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Book ; Online ; E-Book: Manual of cardiovascular proteomics

Agnetti, Giulio / Lindsey, Merry L. / Foster, D. Brian

2016

Author's details	Giulio Agnetti, Merry L. Lindsey, D. Brian Foster editors
Keywords	Cardiovascular Diseases / metabolism ; Proteomics / methods ; Cardiovascular System / metabolism ; Biomarkers / analysis
Language	English
Size	1 Online-Ressource (xvi, 430 Seiten), Illustrationen
Publisher	Springer
Publishing place	Cham
Publishing country	Switzerland
Document type	Book ; Online ; E-Book
Remark	Zugriff für angemeldete ZB MED-Nutzerinnen und -Nutzer
HBZ-ID	HT019474699
ISBN	978-3-319-31828-8 ; 9783319318264 ; 3-319-31828-4 ; 3319318268
Database	ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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Article ; Online: Common Heart Failure With Preserved Ejection Fraction Animal Models Yield Disparate Myofibril Mechanics.

Fenwick, Axel J / Jani, Vivek P / Foster, D Brian / Sharp, Thomas E / Goodchild, Traci T / LaPenna, Kyle / Doiron, Jake E / Lefer, David J / Hill, Joseph A / Kass, David A / Cammarato, Anthony

Journal of the American Heart Association

2024 Volume 13, Issue 2, Page(s) e032037

MeSH term(s)	Animals ; Stroke Volume ; Myofibrils ; Heart Failure ; Ventricular Function, Left ; Models, Animal
Language	English
Publishing date	2024-01-09
Publishing country	England
Document type	Journal Article
ZDB-ID	2653953-6
ISSN	2047-9980 ; 2047-9980
ISSN (online)	2047-9980
ISSN	2047-9980
DOI	10.1161/JAHA.123.032037
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Lysine acetylation of F-actin decreases tropomyosin-based inhibition of actomyosin activity.

Schmidt, William / Madan, Aditi / Foster, D Brian / Cammarato, Anthony

The Journal of biological chemistry

2020 Volume 295, Issue 46, Page(s) 15527–15539

Abstract: Recent proteomics studies of vertebrate striated muscle have identified lysine acetylation at several sites on actin. Acetylation is a reversible post-translational modification that neutralizes lysine's positive charge. Positively charged residues on ... ...

Abstract	Recent proteomics studies of vertebrate striated muscle have identified lysine acetylation at several sites on actin. Acetylation is a reversible post-translational modification that neutralizes lysine's positive charge. Positively charged residues on actin, particularly Lys
MeSH term(s)	Acetylation ; Actins/chemistry ; Actins/genetics ; Actins/metabolism ; Actomyosin/antagonists & inhibitors ; Actomyosin/metabolism ; Amino Acid Sequence ; Animals ; Animals, Genetically Modified/metabolism ; Binding Sites ; Calcium/metabolism ; Cattle ; Drosophila/metabolism ; Drosophila Proteins/chemistry ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism ; Kinetics ; Lysine/metabolism ; Molecular Dynamics Simulation ; Mutagenesis, Site-Directed ; Protein Binding ; Rabbits ; Swine ; Tropomyosin/metabolism
Chemical Substances	Actins ; Drosophila Proteins ; Tropomyosin ; Actomyosin (9013-26-7) ; Lysine (K3Z4F929H6) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2020-09-01
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.RA120.015277
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Article ; Online: Tbx18 Orchestrates Cytostructural Transdifferentiation of Cardiomyocytes to Pacemaker Cells by Recruiting the Epithelial-Mesenchymal Transition Program.

Foster, D Brian / Gu, Jin-Mo / Kim, Elizabeth H / Wolfson, David W / O'Meally, Robert / Cole, Robert N / Cho, Hee Cheol

Journal of proteome research

2022 Volume 21, Issue 10, Page(s) 2277–2292

Abstract: Previously, we reported that heterologous expression of an embryonic transcription factor, Tbx18, reprograms ventricular cardiomyocytes into induced pacemaker cells (Tbx18-iPMs), though the key pathways are unknown. Here, we have used a tandem mass tag ... ...

Abstract	Previously, we reported that heterologous expression of an embryonic transcription factor, Tbx18, reprograms ventricular cardiomyocytes into induced pacemaker cells (Tbx18-iPMs), though the key pathways are unknown. Here, we have used a tandem mass tag proteomic approach to characterize the impact of Tbx18 on neonatal rat ventricular myocytes. Tbx18 expression triggered vast proteome remodeling. Tbx18-iPMs exhibited increased expression of known pacemaker ion channels, including Hcn4 and Cx45 as well as upregulation of the mechanosensitive ion channels Piezo1, Trpp2 (PKD2), and TrpM7. Metabolic pathways were broadly downregulated, as were ion channels associated with ventricular excitation-contraction coupling. Tbx18-iPMs also exhibited extensive intracellular cytoskeletal and extracellular matrix remodeling, including 96 differentially expressed proteins associated with the epithelial-to-mesenchymal transition (EMT). RNAseq extended coverage of low abundance transcription factors, revealing upregulation of EMT-inducing Snai1, Snai2, Twist1, Twist2, and Zeb2. Finally, network diffusion mapping of >200 transcriptional regulators indicates EMT and heart development factors occupy adjacent network neighborhoods downstream of Tbx18 but upstream of metabolic control factors. In conclusion, transdifferentiation of cardiac myocytes into pacemaker cells entails massive electrogenic, metabolic, and cytostructural remodeling. Structural changes exhibit hallmarks of the EMT. The results aid ongoing efforts to maximize the yield and phenotypic stability of engineered biological pacemakers.
MeSH term(s)	Animals ; Cell Transdifferentiation ; Epithelial-Mesenchymal Transition/genetics ; Hyperpolarization-Activated Cyclic Nucleotide-Gated Channels/genetics ; Hyperpolarization-Activated Cyclic Nucleotide-Gated Channels/metabolism ; Myocytes, Cardiac/metabolism ; Proteome/metabolism ; Proteomics ; Rats ; T-Box Domain Proteins/genetics ; T-Box Domain Proteins/metabolism ; TRPM Cation Channels/metabolism ; Transcription Factors/genetics ; Transcription Factors/metabolism
Chemical Substances	Hyperpolarization-Activated Cyclic Nucleotide-Gated Channels ; Proteome ; T-Box Domain Proteins ; TRPM Cation Channels ; Tbx18 protein, rat ; Transcription Factors ; Trpm7 protein, rat (EC 2.7.11.1)
Language	English
Publishing date	2022-08-25
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	2078618-9
ISSN	1535-3907 ; 1535-3893
ISSN (online)	1535-3907
ISSN	1535-3893
DOI	10.1021/acs.jproteome.2c00133
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Article ; Online: Diabetic cardiomyopathy and the role of mitochondrial dysfunction: novel insights, mechanisms, and therapeutic strategies.

Aon, Miguel A / Foster, D Brian

Antioxidants & redox signaling

2015 Volume 22, Issue 17, Page(s) 1499–1501

Abstract: This Forum addresses the role of mitochondrial dysfunction in the multifactorial nature of diabetic cardiomyopathy (DCM) from multiple angles. Contributors deliver a diverse and in-depth view of the state-of-the-art in DCM, from bench to bedside. What ... ...

Abstract	This Forum addresses the role of mitochondrial dysfunction in the multifactorial nature of diabetic cardiomyopathy (DCM) from multiple angles. Contributors deliver a diverse and in-depth view of the state-of-the-art in DCM, from bench to bedside. What emerges is a picture of mitochondrial dysfunction as a central upstream defect, inflicted on the heart by diabetes. Collectively, the authors pinpoint high-value knowledge gaps, propose new conceptual frameworks, and highlight understudied, but promising, research themes.
MeSH term(s)	Animals ; Diabetes Complications/metabolism ; Diabetes Complications/pathology ; Diabetic Cardiomyopathies/physiopathology ; Diabetic Cardiomyopathies/therapy ; Humans ; Mitochondria, Heart/metabolism ; Muscle, Skeletal/metabolism ; Muscle, Skeletal/pathology ; Myocardium/metabolism ; Myocardium/pathology
Language	English
Publishing date	2015-04-29
Publishing country	United States
Document type	Editorial
ZDB-ID	1483836-9
ISSN	1557-7716 ; 1523-0864
ISSN (online)	1557-7716
ISSN	1523-0864
DOI	10.1089/ars.2015.6349
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Zs.A 5488: Show issues

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Article ; Online: Inhibiting O-GlcNAcylation impacts p38 and Erk1/2 signaling and perturbs cardiomyocyte hypertrophy.

Papanicolaou, Kyriakos N / Jung, Jessica / Ashok, Deepthi / Zhang, Wenxi / Modaressanavi, Amir / Avila, Eddie / Foster, D Brian / Zachara, Natasha E / O'Rourke, Brian

The Journal of biological chemistry

2023 Volume 299, Issue 3, Page(s) 102907

Abstract: The dynamic cycling of O-linked GlcNAc (O-GlcNAc) on and off Ser/Thr residues of intracellular proteins, termed O-GlcNAcylation, is mediated by the conserved enzymes O-GlcNAc transferase (OGT) and O-GlcNAcase. O-GlcNAc cycling is important in homeostatic ...

Abstract	The dynamic cycling of O-linked GlcNAc (O-GlcNAc) on and off Ser/Thr residues of intracellular proteins, termed O-GlcNAcylation, is mediated by the conserved enzymes O-GlcNAc transferase (OGT) and O-GlcNAcase. O-GlcNAc cycling is important in homeostatic and stress responses, and its perturbation sensitizes the heart to ischemic and other injuries. Despite considerable progress, many molecular pathways impacted by O-GlcNAcylation in the heart remain unclear. The mitogen-activated protein kinase (MAPK) pathway is a central signaling cascade that coordinates developmental, physiological, and pathological responses in the heart. The developmental or adaptive arm of MAPK signaling is primarily mediated by Erk kinases, while the pathophysiologic arm is mediated by p38 and Jnk kinases. Here, we examine whether O-GlcNAcylation affects MAPK signaling in cardiac myocytes, focusing on Erk1/2 and p38 in basal and hypertrophic conditions induced by phenylephrine. Using metabolic labeling of glycans coupled with alkyne-azide "click" chemistry, we found that Erk1/2 and p38 are O-GlcNAcylated. Supporting the regulation of p38 by O-GlcNAcylation, the OGT inhibitor, OSMI-1, triggers the phosphorylation of p38, an event that involves the NOX2-Ask1-MKK3/6 signaling axis and also the noncanonical activator Tab1. Additionally, OGT inhibition blocks the phenylephrine-induced phosphorylation of Erk1/2. Consistent with perturbed MAPK signaling, OSMI-1-treated cardiomyocytes have a blunted hypertrophic response to phenylephrine, decreased expression of cTnT (key component of the contractile apparatus), and increased expression of maladaptive natriuretic factors Anp and Bnp. Collectively, these studies highlight new roles for O-GlcNAcylation in maintaining a balanced activity of Erk1/2 and p38 MAPKs during hypertrophic growth responses in cardiomyocytes.
MeSH term(s)	Humans ; Myocytes, Cardiac/metabolism ; Signal Transduction/physiology ; Phosphorylation ; Hypertrophy/metabolism ; Proteins/metabolism ; N-Acetylglucosaminyltransferases/genetics ; N-Acetylglucosaminyltransferases/metabolism ; Acetylglucosamine/metabolism
Chemical Substances	Proteins ; N-Acetylglucosaminyltransferases (EC 2.4.1.-) ; Acetylglucosamine (V956696549)
Language	English
Publishing date	2023-01-13
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2023.102907
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Book: Manual of cardiovascular proteomics

Agnetti, Giulio / Lindsey, Merry L / Foster, D. Brian

2016

Author's details	Giulio Agnetti, Merry L. Lindsey, D. Brian Foster, editors
MeSH term(s)	Cardiovascular Diseases/metabolism ; Proteomics/methods ; Cardiovascular System/metabolism ; Biomarkers/analysis
Language	English
Size	xvi, 430 pages :, illustrations
Document type	Book
ISBN	9783319318264 ; 9783319318288 ; 3319318268 ; 3319318284
Database	Catalogue of the US National Library of Medicine (NLM)

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Article ; Online: Seeing the Forest for the Trees.

O'Rourke, Brian / Liu, Ting / Foster, D Brian

Circulation research

2016 Volume 119, Issue 11, Page(s) 1170–1172

MeSH term(s)	Animals ; Genomics/methods ; Genomics/trends ; Heart Failure/genetics ; Heart Failure/therapy ; Humans ; Proteomics/methods ; Proteomics/trends ; Signal Transduction/physiology ; Systems Biology/methods ; Systems Biology/trends
Language	English
Publishing date	2016--11
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	80100-8
ISSN	1524-4571 ; 0009-7330 ; 0931-6876
ISSN (online)	1524-4571
ISSN	0009-7330 ; 0931-6876
DOI	10.1161/CIRCRESAHA.116.310066
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Induced cardiac pacemaker cells survive metabolic stress owing to their low metabolic demand.

Gu, Jin-Mo / Grijalva, Sandra I / Fernandez, Natasha / Kim, Elizabeth / Foster, D Brian / Cho, Hee Cheol

Experimental & molecular medicine

2019 Volume 51, Issue 9, Page(s) 1–12

Abstract: Cardiac pacemaker cells of the sinoatrial node initiate each and every heartbeat. Compared with our understanding of the constituents of their electrical excitation, little is known about the metabolic underpinnings that drive the automaticity of ... ...

Abstract	Cardiac pacemaker cells of the sinoatrial node initiate each and every heartbeat. Compared with our understanding of the constituents of their electrical excitation, little is known about the metabolic underpinnings that drive the automaticity of pacemaker myocytes. This lack is largely owing to the scarcity of native cardiac pacemaker myocytes. Here, we take advantage of induced pacemaker myocytes generated by TBX18-mediated reprogramming (TBX18-iPMs) to investigate comparative differences in the metabolic program between pacemaker myocytes and working cardiomyocytes. TBX18-iPMs were more resistant to metabolic stresses, exhibiting higher cell viability upon oxidative stress. TBX18-induced pacemaker myocytes (iPMs) expensed a lower degree of oxidative phosphorylation and displayed a smaller capacity for glycolysis compared with control ventricular myocytes. Furthermore, the mitochondria were smaller in TBX18-iPMs than in the control. We reasoned that a shift in the balance between mitochondrial fusion and fission was responsible for the smaller mitochondria observed in TBX18-iPMs. We identified a mitochondrial inner membrane fusion protein, Opa1, as one of the key mediators of this process and demonstrated that the suppression of Opa1 expression increases the rate of synchronous automaticity in TBX18-iPMs. Taken together, our data demonstrate that TBX18-iPMs exhibit a low metabolic demand that matches their mitochondrial morphology and ability to withstand metabolic insult.
MeSH term(s)	Animals ; Cellular Reprogramming/genetics ; GTP Phosphohydrolases/genetics ; Gene Expression Regulation/genetics ; Glycolysis/genetics ; Humans ; Mitochondria/genetics ; Mitochondria/metabolism ; Mitochondrial Dynamics/genetics ; Mitochondrial Membranes/metabolism ; Myocytes, Cardiac/metabolism ; Oxidative Stress/genetics ; Rats ; Sinoatrial Node/metabolism ; Sinoatrial Node/pathology ; Stress, Physiological/genetics ; T-Box Domain Proteins/genetics
Chemical Substances	T-Box Domain Proteins ; Tbx18 protein, rat ; GTP Phosphohydrolases (EC 3.6.1.-) ; Opa1 protein, rat (EC 3.6.1.-)
Language	English
Publishing date	2019-09-13
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1328915-9
ISSN	2092-6413 ; 1226-3613 ; 0378-8512
ISSN (online)	2092-6413
ISSN	1226-3613 ; 0378-8512
DOI	10.1038/s12276-019-0303-6
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Article ; Online: Troponin I Tyrosine Phosphorylation Beneficially Accelerates Diastolic Function.

Salyer, Lorien G / Salhi, Hussam E / Brundage, Elizabeth A / Shettigar, Vikram / Sturgill, Sarah L / Zanella, Helena / Templeton, Benjamin / Abay, Eaman / Emmer, Kathryn M / Lowe, Jeovanna / Rafael-Fortney, Jill A / Parinandi, Narasimham / Foster, D Brian / McKinsey, Timothy A / Woulfe, Kathleen C / Ziolo, Mark T / Biesiadecki, Brandon J

Circulation research

2023 Volume 134, Issue 1, Page(s) 33–45

Abstract: Background: A healthy heart is able to modify its function and increase relaxation through post-translational modifications of myofilament proteins. While there are known examples of serine/threonine kinases directly phosphorylating myofilament proteins ...

Abstract	Background: A healthy heart is able to modify its function and increase relaxation through post-translational modifications of myofilament proteins. While there are known examples of serine/threonine kinases directly phosphorylating myofilament proteins to modify heart function, the roles of tyrosine (Y) phosphorylation to directly modify heart function have not been demonstrated. The myofilament protein TnI (troponin I) is the inhibitory subunit of the troponin complex and is a key regulator of cardiac contraction and relaxation. We previously demonstrated that TnI-Y26 phosphorylation decreases calcium-sensitive force development and accelerates calcium dissociation, suggesting a novel role for tyrosine kinase-mediated TnI-Y26 phosphorylation to regulate cardiac relaxation. Therefore, we hypothesize that increasing TnI-Y26 phosphorylation will increase cardiac relaxation in vivo and be beneficial during pathological diastolic dysfunction. Methods: The signaling pathway involved in TnI-Y26 phosphorylation was predicted in silico and validated by tyrosine kinase activation and inhibition in primary adult murine cardiomyocytes. To investigate how TnI-Y26 phosphorylation affects cardiac muscle, structure, and function in vivo, we developed a novel TnI-Y26 phosphorylation-mimetic mouse that was subjected to echocardiography, pressure-volume loop hemodynamics, and myofibril mechanical studies. TnI-Y26 phosphorylation-mimetic mice were further subjected to the nephrectomy/DOCA (deoxycorticosterone acetate) model of diastolic dysfunction to investigate the effects of increased TnI-Y26 phosphorylation in disease. Results: Src tyrosine kinase is sufficient to phosphorylate TnI-Y26 in cardiomyocytes. TnI-Y26 phosphorylation accelerates in vivo relaxation without detrimental structural or systolic impairment. In a mouse model of diastolic dysfunction, TnI-Y26 phosphorylation is beneficial and protects against the development of disease. Conclusions: We have demonstrated that tyrosine kinase phosphorylation of TnI is a novel mechanism to directly and beneficially accelerate myocardial relaxation in vivo.
MeSH term(s)	Mice ; Animals ; Phosphorylation ; Troponin I/genetics ; Calcium/metabolism ; Protein Processing, Post-Translational ; Myocardial Contraction/physiology ; Myofibrils/metabolism ; Protein-Tyrosine Kinases ; Tyrosine/metabolism ; Tyrosine/pharmacology
Chemical Substances	Troponin I ; Calcium (SY7Q814VUP) ; Protein-Tyrosine Kinases (EC 2.7.10.1) ; Tyrosine (42HK56048U)
Language	English
Publishing date	2023-12-14
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	80100-8
ISSN	1524-4571 ; 0009-7330 ; 0931-6876
ISSN (online)	1524-4571
ISSN	0009-7330 ; 0931-6876
DOI	10.1161/CIRCRESAHA.123.323132
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