Journal: Redox Biology

Article Title: SARS-CoV-2 mitochondriopathy in COVID-19 pneumonia exacerbates hypoxemia

doi: 10.1016/j.redox.2022.102508

Figure Lengend Snippet: SARS-CoV-2 infection of Calu-3 human AEC causes mitochondrial fission. A) Calu-3 cells were infected with SARS-CoV-2 for 72 h and then loaded with TMRM, revealing mitochondrial structure (red), and DAPI, identifying the nucleus (blue). Infection causes mitochondrial fission, evident as mitochondrial fragmentation. Scale bar = 10 μm. B–C) Mitochondrial fission was quantified by machine learning, which uses an algorithm to automatically categorize and colour code mitochondria as punctate, intermediate, or filamentous, as described . Quantitative analysis shows that SARS-CoV-2 significantly increases the percentage area of punctate mitochondria and reduces the number of filamentous mitochondria. (**** P < 0.0001; n = 21 cells/group). D-E) Confocal imaging shows increased expression of activated and total Drp1 48 -h post SARS-CoV-2 infection. Tomm 20 is used to image the mitochondria (red) with p-Drp1 S616 and Drp1 imaged in green. Scale bar = 2–15 μm. Representative images (i), 400% zoom (ii) and mean data (iii) are shown. (*** P < 0.001 n = 5/group). The mean data in panel iii derive from analysis of the low power images (Di and Ei). Note the increase in p-Drp1 S616 primarily occurs in the mitochondria, seen as increased yellow (from red/green colocalization in low power images, Di) and seen directly on high power STED images (Dii), with most green p-Drp1 S616 localizing to the mitochondrial outer membrane, F–I) Immunoblot confirms that SARS-CoV-2 infection increases the expression of activated Drp1, increases the expression of the apoptosis mediator AIF and activates caspase 7. (F) Marked increase in SASR-CoV-2 N protein expression only in infected cells confirms infection. The Calu-3 cells were harvested for immunoblot analyses after 48 h of infection with SARs-C0V-2. Representative image of the immunoblots and the densitometry of the expressions of (G) p-Drp1 ser616 , (H) AIF and (I) cleaved caspase 7. (* P < 0.05; ** P < 0.01; n = 3–5 technical replicates/group).

Article Snippet: Antibodies against cleaved caspase 7 (9491), caspase 7 (12827), SARS-CoV2 N-protein (33717), AIF (5318), p-Drp1 (ser616) (3455), Smac/Diablo (15108), Caspase 1(2225) and Bid (2002) were purchased from Cell Signaling Technology (Beverly, MA, USA).

Techniques: Infection, Imaging, Expressing, Western Blot

Journal: Redox Biology

Article Title: SARS-CoV-2 mitochondriopathy in COVID-19 pneumonia exacerbates hypoxemia

doi: 10.1016/j.redox.2022.102508

Figure Lengend Snippet: HCoV-OC43 infection increases expression of apoptosis mediators and reduces oxidative metabolism in BEAS-2B cells and causes mitochondrial fission in HPAEC Assessment of the effects of HCoV-OC43 infection of BEAS-2B cells and HPAEC occurred at 72 h post infection. A) HCoV-OC43 infection increases expression of apoptosis and mitochondrial fission mediators in BEAS-2B cells. Representative immunoblots and densitometry i) confirming infection with HCoV-OC43 (inset showing viral N-protein only in infected cells). Infection of human AEC upregulates ii) mediators of mitochondrial fission (total and activated Drp1, p-Drp1 S616 ). iii) downregulates CDK4, a cyclin dependent kinase responsible for cell cycle progression. iv-vii) upregulates apoptosis mediators (Smac/Diablo, Caspase 1, Bid, and AIF). * P < 0.05; ** P < 0.01; *** P < 0.001; n = 3/group. viii) Using STED microscopy at 50 nm resolution, coronavirus HCov-OC43 (green; nucleoprotein-targeted antibody) colocalizes with AIF (yellow) on the mitochondrial outer membrane (red) in AEC; AIF expression is also increased in infected cells (bottom) versus mock cells in these images (top), as in the immunoblot (vii). Scale bar = 1–5 μm B) HCoV-OC43 infection inhibits oxidative metabolism and increases mitochondrial fission in BEAS-2B cells i-iv) Infection of human AEC with HCoV-OC43, inhibits basal and FCCP-stimulated maximal respiration and ATP-linked OCR, as measured by micropolarimetry. * P < 0.05; n = 5/group. v) Infection with HCoV-OC43 reduces ATP concentration in BEAS-2B cells. * P < 0.05; n = 9/group. vi) Infection with HCoV-OC43 inhibits ETC Complex I activity in BEAS-2B cells. *** P < 0.001; n = 5/group. vii-viii) TEM shows that mitochondria in infected cells are more swollen with increased intercristal space. **** P < 0.0001; n = 39 mitochondria/group. ix) TEM shows HCoV-OC43 virus in an intracellular vesicle. C) HCoV-OC43 fragments mitochondria in HPAEC. Infection of HPAEC with HCoV-OC43 causes mitochondrial fission (more punctate mitochondria in infected cells on right vs control cells on left). The mitochondrial network is red (loaded with the potentiometric dye tetra methylrhodamine, TMRM). We used machine learning to allow a computer algorithm to classify mitochondria as punctate, intermediate, or filamentous, as described . Infection increases the percentage area of intermediate and punctate mitochondria, consistent with induction of mitochondrial fission. ** P < 0.01, **** P < 0.0001; n = 20 cells/group.

Article Snippet: Antibodies against cleaved caspase 7 (9491), caspase 7 (12827), SARS-CoV2 N-protein (33717), AIF (5318), p-Drp1 (ser616) (3455), Smac/Diablo (15108), Caspase 1(2225) and Bid (2002) were purchased from Cell Signaling Technology (Beverly, MA, USA).

Techniques: Infection, Expressing, Western Blot, Microscopy, Concentration Assay, Activity Assay

Journal: Scientific Reports

Article Title: PhagoStat a scalable and interpretable end to end framework for efficient quantification of cell phagocytosis in neurodegenerative disease studies

doi: 10.1038/s41598-024-56081-7

Figure Lengend Snippet: Efficient data loading and normalization pipeline. ( a ) Detailed steps of the data loading and normalization module where: the two channels (aggregates and cells) are extracted directly from the microscope raw data, then it applies the local and global normalization to standardize the data. ( b ) High performance computing (HPC) cluster compatible scheme that scales to big datasets. ( c ) Quantitative comparison of our single-CPU/multi-CPU method and the GPU-accelerated Carl Zeiss ZEN software when processing 76GB CZI file (raw data). To facilitate direct comparison, ‘Frame input and output’ times are the combination of “read and write” times for all systems. As an insight, our method’s time allocation for SSDs (25% reading and 75% saving) and HDDs (76.6% reading and 23.3% saving).

Article Snippet: Our module was tested on converting Carl Zeiss Image (CZI) files to TIFF format, and it is compatible with Windows, macOS, and Unix.

Techniques: Microscopy, Comparison, Software

Journal: Oral Diseases

Article Title: Significance of chlorine‐dioxide‐based oral rinses in preventing SARS‐CoV ‐2 cell entry

doi: 10.1111/odi.14319

Figure Lengend Snippet: Effect of oral rinses (ORs) on SARS‐CoV‐2 cell entry using quantitative luciferase reporter‐based pseudovirus assay. In this experiment, the SARS‐CoV‐2 pseudovirus was pre‐incubated with each OR for 5 min and then transduced to HEK293T‐ACE2 cells for 48 h at 37°C. The dosage‐dependent treatment was performed in triplicate experiment using 100%–12.5% concentrations of either CloSYS (a) or OraCare (b). The HEK293T‐ACE2 cells transduced with the untreated SARS‐CoV‐2 pseudovirus were considered as a positive control (+), while the un‐transduced HEK293T‐ACE2 cells were considered as a negative control (−). Asterisks (****) indicate a significant difference between the positive control and the cells infected with OR‐treated pseudovirus ( p < .0001)

Article Snippet: The mammalian expression plasmid encoding SARS‐CoV‐2 spike glycoprotein of 2019‐nCoV (Cat # VG40589‐UT, VG40589‐ACG) and human ACE2 receptor (Cat # HG10108‐UT, HG10108‐ACR) were purchased from Sino Biological (Wayne, PA, USA).

Techniques: Luciferase, Incubation, Transduction, Positive Control, Negative Control, Infection

Journal: Oral Diseases

Article Title: Significance of chlorine‐dioxide‐based oral rinses in preventing SARS‐CoV ‐2 cell entry

doi: 10.1111/odi.14319

Figure Lengend Snippet: Confocal imaging of HEK293T‐ACE2 cells transduced with GFP expressing SARS‐CoV‐2 pseudovirus in the presence and absence of the ORs. In this experiment, GFP‐tagged SARS‐CoV‐2 pseudovirus was pretreated for 5 min with 50% dilution of ORs or mock (PBS)‐treated at room temperature before introducing the cocktail to the cultured HEK293T‐ACE2 cells. Shown are the representative images of GFP positive control cells transduced with SARS‐CoV‐2 in the absence of ORs (a), the mock un‐transduced GFP‐negative control cells (b), and the HEK293T‐ACE2 cells transduced with green fluorescent protein (GFP)‐tagged baculovirus pseudotyped SARS‐CoV‐2, which was pretreated with ORs (CloSYS; [c] and or with OraCare; [d]; at 50% dilution). The fixed HEK293T‐ACE2 cells were finally stained with red‐phalloidin for cell background. The SARS‐CoV‐2 pseudovirus generated a sharp green punctate signal was an indicator for successful viral entry into target cells (a). Confocal imaging was performed in triplicate experiment using Nikon A1R confocal microscope

Article Snippet: The mammalian expression plasmid encoding SARS‐CoV‐2 spike glycoprotein of 2019‐nCoV (Cat # VG40589‐UT, VG40589‐ACG) and human ACE2 receptor (Cat # HG10108‐UT, HG10108‐ACR) were purchased from Sino Biological (Wayne, PA, USA).

Techniques: Imaging, Transduction, Expressing, Cell Culture, Positive Control, Negative Control, Staining, Generated, Microscopy

Journal: Oral Diseases

Article Title: Significance of chlorine‐dioxide‐based oral rinses in preventing SARS‐CoV ‐2 cell entry

doi: 10.1111/odi.14319

Figure Lengend Snippet: (a,b) Quantification of luciferase signal generated after co‐culturing the SARS‐CoV‐2 spike glycoprotein expressing effector cell with the target cells expressing the human ACE‐2 receptor in the presence and absence of the ORs. In this experiment, effector CHO‐K1 cells co‐transfected with SARS‐CoV‐2 spike glycoprotein with T7 RNA polymerase. In parallel, target CHO‐K1 cells were co‐transfected with human ACE2 expression plasmid and luciferase gene. Both the effector and target cell were mixed and co‐cultured for additional 24 h before measuring the luciferase activity. Effector cells were pre‐incubated with the CloSYS (a) or OralCare (b) in a dosage‐dependent manner before mixing the effector cells with the target cells. Asterisks (****) indicate a significant difference between the positive control and the ORs treated cells ( p < .0001). (c) Expression of SARS‐CoV‐2 spike glycoprotein, human ACE‐2 receptor, in the effector and target cell respectively. The post‐co‐culture event demonstrating the co‐localization and the formation of multinucleated giant cell (syncytia) using confocal imaging. In this experiment, CHO‐K1 effector and target cells independently transfected with GFP‐tagged SARS‐CoV‐2 (panel i), and or RFP‐tagged human ACE‐2 receptor (panel ii) respectively. A GFP‐positive spike glycoprotein expressing effector cell co‐cultured with RFP‐positive ACE‐2 expressing target cells imaged 24 h post‐mixing shows co‐localization and the formation of multinucleated giant cell (syncytia; panel iii). Confocal microscopy was performed in triplicate using Nikon A1R confocal microscope

Article Snippet: The mammalian expression plasmid encoding SARS‐CoV‐2 spike glycoprotein of 2019‐nCoV (Cat # VG40589‐UT, VG40589‐ACG) and human ACE2 receptor (Cat # HG10108‐UT, HG10108‐ACR) were purchased from Sino Biological (Wayne, PA, USA).

Techniques: Luciferase, Generated, Expressing, Transfection, Plasmid Preparation, Cell Culture, Activity Assay, Incubation, Positive Control, Co-Culture Assay, Imaging, Confocal Microscopy, Microscopy

Journal: Journal of Molecular and Cellular Cardiology

Article Title: Angiotensin peptide synthesis and cyclic nucleotide modulation in sympathetic stellate ganglia

doi: 10.1016/j.yjmcc.2019.11.157

Figure Lengend Snippet: Angiotensin synthesizing enzymes and precursors are expressed in human stellate ganglia. In human stellate ganglia the presence of the mRNA transcripts encoding Agt ( n = 4), Ren ( n = 3) , Ace (n = 4) , Ace2 (n = 3) , Agtr1 (n = 4) , Agtr2 (n = 3) and Mas1 (n = 4) were confirmed by qRT-PCR. The qRT-PCR raw counts for the genes of interest were normalized to the control gene B2m using the ∆C T method and expressed as ∆C T mean ± SEM (a). ELISAs were used to demonstrate the protein expression of the relevant proteins of interest including Agt, Ren, AngII, ACE2 and Ang1–7 in human stellate ganglia. Agt was found to be highly expressed in human stellate ganglia ( n = 2, ~53,694 pg/mg), as was Ren (n = 3, 2005 ± 388 pg/mg). AngII (n = 3, 188.7 ± 15.37 pg/mg), ACE2 (n = 2, 171.9 ± 2.60 pg/mg) and Ang1–7 (n = 3, 179.9 ± 6.13 pg/mg) were also identified and were found to have similar levels of expression (b). Data are displayed as mean ± SEM. A model diagram depicts AngII and Ang1–7 release from the stellate ganglia and the proposed pre-and post-synaptic effects.

Article Snippet: Two-step qRT-PCR was used to confirm the presence of the following mRNA transcripts in the stellate ganglia cDNA libraries: angiotensinogen (AGT, Agt; Rn00593114_m1, Hs01586213_m1; rat, human respectively), renin ( Ren ; Rn00561847_m1, Hs00982555_m1; rat, human), angiotensin converting enzyme (ACE, Ace, Rn00561094_m1, Hs00174179_m1; rat, human), angiotensin converting enzyme type 2 (ACE2, Ace2 ; Rn01416293_m1, Hs01085333_m1; rat, human), angiotensin II receptor subtype 1a (AT 1A R, Agtr1a ; Rn02758772_s1; rat), angiotensin II receptor subtype 1b (AT 1B R, Agtr1b ; Rn02132799_s1; rat), angiotensin II receptor type 1 (AT 1 R, Agtr1 ; Hs00258938_m1; human), angiotensin II receptor type 2 (AT 2 R, Agtr2 ; Rn00560677_s1, Hs02621316_s1; rat, human), Mas receptor (Mas R, Mas1 ; Rn00562673_s1, Hs00267157_s1; rat, human).

Techniques: Quantitative RT-PCR, Control, Expressing

Journal: Journal of Molecular and Cellular Cardiology

Article Title: Angiotensin peptide synthesis and cyclic nucleotide modulation in sympathetic stellate ganglia

doi: 10.1016/j.yjmcc.2019.11.157

Figure Lengend Snippet: Transcripts of angiotensin synthesizing genes were observed in the rat sympathetic stellate ganglia in the RNA-seq dataset. The transcriptome of the sympathetic stellate ganglia was sequenced using stellate ganglia extracted from four-week-old male Wistar rats ( n = 5) and age-matched male prehypertensive SHR (preSHR, n = 5). A KEGG analysis was carried out using the differentially expressed transcripts where the gene input was selected using the Benjamini-Hochburg p.adj < 0.05. The KEGG group ‘Renin Secretion’ was found to be significantly altered in the preSHR ganglia, where the gene input was selected using the Benjamini-Hochburg p.adj < 0.05 (a). A full list of the genes, the fold changes and respective levels of significance are reported in . The AngII and Ang1–7 synthesis pathways are outlined (b). Transcripts encoding the enzymes and precursors classically involved in the synthesis of AngII and Ang1–7 were identified in young rat stellate ganglia (b), where the relevant transcripts included Angiotensinogen ( Agt), Renin ( Ren ) and the Angiotensin Converting Enzymes ( Ace, Ace2 ). The transcripts for AngII receptors type 1 and 2 ( Agtr1a, Agtr1b, Agtr2) and for the Ang1–7 receptor Mas ( M as1 ) were also observed (c). Transcript abundances were not found to be differentially expressed in preSHR vs. Wistar ganglia, with the exception of Agtr1a that was significantly downregulated in the preSHR stellate ganglia (p. adj = 3.72 × 10 −8 , Salmon-DESeq2 method [ , ]).

Article Snippet: Two-step qRT-PCR was used to confirm the presence of the following mRNA transcripts in the stellate ganglia cDNA libraries: angiotensinogen (AGT, Agt; Rn00593114_m1, Hs01586213_m1; rat, human respectively), renin ( Ren ; Rn00561847_m1, Hs00982555_m1; rat, human), angiotensin converting enzyme (ACE, Ace, Rn00561094_m1, Hs00174179_m1; rat, human), angiotensin converting enzyme type 2 (ACE2, Ace2 ; Rn01416293_m1, Hs01085333_m1; rat, human), angiotensin II receptor subtype 1a (AT 1A R, Agtr1a ; Rn02758772_s1; rat), angiotensin II receptor subtype 1b (AT 1B R, Agtr1b ; Rn02132799_s1; rat), angiotensin II receptor type 1 (AT 1 R, Agtr1 ; Hs00258938_m1; human), angiotensin II receptor type 2 (AT 2 R, Agtr2 ; Rn00560677_s1, Hs02621316_s1; rat, human), Mas receptor (Mas R, Mas1 ; Rn00562673_s1, Hs00267157_s1; rat, human).

Techniques: RNA Sequencing

Journal: Journal of Molecular and Cellular Cardiology

Article Title: Angiotensin peptide synthesis and cyclic nucleotide modulation in sympathetic stellate ganglia

doi: 10.1016/j.yjmcc.2019.11.157

Figure Lengend Snippet: Angiotensinergic mRNA transcript validation by qRT-PCR in rat stellate ganglia. The presence of the RNA transcripts Agt, Ren, Ace, Ace2, Agtr1a, Agtr1b, Agtr2 and Mas1 was confirmed by qRT-PCR in sympathetic stellate ganglia from four-week Wistar and preSHR ganglia (a), and 16-week adult Wistar and SHR (b). The qRT-PCR raw counts were first normalized to a control gene B2m as per the comparative (∆C T ) method . Each data point corresponds to one stellate RNA sample from one rat. Data are displayed as ∆C T mean ± SEM. FRET microscopy was conducted on sympathetic stellate neurons obtained from Wistar ( n = 11 rats, 3 cultures, 20 cells) and preSHR rats ( n = 9 rats, 3 cultures, 19 cells). Cells were transduced with the cGi500 FRET sensor and randomly selected for imaging. Increases in cGMP generation was observed in sympathetic neurons in response to Ang1–7 and AngII (c, d). Maximal FRET changes were evoked following administration of a combination of the NO-donor Sin-1 (10 μM) and the PDE inhibitor IBMX (100 μM). There was significantly greater cGMP generation in response to AngII in Wistar vs. preSHR neurons (two-way ANOVA, p = .0403). Peak FRET changes were obtained in response to AngII or Ang1–7 and converted to percentage FRET changes and values are depicted as a proportion of the maximal FRET change (%). There was no difference in peak FRET responses in response to Ang1–7 or between strains (d). Data are displayed as mean ± SEM.

Article Snippet: Two-step qRT-PCR was used to confirm the presence of the following mRNA transcripts in the stellate ganglia cDNA libraries: angiotensinogen (AGT, Agt; Rn00593114_m1, Hs01586213_m1; rat, human respectively), renin ( Ren ; Rn00561847_m1, Hs00982555_m1; rat, human), angiotensin converting enzyme (ACE, Ace, Rn00561094_m1, Hs00174179_m1; rat, human), angiotensin converting enzyme type 2 (ACE2, Ace2 ; Rn01416293_m1, Hs01085333_m1; rat, human), angiotensin II receptor subtype 1a (AT 1A R, Agtr1a ; Rn02758772_s1; rat), angiotensin II receptor subtype 1b (AT 1B R, Agtr1b ; Rn02132799_s1; rat), angiotensin II receptor type 1 (AT 1 R, Agtr1 ; Hs00258938_m1; human), angiotensin II receptor type 2 (AT 2 R, Agtr2 ; Rn00560677_s1, Hs02621316_s1; rat, human), Mas receptor (Mas R, Mas1 ; Rn00562673_s1, Hs00267157_s1; rat, human).

Techniques: Biomarker Discovery, Quantitative RT-PCR, Control, Microscopy, Transduction, Imaging

Journal: Journal of Molecular and Cellular Cardiology

Article Title: Angiotensin peptide synthesis and cyclic nucleotide modulation in sympathetic stellate ganglia

doi: 10.1016/j.yjmcc.2019.11.157

Figure Lengend Snippet: Model diagram depicts angiotensin synthesis and pre- and post-synaptic signaling pathways. In sympathetic stellate neurons, the classical pathway for Angiotensin II (AngII) synthesis occurs by sequential enzymatic cleavage of Angiotensinogen (Agt) by renin and Angiotensin Converting Enzymes (ACE). AngII is hydrolyzed by ACE2 producing the bioactive metabolite of Angiotensin 1–7 (Ang1–7). We identified the presence of precursors and transcripts encoding these enzymes and depict here a proposed model for angiotensin synthesis (a). We also identified the presence of AngII and Ang1–7 receptors on sympathetic stellate ganglia of human and rat. AngII has been shown to elevate intracellular Ca 2+ and enhance noradrenaline release via actions at AT 1 R [ , ]. Conversely Ang1–7-dependent activation of its cognate receptor, Mas R, has been shown to couple to NO in the brain and several other receptor sites . In this study, we show that administration of both AngII and Ang1–7 elevate cGMP in the rat stellate ganglia. We and others have previously demonstrated the importance of NO-cGMP signaling in reducing [Ca 2+ ] i [ , ] and end-organ transmission in peripheral sympathetic stellate nerves [ , , , ] although the effects of Ang1–7 may be biphasic . Dotted lines indicate intermediates in these intracellular signaling pathway. Several effects of AngII and Ang1–7 on the myocardium have been established [ , , , , , ].

Article Snippet: Two-step qRT-PCR was used to confirm the presence of the following mRNA transcripts in the stellate ganglia cDNA libraries: angiotensinogen (AGT, Agt; Rn00593114_m1, Hs01586213_m1; rat, human respectively), renin ( Ren ; Rn00561847_m1, Hs00982555_m1; rat, human), angiotensin converting enzyme (ACE, Ace, Rn00561094_m1, Hs00174179_m1; rat, human), angiotensin converting enzyme type 2 (ACE2, Ace2 ; Rn01416293_m1, Hs01085333_m1; rat, human), angiotensin II receptor subtype 1a (AT 1A R, Agtr1a ; Rn02758772_s1; rat), angiotensin II receptor subtype 1b (AT 1B R, Agtr1b ; Rn02132799_s1; rat), angiotensin II receptor type 1 (AT 1 R, Agtr1 ; Hs00258938_m1; human), angiotensin II receptor type 2 (AT 2 R, Agtr2 ; Rn00560677_s1, Hs02621316_s1; rat, human), Mas receptor (Mas R, Mas1 ; Rn00562673_s1, Hs00267157_s1; rat, human).

Techniques: Protein-Protein interactions, Activation Assay, Transmission Assay

Journal: Cell

Article Title: Serotonin reduction in post-acute sequelae of viral infection

doi: 10.1016/j.cell.2023.09.013

Figure Lengend Snippet: (A–P) Ace2 and Slc6a19 expression in poly(I:C)-treated small intestinal organoids (A and B), poly(I:C)-treated TLR3 −/− mice (C and D), poly(I:C) and IKK-16-treated small intestinal organoids (E and F), IFN-α- and IFN-β-treated small intestinal organoids (G and H), poly(I:C)-treated STAT1 −/− mice (I and J), poly(I:C)-treated Villin Cre–ERT/+ STAT1 flox/flox mice (K and L), ileum of VSV-infected mice (M and N), and ileum of LCMV CL13-infected mice 27 days post-infection (O and P). (Q and R) Intestinal viral RNA after infection with the indicated strains of SARS-CoV-2. (S and T) Normalized expression of Ace2 (S) and Slc6a19 (T) in SARS-CoV-2-infected human small intestinal organoids. (U–W) Study schematic (U), SARS-CoV-2 RNA detected in tissues obtained from autopsies during the acute or post-acute phase after infection (V), and SARS-CoV-2 RNA detected in stool obtained from individuals with PASC and a control group of individuals with prior SARS-CoV-2 infection but no persistent symptoms (W). Plotted are means ± SEM. n.s. p > 0.05, *p < 0.05, **p < 0.01, ***p < 0.001, ****p < 0.0001. See also .

Article Snippet: Ace2 Taqman assay , Thermo Scientific , Mm01159006_m1.

Techniques: Expressing, Infection, Control

Journal: Cell

Article Title: Serotonin reduction in post-acute sequelae of viral infection

doi: 10.1016/j.cell.2023.09.013

Figure Lengend Snippet: (A and B) Targeted plasma metabolomics in poly(I:C)-treated mice vs. controls (A) and ACE2 −/− vs. ACE2 +/+ mice (B). (C) Plasma tryptophan in ACE2 +/+ , ACE2 +/− , and ACE2 −/− mice. (D and E) Plasma tryptophan in ACE2 +/+ vs. ACE2 −/− mice (D) and poly(I:C)-treated mice vs. controls (E) after tryptophan gavage. (F and G) Tryptophan levels in sera (F) and ileal content (G) of poly(I:C)-treated mice 30 min following tryptophan gavage. (H–J) Plasma tryptophan (H) and serotonin (I and J) in poly(I:C)-treated mice fed a Gly-Trp dipeptide diet (H and I) or given the serotonin precursor 5-HTP (J). (K) Schematic of serotonin reduction by viral RNA via reduced tryptophan uptake. Plotted are means ± SEM. n.s. p > 0.05, *p < 0.05, **p < 0.01, ***p < 0.001, ****p < 0.0001. See also .

Article Snippet: Ace2 Taqman assay , Thermo Scientific , Mm01159006_m1.

Techniques: Clinical Proteomics

Journal: Cell

Article Title: Serotonin reduction in post-acute sequelae of viral infection

doi: 10.1016/j.cell.2023.09.013

Figure Lengend Snippet: KEY RESOURCES TABLE

Article Snippet: Ace2 Taqman assay , Thermo Scientific , Mm01159006_m1.

Techniques: Virus, Clinical Proteomics, Recombinant, Enzyme-linked Immunosorbent Assay, Reverse Transcription, Bicinchoninic Acid Protein Assay, SYBR Green Assay, TaqMan Assay, Software, Imaging, Control, Electron Microscopy, Low Protein Binding, Membrane