier B.V.
    Document type Article ; Online
    ZDB-ID 282732-3
    ISSN 1879-0003 ; 0141-8130
    ISSN (online) 1879-0003
    ISSN 0141-8130
    DOI 10.1016/j.ijbiomac.2023.123205
    Database NAL-Catalogue (AGRICOLA)

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  6. Article ; Online: Valproic acid upregulates sodium-dependent vitamin C transporter-2 functional expression in neuronal cells.

    Teafatiller, Trevor / Subramanian, Sreya / Marquez, Felerico E / Kitazawa, Masashi / Subramanian, Veedamali S

    Life sciences

    2022  Volume 308, Page(s) 120944

    Abstract: ... the functional expression of SVCT2 via HDAC2 and transcriptional mechanism(s). ...

    Abstract Neuronal uptake of ascorbic acid (AA) in humans occurs via the human sodium-dependent vitamin C transporter-2 (hSVCT2). Recent studies show that a significantly lower level of vitamin C is present in the blood of epileptic patients. Consequently, focused studies investigating the involved molecular mechanisms for hSVCT2 regulation are vital to enhance vitamin C body homeostasis. Currently, little is known about the role of valproic acid (VPA), a drug utilized to treat epilepsy and a class I histone deacetylase inhibitor (HDACi), on AA uptake in neuronal systems. Thus, this study aims to examine the effect of VPA on hSVCT2 functional expression in neuronal cells. VPA treatment upregulated the AA uptake and this increased AA uptake was associated with a significant increase in hSVCT2 expression and SLC23A2 promoter activity in SH-SY5Y cells. Knockdown of HDAC2, a predominant isoform in neuronal systems, significantly increased hSVCT2 functional expression. VPA treatment in mice displayed increased mouse (m)SVCT2 protein, mRNA and heterogenous nuclear RNA (hnRNA) expression in the brain. In addition, Yin Yang-1 (YY1), a transcription factor that drives the SLC23A2 promoter activity, protein and mRNA expression levels were markedly upregulated in VPA-treated SH-SY5Y cells and mice brain. Together, our findings suggest that VPA upregulates the functional expression of SVCT2 via HDAC2 and transcriptional mechanism(s).
    MeSH term(s) Animals ; Ascorbic Acid/pharmacology ; Histone Deacetylase Inhibitors/pharmacology ; Humans ; Mice ; Neuroblastoma ; Protein Isoforms/metabolism ; RNA, Heterogeneous Nuclear ; RNA, Messenger/genetics ; Sodium-Coupled Vitamin C Transporters/genetics ; Sodium-Coupled Vitamin C Transporters/metabolism ; Transcription Factors/metabolism ; Valproic Acid/pharmacology ; Vitamins
    Chemical Substances Histone Deacetylase Inhibitors ; Protein Isoforms ; RNA, Heterogeneous Nuclear ; RNA, Messenger ; Sodium-Coupled Vitamin C Transporters ; Transcription Factors ; Vitamins ; Valproic Acid (614OI1Z5WI) ; Ascorbic Acid (PQ6CK8PD0R)
    Language English
    Publishing date 2022-09-10
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 3378-9
    ISSN 1879-0631 ; 0024-3205
    ISSN (online) 1879-0631
    ISSN 0024-3205
    DOI 10.1016/j.lfs.2022.120944
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  7. Article: Valproic acid upregulates sodium-dependent vitamin C transporter-2 functional expression in neuronal cells

    Teafatiller, Trevor / Subramanian, Sreya / Marquez, Felerico E. / Kitazawa, Masashi / Subramanian, Veedamali S.

    Life sciences. 2022 Nov. 01, v. 308

    2022  

    Abstract: ... the functional expression of SVCT2 via HDAC2 and transcriptional mechanism(s). ...

    Abstract Neuronal uptake of ascorbic acid (AA) in humans occurs via the human sodium-dependent vitamin C transporter-2 (hSVCT2). Recent studies show that a significantly lower level of vitamin C is present in the blood of epileptic patients. Consequently, focused studies investigating the involved molecular mechanisms for hSVCT2 regulation are vital to enhance vitamin C body homeostasis. Currently, little is known about the role of valproic acid (VPA), a drug utilized to treat epilepsy and a class I histone deacetylase inhibitor (HDACi), on AA uptake in neuronal systems. Thus, this study aims to examine the effect of VPA on hSVCT2 functional expression in neuronal cells. VPA treatment upregulated the AA uptake and this increased AA uptake was associated with a significant increase in hSVCT2 expression and SLC23A2 promoter activity in SH-SY5Y cells. Knockdown of HDAC2, a predominant isoform in neuronal systems, significantly increased hSVCT2 functional expression. VPA treatment in mice displayed increased mouse (m)SVCT2 protein, mRNA and heterogenous nuclear RNA (hnRNA) expression in the brain. In addition, Yin Yang-1 (YY1), a transcription factor that drives the SLC23A2 promoter activity, protein and mRNA expression levels were markedly upregulated in VPA-treated SH-SY5Y cells and mice brain. Together, our findings suggest that VPA upregulates the functional expression of SVCT2 via HDAC2 and transcriptional mechanism(s).
    Keywords RNA ; ascorbic acid ; blood ; brain ; epilepsy ; gene expression ; histone deacetylase ; homeostasis ; humans ; mice ; neurons ; transcription (genetics) ; transcription factors ; valproic acid
    Language English
    Dates of publication 2022-1101
    Publishing place Elsevier Inc.
    Document type Article
    ZDB-ID 3378-9
    ISSN 1879-0631 ; 0024-3205
    ISSN (online) 1879-0631
    ISSN 0024-3205
    DOI 10.1016/j.lfs.2022.120944
    Database NAL-Catalogue (AGRICOLA)

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  8. Article ; Online: Histone deacetylase inhibitors regulate vitamin C transporter functional expression in intestinal epithelial cells.

    Subramanian, Veedamali S / Teafatiller, Trevor / Moradi, Hamid / Marchant, Jonathan S

    The Journal of nutritional biochemistry

    2021  Volume 98, Page(s) 108838

    Abstract: Intestinal absorption of vitamin C in humans is mediated via the sodium-dependent vitamin C transporters (hSVCT1 and hSVCT2). hSVCT1 and hSVCT2 are localized at the apical and basolateral membranes, respectively, of polarized intestinal epithelia. ... ...

    Abstract Intestinal absorption of vitamin C in humans is mediated via the sodium-dependent vitamin C transporters (hSVCT1 and hSVCT2). hSVCT1 and hSVCT2 are localized at the apical and basolateral membranes, respectively, of polarized intestinal epithelia. Studies have identified low plasma levels of vitamin C and decreased expression of hSVCT1 in patients with several inflammatory conditions including inflammatory bowel disease (IBD). Investigating the underlying mechanisms responsible for regulating hSVCT1 expression are critical for understanding vitamin C homeostasis, particularly in conditions where suboptimal vitamin C levels detrimentally affect human health. Previous research has shown that hSVCT1 expression is regulated at the transcriptional level, however, little is known about epigenetic regulatory pathways that modulate hSVCT1 expression in the intestine. In this study, we found that hSVCT1 expression and function were significantly decreased in intestinal epithelial cells by the histone deacetylase inhibitors (HDACi), valproic acid (VPA), and sodium butyrate (NaB). Further, expression of transcription factor HNF1α, which is critical for SLC23A1 promoter activity, was significantly down regulated in VPA-treated cells. Chromatin immunoprecipitation (ChIP) assays showed significantly increased enrichment of tetra-acetylated histone H3 and H4 within the SLC23A1 promoter following VPA treatment. In addition, knockdown of HDAC isoforms two, and three significantly decreased hSVCT1 functional expression. Following VPA administration to mice, functional expression of SVCT1 in the jejunum was significantly decreased. Collectively, these in vitro and in vivo studies demonstrate epigenetic regulation of SVCT1 expression in intestinal epithelia partly mediated through HDAC isoforms two and three.
    MeSH term(s) Acetylation ; Animals ; Ascorbic Acid/metabolism ; Butyric Acid/pharmacology ; Caco-2 Cells ; Epigenesis, Genetic ; Epithelial Cells/metabolism ; Histone Deacetylase Inhibitors/metabolism ; Histone Deacetylase Inhibitors/pharmacology ; Humans ; Intestinal Mucosa/metabolism ; Jejunum/metabolism ; Mice ; Mice, Inbred BALB C ; Promoter Regions, Genetic/drug effects ; RNA, Small Interfering/metabolism ; Sodium-Coupled Vitamin C Transporters/genetics ; Sodium-Coupled Vitamin C Transporters/metabolism ; Valproic Acid/pharmacology
    Chemical Substances Histone Deacetylase Inhibitors ; RNA, Small Interfering ; Sodium-Coupled Vitamin C Transporters ; Butyric Acid (107-92-6) ; Valproic Acid (614OI1Z5WI) ; Ascorbic Acid (PQ6CK8PD0R)
    Language English
    Publishing date 2021-08-14
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 1014929-6
    ISSN 1873-4847 ; 0955-2863
    ISSN (online) 1873-4847
    ISSN 0955-2863
    DOI 10.1016/j.jnutbio.2021.108838
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Cis-Nerolidol Inhibits MAP Kinase and NF-κB Signaling Pathways and Prevents Epithelial Tight Junction Dysfunction in Colon Inflammation: In Vivo and In Vitro Studies.

    Raj, Vishnu / Venkataraman, Balaji / Ojha, Shreesh K / Almarzooqi, Saeeda / Subramanian, Veedamali S / Al-Ramadi, Basel K / Adrian, Thomas E / Subramanya, Sandeep B

    Molecules (Basel, Switzerland)

    2023  Volume 28, Issue 7

    Abstract: Inflammation of the GI tract leads to compromised epithelial barrier integrity, which increases intestine permeability. A compromised intestinal barrier is a critical event that leads to microbe entry and promotes inflammatory responses. Inflammatory ... ...

    Abstract Inflammation of the GI tract leads to compromised epithelial barrier integrity, which increases intestine permeability. A compromised intestinal barrier is a critical event that leads to microbe entry and promotes inflammatory responses. Inflammatory bowel diseases that comprise Crohn's disease (CD) and ulcerative colitis (UC) show an increase in intestinal permeability. Nerolidol (NED), a naturally occurring sesquiterpene alcohol, has potent anti-inflammatory properties in preclinical models of colon inflammation. In this study, we investigated the effect of NED on MAPKs, NF-κB signaling pathways, and intestine epithelial tight junction physiology using in vivo and in vitro models. The effect of NED on proinflammatory cytokine release and MAPK and NF-κB signaling pathways were evaluated using lipopolysaccharides (LPS)-stimulated RAW 264.7 macrophages. Subsequently, the role of NED on MAPKs, NF-κB signaling, and the intestine tight junction integrity were assessed using DSS-induced colitis and LPS-stimulated Caco-2 cell culture models. Our result indicates that NED pre-treatment significantly inhibited proinflammatory cytokine release, expression of proteins involved in MAP kinase, and NF-κB signaling pathways in LPS-stimulated RAW macrophages and DSS-induced colitis. Furthermore, NED treatment significantly decreased FITC-dextran permeability in DSS-induced colitis. NED treatment enhanced tight junction protein expression (claudin-1, 3, 7, and occludin). Time-dependent increases in transepithelial electrical resistance (TEER) measurements reflect the formation of healthy tight junctions in the Caco-2 monolayer. LPS-stimulated Caco-2 showed a significant decrease in TEER. However, NED pre-treatment significantly prevented the fall in TEER measurements, indicating its protective role. In conclusion, NED significantly decreased MAPK and NF-κB signaling pathways and decreased tight junction permeability by enhancing epithelial tight junction protein expression.
    MeSH term(s) Humans ; NF-kappa B/metabolism ; Tight Junctions/metabolism ; Caco-2 Cells ; Lipopolysaccharides/pharmacology ; Intestinal Mucosa/metabolism ; Signal Transduction ; Colitis/chemically induced ; Colitis/drug therapy ; Colitis/metabolism ; Sesquiterpenes/pharmacology ; Tight Junction Proteins/metabolism ; Mitogen-Activated Protein Kinases/metabolism ; Inflammation/drug therapy ; Inflammation/metabolism ; Cytokines/metabolism ; Dextran Sulfate/adverse effects
    Chemical Substances NF-kappa B ; nerolidol (QR6IP857S6) ; Lipopolysaccharides ; Sesquiterpenes ; Tight Junction Proteins ; Mitogen-Activated Protein Kinases (EC 2.7.11.24) ; Cytokines ; Dextran Sulfate (9042-14-2)
    Language English
    Publishing date 2023-03-27
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 1413402-0
    ISSN 1420-3049 ; 1431-5165 ; 1420-3049
    ISSN (online) 1420-3049
    ISSN 1431-5165 ; 1420-3049
    DOI 10.3390/molecules28072982
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  10. Article ; Online: Effect of Lipopolysaccharide and TNF

    Subramanian, Veedamali S / Teafatiller, Trevor / Agrawal, Anshu / Kitazawa, Masashi / Marchant, Jonathan S

    Mediators of inflammation

    2021  Volume 2021, Page(s) 4157132

    Abstract: Vitamin C (ascorbic acid: AA) uptake in neurons occurs via the sodium-dependent vitamin C transporter-2 (SVCT2), which is highly expressed in the central nervous system (CNS). During chronic neuroinflammation or infection, CNS levels of ... ...

    Abstract Vitamin C (ascorbic acid: AA) uptake in neurons occurs via the sodium-dependent vitamin C transporter-2 (SVCT2), which is highly expressed in the central nervous system (CNS). During chronic neuroinflammation or infection, CNS levels of lipopolysaccharide (LPS) and LPS-induced tumor necrosis factor-
    MeSH term(s) Animals ; Ascorbic Acid/metabolism ; Ascorbic Acid/pharmacology ; Lipopolysaccharides/metabolism ; Lipopolysaccharides/pharmacology ; Mice ; Neurons/metabolism ; Sodium-Coupled Vitamin C Transporters/genetics ; Sodium-Coupled Vitamin C Transporters/metabolism ; Tumor Necrosis Factor-alpha/metabolism
    Chemical Substances Lipopolysaccharides ; Sodium-Coupled Vitamin C Transporters ; Tumor Necrosis Factor-alpha ; Ascorbic Acid (PQ6CK8PD0R)
    Language English
    Publishing date 2021-07-03
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1137605-3
    ISSN 1466-1861 ; 0962-9351
    ISSN (online) 1466-1861
    ISSN 0962-9351
    DOI 10.1155/2021/4157132
    Database MEDical Literature Analysis and Retrieval System OnLINE

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