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Article: Endothelial APC/PAR1 distinctly regulates cytokine-induced pro-inflammatory VCAM-1 expression.

Birch, Cierra A / Wedegaertner, Helen / Orduña-Castillo, Lennis B / Gonzalez Ramirez, Monica L / Qin, Huaping / Trejo, JoAnn

Frontiers in molecular biosciences

2023 Volume 10, Page(s) 1211597

Abstract: Introduction: ...

Abstract	Introduction:
Language	English
Publishing date	2023-08-24
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2814330-9
ISSN	2296-889X
ISSN	2296-889X
DOI	10.3389/fmolb.2023.1211597
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Article ; Online: Subcellular hot spots of GPCR signaling promote vascular inflammation.

Birch, Cierra A / Molinar-Inglis, Olivia / Trejo, JoAnn

Current opinion in endocrine and metabolic research

2020 Volume 16, Page(s) 37–42

Abstract: G-coupled protein receptors (GPCRs) comprise the largest class of druggable targets. Signaling by GPCRs is initiated from subcellular hot spots including the plasma membrane, signalosomes, and endosomes to contribute to vascular inflammation. GPCR-G ... ...

Abstract	G-coupled protein receptors (GPCRs) comprise the largest class of druggable targets. Signaling by GPCRs is initiated from subcellular hot spots including the plasma membrane, signalosomes, and endosomes to contribute to vascular inflammation. GPCR-G protein signaling at the plasma membrane causes endothelial barrier disruption and also cross-talks with growth factor receptors to promote proinflammatory signaling. A second surge of GPCR signaling is initiated by cytoplasmic NFκB activation mediated by β-arrestins and CARMA-BCL10-MALT1 signalosomes. Once internalized, ubiquitinated GPCRs initiate signaling from endosomes via assembly of the transforming growth factor-β-activated kinase binding protein-1 (TAB1)-TAB2-p38 MAPK complex to promote vascular inflammation. Understanding the complexities of GPCR signaling is critical for development of new strategies to treat vascular inflammation such as that associated with COVID-19.
Keywords	covid19
Language	English
Publishing date	2020-08-18
Publishing country	England
Document type	Journal Article ; Review
ISSN	2451-9650
ISSN (online)	2451-9650
DOI	10.1016/j.coemr.2020.07.011
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Article: Subcellular hot spots of GPCR signaling promote vascular inflammation

Birch, Cierra A / Molinar-Inglis, Olivia / Trejo, JoAnn

Abstract: G-coupled protein receptors (GPCRs) comprise the largest class of druggable targets. Signaling by GPCRs is initiated from subcellular hot spots including the plasma membrane, signalosomes and endosomes to contribute to vascular inflammation. GPCR-G ... ...

Abstract	G-coupled protein receptors (GPCRs) comprise the largest class of druggable targets. Signaling by GPCRs is initiated from subcellular hot spots including the plasma membrane, signalosomes and endosomes to contribute to vascular inflammation. GPCR-G protein signaling at the plasma membrane causes endothelial barrier disruption and also cross-talks with growth factor receptors to promote proinflammatory signaling. A second surge of GPCR signaling is initiated by cytoplasmic NFκB activation mediated by ß-arrestins and CARMA-Bcl10-MALT1 signalosomes. Once internalized, ubiquitinated GPCRs initiate signaling from endosomes via assembly of the transforming growth factor-ß-activated kinase binding protein-1 (TAB1)-TAB2-p38 MAPK complex to promote vascular inflammation. Understanding the complexities of GPCR signaling is critical for development of new strategies to treat vascular inflammation such as that associated with COVID-19.
Keywords	covid19
Publisher	WHO
Document type	Article
Note	WHO #Covidence: #718706
Database	COVID19

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Article ; Online: Exploring the Amino Acid Residue Requirements of the RNA Polymerase (RNAP) α Subunit C-Terminal Domain for Productive Interaction between Spx and RNAP of Bacillus subtilis.

Birch, Cierra A / Davis, Madison J / Mbengi, Lea / Zuber, Peter

Journal of bacteriology

2017 Volume 199, Issue 14

Abstract: ... Bacillus ... ...

Abstract	Bacillus subtilis
MeSH term(s)	Alleles ; Amino Acid Sequence ; Bacillus subtilis/genetics ; Bacillus subtilis/metabolism ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; DNA-Directed RNA Polymerases/genetics ; DNA-Directed RNA Polymerases/metabolism ; Gene Expression Regulation, Bacterial/physiology ; Genotype ; Models, Molecular ; Protein Conformation ; Protein Domains
Chemical Substances	Bacterial Proteins ; DNA-Directed RNA Polymerases (EC 2.7.7.6) ; RNA polymerase alpha subunit (EC 2.7.7.6)
Language	English
Publishing date	2017-07-15
Publishing country	United States
Document type	Journal Article
ZDB-ID	2968-3
ISSN	1098-5530 ; 0021-9193
ISSN (online)	1098-5530
ISSN	0021-9193
DOI	10.1128/JB.00124-17
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Article ; Online: Phosphoproteomic analysis of thrombin- and p38 MAPK-regulated signaling networks in endothelial cells.

Molinar-Inglis, Olivia / Wozniak, Jacob M / Grimsey, Neil J / Orduña-Castillo, Lennis B / Cheng, Norton / Lin, Ying / Gonzalez Ramirez, Monica L / Birch, Cierra A / Lapek, John D / Gonzalez, David J / Trejo, JoAnn

The Journal of biological chemistry

2022 Volume 298, Issue 4, Page(s) 101801

Abstract: Endothelial dysfunction is a hallmark of inflammation and is mediated by inflammatory factors that signal through G protein-coupled receptors including protease-activated receptor-1 (PAR1). PAR1, a receptor for thrombin, signals via the small GTPase RhoA ...

Abstract	Endothelial dysfunction is a hallmark of inflammation and is mediated by inflammatory factors that signal through G protein-coupled receptors including protease-activated receptor-1 (PAR1). PAR1, a receptor for thrombin, signals via the small GTPase RhoA and myosin light chain intermediates to facilitate endothelial barrier permeability. PAR1 also induces endothelial barrier disruption through a p38 mitogen-activated protein kinase-dependent pathway, which does not integrate into the RhoA/MLC pathway; however, the PAR1-p38 signaling pathways that promote endothelial dysfunction remain poorly defined. To identify effectors of this pathway, we performed a global phosphoproteome analysis of thrombin signaling regulated by p38 in human cultured endothelial cells using multiplexed quantitative mass spectrometry. We identified 5491 unique phosphopeptides and 2317 phosphoproteins, four distinct dynamic phosphoproteome profiles of thrombin-p38 signaling, and an enrichment of biological functions associated with endothelial dysfunction, including modulators of endothelial barrier disruption and a subset of kinases predicted to regulate p38-dependent thrombin signaling. Using available antibodies to detect identified phosphosites of key p38-regulated proteins, we discovered that inhibition of p38 activity and siRNA-targeted depletion of the p38α isoform increased basal phosphorylation of extracellular signal-regulated protein kinase 1/2, resulting in amplified thrombin-stimulated extracellular signal-regulated protein kinase 1/2 phosphorylation that was dependent on PAR1. We also discovered a role for p38 in the phosphorylation of α-catenin, a component of adherens junctions, suggesting that this phosphorylation may function as an important regulatory process. Taken together, these studies define a rich array of thrombin- and p38-regulated candidate proteins that may serve important roles in endothelial dysfunction.
MeSH term(s)	Cells, Cultured ; Endothelial Cells/metabolism ; Humans ; MAP Kinase Signaling System ; Phosphorylation ; Proteomics ; Receptor, PAR-1/metabolism ; Thrombin/metabolism ; p38 Mitogen-Activated Protein Kinases/metabolism
Chemical Substances	Receptor, PAR-1 ; p38 Mitogen-Activated Protein Kinases (EC 2.7.11.24) ; Thrombin (EC 3.4.21.5)
Language	English
Publishing date	2022-03-04
Publishing country	United States
Document type	Journal Article
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2022.101801
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Article ; Online: aPC/PAR1 confers endothelial anti-apoptotic activity via a discrete, β-arrestin-2-mediated SphK1-S1PR1-Akt signaling axis.

Molinar-Inglis, Olivia / Birch, Cierra A / Nicholas, Dequina / Orduña-Castillo, Lennis / Cisneros-Aguirre, Metztli / Patwardhan, Anand / Chen, Buxin / Grimsey, Neil J / Coronel, Luisa J / Lin, Huilan / Gomez Menzies, Patrick K / Lawson, Mark A / Patel, Hemal H / Trejo, JoAnn

Proceedings of the National Academy of Sciences of the United States of America

2021 Volume 118, Issue 49

Abstract: Endothelial dysfunction is associated with vascular disease and results in disruption of endothelial barrier function and increased sensitivity to apoptosis. Currently, there are limited treatments for improving endothelial dysfunction. Activated protein ...

Abstract	Endothelial dysfunction is associated with vascular disease and results in disruption of endothelial barrier function and increased sensitivity to apoptosis. Currently, there are limited treatments for improving endothelial dysfunction. Activated protein C (aPC), a promising therapeutic, signals via protease-activated receptor-1 (PAR1) and mediates several cytoprotective responses, including endothelial barrier stabilization and anti-apoptotic responses. We showed that aPC-activated PAR1 signals preferentially via β-arrestin-2 (β-arr2) and dishevelled-2 (Dvl2) scaffolds rather than G proteins to promote Rac1 activation and barrier protection. However, the signaling pathways utilized by aPC/PAR1 to mediate anti-apoptotic activities are not known. aPC/PAR1 cytoprotective responses also require coreceptors; however, it is not clear how coreceptors impact different aPC/PAR1 signaling pathways to drive distinct cytoprotective responses. Here, we define a β-arr2-mediated sphingosine kinase-1 (SphK1)-sphingosine-1-phosphate receptor-1 (S1PR1)-Akt signaling axis that confers aPC/PAR1-mediated protection against cell death. Using human cultured endothelial cells, we found that endogenous PAR1 and S1PR1 coexist in caveolin-1 (Cav1)-rich microdomains and that S1PR1 coassociation with Cav1 is increased by aPC activation of PAR1. Our study further shows that aPC stimulates β-arr2-dependent SphK1 activation independent of Dvl2 and is required for transactivation of S1PR1-Akt signaling and protection against cell death. While aPC/PAR1-induced, extracellular signal-regulated kinase 1/2 (ERK1/2) activation is also dependent on β-arr2, neither SphK1 nor S1PR1 are integrated into the ERK1/2 pathway. Finally, aPC activation of PAR1-β-arr2-mediated protection against apoptosis is dependent on Cav1, the principal structural protein of endothelial caveolae. These studies reveal that different aPC/PAR1 cytoprotective responses are mediated by discrete, β-arr2-driven signaling pathways in caveolae.
MeSH term(s)	Anilides/pharmacology ; Apoptosis/physiology ; Endothelial Cells/physiology ; Enzyme Inhibitors/pharmacology ; Gene Expression Regulation/drug effects ; Heterocyclic Compounds, 3-Ring/pharmacology ; Humans ; Lactones/pharmacology ; Methanol/pharmacology ; Organophosphonates/pharmacology ; Phosphotransferases (Alcohol Group Acceptor)/genetics ; Phosphotransferases (Alcohol Group Acceptor)/metabolism ; Platelet Aggregation Inhibitors/pharmacology ; Protein C/genetics ; Protein C/metabolism ; Proto-Oncogene Proteins c-akt/genetics ; Proto-Oncogene Proteins c-akt/metabolism ; Pyridines/pharmacology ; Pyrrolidines/pharmacology ; Receptor, PAR-1/genetics ; Receptor, PAR-1/metabolism ; Sphingosine-1-Phosphate Receptors/genetics ; Sphingosine-1-Phosphate Receptors/metabolism ; Sulfones/pharmacology ; beta-Arrestin 2/genetics ; beta-Arrestin 2/metabolism
Chemical Substances	3-amino-4-(3-hexylphenylamino)-4-oxobutylphosphonic acid ; Anilides ; Enzyme Inhibitors ; Heterocyclic Compounds, 3-Ring ; Lactones ; MK 2206 ; Organophosphonates ; PF-543 ; Platelet Aggregation Inhibitors ; Protein C ; Pyridines ; Pyrrolidines ; Receptor, PAR-1 ; S1PR1 protein, human ; Sphingosine-1-Phosphate Receptors ; Sulfones ; beta-Arrestin 2 ; Phosphotransferases (Alcohol Group Acceptor) (EC 2.7.1.-) ; sphingosine kinase (EC 2.7.1.-) ; Proto-Oncogene Proteins c-akt (EC 2.7.11.1) ; Methanol (Y4S76JWI15) ; vorapaxar (ZCE93644N2)
Language	English
Publishing date	2021-12-16
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.2106623118
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Article ; Online: Evidence that Oxidative Stress Induces spxA2 Transcription in Bacillus anthracis Sterne through a Mechanism Requiring SpxA1 and Positive Autoregulation.

Barendt, Skye / Birch, Cierra / Mbengi, Lea / Zuber, Peter

Journal of bacteriology

2016 Volume 198, Issue 21, Page(s) 2902–2913

Abstract: Bacillus anthracis possesses two paralogs of the transcriptional regulator, Spx. SpxA1 and SpxA2 interact with RNA polymerase (RNAP) to activate the transcription of genes implicated in the prevention and alleviation of oxidative protein damage. The ... ...

Abstract	Bacillus anthracis possesses two paralogs of the transcriptional regulator, Spx. SpxA1 and SpxA2 interact with RNA polymerase (RNAP) to activate the transcription of genes implicated in the prevention and alleviation of oxidative protein damage. The spxA2 gene is highly upregulated in infected macrophages, but how this is achieved is unknown. Previous studies have shown that the spxA2 gene was under negative control by the Rrf2 family repressor protein, SaiR, whose activity is sensitive to oxidative stress. These studies also suggested that spxA2 was under positive autoregulation. In the present study, we show by in vivo and in vitro analyses that spxA2 is under direct autoregulation but is also dependent on the SpxA1 paralogous protein. The deletion of either spxA1 or spxA2 reduced the diamide-inducible expression of an spxA2-lacZ construct. In vitro transcription reactions using purified B. anthracis RNAP showed that SpxA1 and SpxA2 protein stimulates transcription from a DNA fragment containing the spxA2 promoter. Ectopically positioned spxA2-lacZ fusion requires both SpxA1 and SpxA2 for expression, but the requirement for SpxA1 is partially overcome when saiR is deleted. Electrophoretic mobility shift assays showed that SpxA1 and SpxA2 enhance the affinity of RNAP for spxA2 promoter DNA and that this activity is sensitive to reductant. We hypothesize that the previously observed upregulation of spxA2 in the oxidative environment of the macrophage is at least partly due to SpxA1-mediated SaiR repressor inactivation and the positive autoregulation of spxA2 transcription. Importance: Regulators of transcription initiation are known to govern the expression of genes required for virulence in pathogenic bacterial species. Members of the Spx family of transcription factors function in control of genes required for virulence and viability in low-GC Gram-positive bacteria. In Bacillus anthracis, the spxA2 gene is highly induced in infected macrophages, which suggests an important role in the control of virulence gene expression during the anthrax disease state. We provide evidence that elevated concentrations of oxidized, active SpxA2 result from an autoregulatory positive-feedback loop driving spxA2 transcription.
MeSH term(s)	Bacillus anthracis/genetics ; Bacillus anthracis/metabolism ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Gene Expression Regulation, Bacterial ; Oxidation-Reduction ; Oxidative Stress ; Promoter Regions, Genetic ; Transcription Factors/genetics ; Transcription Factors/metabolism ; Transcription, Genetic
Chemical Substances	Bacterial Proteins ; Transcription Factors
Language	English
Publishing date	2016-10-07
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	2968-3
ISSN	1098-5530 ; 0021-9193
ISSN (online)	1098-5530
ISSN	0021-9193
DOI	10.1128/JB.00512-16
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Article ; Online: Transcriptomic and phenotypic analysis of paralogous spx gene function in Bacillus anthracis Sterne.

Barendt, Skye / Lee, Hyunwoo / Birch, Cierra / Nakano, Michiko M / Jones, Marcus / Zuber, Peter

MicrobiologyOpen

2013 Volume 2, Issue 4, Page(s) 695–714

Abstract: Spx of Bacillus subtilis is a redox-sensitive protein, which, under disulfide stress, interacts with RNA polymerase to activate genes required for maintaining thiol homeostasis. Spx orthologs are highly conserved among low %GC Gram-positive bacteria, and ...

Abstract	Spx of Bacillus subtilis is a redox-sensitive protein, which, under disulfide stress, interacts with RNA polymerase to activate genes required for maintaining thiol homeostasis. Spx orthologs are highly conserved among low %GC Gram-positive bacteria, and often exist in multiple paralogous forms. In this study, we used B. anthracis Sterne, which harbors two paralogous spx genes, spxA1 and spxA2, to examine the phenotypes of spx null mutations and to identify the genes regulated by each Spx paralog. Cells devoid of spxA1 were sensitive to diamide and hydrogen peroxide, while the spxA1 spoxA2 double mutant was hypersensitive to the thiol-specific oxidant, diamide. Bacillus anthracis Sterne strains expressing spxA1DD or spxA2DD alleles encoding protease-resistant products were used in microarray and quantitative real-time polymerase chain reaction (RT-qPCR) analyses in order to uncover genes under SpxA1, SpxA2, or SpxA1/SpxA2 control. Comparison of transcriptomes identified many genes that were upregulated when either SpxA1DD or SpxA2DD was produced, but several genes were uncovered whose transcript levels increased in only one of the two SpxADD-expression strains, suggesting that each Spx paralog governs a unique regulon. Among genes that were upregulated were those encoding orthologs of proteins that are specifically involved in maintaining intracellular thiol homeostasis or alleviating oxidative stress. Some of these genes have important roles in B. anthracis pathogenesis, and a large number of upregulated hypothetical genes have no homology outside of the B. cereus/thuringiensis group. Microarray and RT-qPCR analyses also unveiled a regulatory link that exists between the two spx paralogous genes. The data indicate that spxA1 and spxA2 are transcriptional regulators involved in relieving disulfide stress but also control a set of genes whose products function in other cellular processes.
MeSH term(s)	Amino Acid Sequence ; Bacillus anthracis/drug effects ; Bacillus anthracis/genetics ; Bacillus anthracis/physiology ; Bacterial Proteins/biosynthesis ; Bacterial Proteins/genetics ; Diamide/toxicity ; Gene Deletion ; Gene Expression Profiling ; Gene Order ; Hydrogen Peroxide/toxicity ; Microarray Analysis ; Molecular Sequence Data ; Oxidants/toxicity ; Oxidative Stress ; Real-Time Polymerase Chain Reaction ; Transcription Factors/biosynthesis ; Transcription Factors/genetics
Chemical Substances	Bacterial Proteins ; Oxidants ; Transcription Factors ; Diamide (10465-78-8) ; Hydrogen Peroxide (BBX060AN9V)
Language	English
Publishing date	2013-07-22
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2661368-2
ISSN	2045-8827 ; 2045-8827
ISSN (online)	2045-8827
ISSN	2045-8827
DOI	10.1002/mbo3.109
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Article: Endothelial APC/PAR1 distinctly regulates cytokine-induced pro-inflammatory VCAM-1 expression.

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Article ; Online: Subcellular hot spots of GPCR signaling promote vascular inflammation.

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Article: Subcellular hot spots of GPCR signaling promote vascular inflammation

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Article ; Online: Exploring the Amino Acid Residue Requirements of the RNA Polymerase (RNAP) α Subunit C-Terminal Domain for Productive Interaction between Spx and RNAP of Bacillus subtilis.

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Article ; Online: Phosphoproteomic analysis of thrombin- and p38 MAPK-regulated signaling networks in endothelial cells.

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Article ; Online: aPC/PAR1 confers endothelial anti-apoptotic activity via a discrete, β-arrestin-2-mediated SphK1-S1PR1-Akt signaling axis.

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Article ; Online: Evidence that Oxidative Stress Induces spxA2 Transcription in Bacillus anthracis Sterne through a Mechanism Requiring SpxA1 and Positive Autoregulation.

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Article ; Online: Transcriptomic and phenotypic analysis of paralogous spx gene function in Bacillus anthracis Sterne.

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