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Article ; Online: The Structural-Functional Crosstalk of the Calsequestrin System: Insights and Pathological Implications.

Marabelli, Chiara / Santiago, Demetrio J / Priori, Silvia G

2023 Volume 13, Issue 12

Abstract: Calsequestrin (CASQ) is a key intra-sarcoplasmic reticulum ... ...

Abstract	Calsequestrin (CASQ) is a key intra-sarcoplasmic reticulum Ca
MeSH term(s)	Humans ; Calsequestrin/genetics ; Calsequestrin/metabolism ; Heart ; Tachycardia, Ventricular/genetics ; Tachycardia, Ventricular/metabolism ; Sarcoplasmic Reticulum/metabolism ; Mutation, Missense ; Calcium/metabolism
Chemical Substances	Calsequestrin ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2023-11-23
Publishing country	Switzerland
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't
ZDB-ID	2701262-1
ISSN	2218-273X ; 2218-273X
ISSN (online)	2218-273X
ISSN	2218-273X
DOI	10.3390/biom13121693
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Arrhythmogenic Cardiomyopathy: Pathophysiology Beyond Cardiac Myocytes.

Priori, Silvia G / Santiago, Demetrio J

Circulation research

2017 Volume 121, Issue 12, Page(s) 1296–1298

MeSH term(s)	Arrhythmias, Cardiac ; Cardiomyopathies ; Desmoplakins/genetics ; Humans ; Myocytes, Cardiac ; Phenotype ; Syndrome
Chemical Substances	Desmoplakins
Language	English
Publishing date	2017-12-07
Publishing country	United States
Document type	Editorial ; Research Support, Non-U.S. Gov't ; Comment
ZDB-ID	80100-8
ISSN	1524-4571 ; 0009-7330 ; 0931-6876
ISSN (online)	1524-4571
ISSN	0009-7330 ; 0931-6876
DOI	10.1161/CIRCRESAHA.117.312211
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Article ; Online: Ligand sensitivity of type-1 inositol 1,4,5-trisphosphate receptor is enhanced by the D2594K mutation.

Tambeaux, Allison / Aguilar-Sánchez, Yuriana / Santiago, Demetrio J / Mascitti, Madeleine / DiNovo, Karyn M / Mejía-Alvarez, Rafael / Fill, Michael / Wayne Chen, S R / Ramos-Franco, Josefina

Pflugers Archiv : European journal of physiology

2023 Volume 475, Issue 5, Page(s) 569–581

Abstract: Inositol 1,4,5-trisphosphate receptor ( ... ...

Abstract	Inositol 1,4,5-trisphosphate receptor (IP
MeSH term(s)	Inositol 1,4,5-Trisphosphate Receptors/genetics ; Inositol 1,4,5-Trisphosphate Receptors/metabolism ; Ligands ; Calcium Signaling ; Mutation ; Endoplasmic Reticulum/metabolism ; Calcium/metabolism
Chemical Substances	Inositol 1,4,5-Trisphosphate Receptors ; Ligands ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2023-03-07
Publishing country	Germany
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	6380-0
ISSN	1432-2013 ; 0031-6768
ISSN (online)	1432-2013
ISSN	0031-6768
DOI	10.1007/s00424-023-02796-x
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Article ; Online: Precision Medicine in Catecholaminergic Polymorphic Ventricular Tachycardia: JACC Focus Seminar 5/5.

Priori, Silvia G / Mazzanti, Andrea / Santiago, Demetrio J / Kukavica, Deni / Trancuccio, Alessandro / Kovacic, Jason C

Journal of the American College of Cardiology

2021 Volume 77, Issue 20, Page(s) 2592–2612

Abstract: In this final of a 5-part Focus Seminar series on precision medicine, we focus on catecholaminergic polymorphic ventricular tachycardia (CPVT). This focus on CPVT allows us to take a "deep dive" and explore the full extent of the precision medicine ... ...

Abstract	In this final of a 5-part Focus Seminar series on precision medicine, we focus on catecholaminergic polymorphic ventricular tachycardia (CPVT). This focus on CPVT allows us to take a "deep dive" and explore the full extent of the precision medicine opportunities for a single cardiovascular condition at a level that was not possible in the preceding articles. As a new paradigm presented in this article, it has become clear that CPVT can occur as either a typical or atypical form. Although there is a degree of overlap between the typical and atypical forms, it is notable that they arise due to different underlying genetic changes, likely exhibiting differing mechanisms of action, and presenting with different phenotypic features. The recognition of these differing forms of CPVT and their different etiologies and mechanisms is an important step toward implementing rapidly emerging precision medicine approaches that will tailor novel therapies to specific gene defects.
MeSH term(s)	Humans ; Precision Medicine ; Tachycardia, Ventricular/genetics ; Tachycardia, Ventricular/therapy
Language	English
Publishing date	2021-05-20
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	605507-2
ISSN	1558-3597 ; 0735-1097
ISSN (online)	1558-3597
ISSN	0735-1097
DOI	10.1016/j.jacc.2020.12.073
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Article ; Online: Isoproterenol increases the fraction of spark-dependent RyR-mediated leak in ventricular myocytes.

Santiago, Demetrio J / Ríos, Eduardo / Shannon, Thomas R

Biophysical journal

2013 Volume 104, Issue 5, Page(s) 976–985

Abstract: Recent research suggests that the diastolic ryanodine-receptor-mediated release of Ca(2+) (J(leak ... of these release manifestations is scarce, however. This study addresses whether the fraction of spark-mediated J ... Ca(2+) sparks and quantify J(leak) in intact rabbit myocytes, either in the absence or ...

Abstract	Recent research suggests that the diastolic ryanodine-receptor-mediated release of Ca(2+) (J(leak)) from the sarcoplasmic reticulum of ventricular myocytes occurs in spark and nonspark forms. Further information about the role(s) of these release manifestations is scarce, however. This study addresses whether the fraction of spark-mediated J(leak) increases due to β-adrenergic stimulation. Confocal microscopy was used to simultaneously image Ca(2+) sparks and quantify J(leak) in intact rabbit myocytes, either in the absence or in the presence of 125 nM isoproterenol. It was found that isoproterenol treatment shifts the spark-frequency-J(leak) relationship toward an increased sensitivity to a [Ca(2+)] trigger. In agreement, a small but significant increase in spark width was found for cells with matched baseline [Ca(2+)] and total SR [Ca(2+)]. The reconstruction of release fluxes, when applied to the average sparks from those selected cells, yielded a wider release source in the isoproterenol event, indicating the recruitment of peripheral ryanodine receptors. Overall, the results presented here indicate that β-adrenergic stimulation increases the spark-dependent fraction of J(leak). Working together, the increased Ca(2+) sensitivity and the greater spark width found during isoproterenol treatment may increase the probability of Ca(2+) wave generation.
MeSH term(s)	Adrenergic beta-Agonists/pharmacology ; Animals ; Calcium/metabolism ; Calcium Signaling/drug effects ; Cytoplasm/metabolism ; Heart Ventricles/cytology ; Isoproterenol/pharmacology ; Myocytes, Cardiac/metabolism ; Rabbits ; Ryanodine Receptor Calcium Release Channel/metabolism ; Sarcoplasmic Reticulum/metabolism
Chemical Substances	Adrenergic beta-Agonists ; Ryanodine Receptor Calcium Release Channel ; Isoproterenol (L628TT009W) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2013-03-06
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	218078-9
ISSN	1542-0086 ; 0006-3495
ISSN (online)	1542-0086
ISSN	0006-3495
DOI	10.1016/j.bpj.2013.01.026
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Article ; Online: Altered adrenergic response in myocytes bordering a chronic myocardial infarction underlies in vivo triggered activity and repolarization instability.

Dries, Eef / Amoni, Matthew / Vandenberk, Bert / Johnson, Daniel M / Gilbert, Guillaume / Nagaraju, Chandan K / Puertas, Rosa Doñate / Abdesselem, Mouna / Santiago, Demetrio J / Roderick, H Llewelyn / Claus, Piet / Willems, Rik / Sipido, Karin R

The Journal of physiology

2020 Volume 598, Issue 14, Page(s) 2875–2895

Abstract: Key points: Ventricular arrhythmias are a major complication after myocardial infarction (MI), associated with sympathetic activation. The structurally heterogeneous peri-infarct zone is a known substrate, but the functional role of the myocytes is less ...

Abstract	Key points: Ventricular arrhythmias are a major complication after myocardial infarction (MI), associated with sympathetic activation. The structurally heterogeneous peri-infarct zone is a known substrate, but the functional role of the myocytes is less well known. Recordings of monophasic action potentials in vivo reveal that the peri-infarct zone is a source of delayed afterdepolarizations (DADs) and has a high beat-to-beat variability of repolarization (BVR) during adrenergic stimulation (isoproterenol, ISO). Myocytes isolated from the peri-infarct region have more DADs and spontaneous action potentials, with spontaneous Ca Abstract: Ventricular arrhythmias are a major early complication after myocardial infarction (MI). The heterogeneous peri-infarct zone forms a substrate for re-entry while arrhythmia initiation is often associated with sympathetic activation. We studied the mechanisms triggering these post-MI arrhythmias in vivo and their relation to regional myocyte remodelling. In pigs with chronic MI (6 weeks), in vivo monophasic action potentials were simultaneously recorded in the peri-infarct and remote regions during adrenergic stimulation with isoproterenol (isoprenaline; ISO). Sham animals served as controls. During infusion of ISO in vivo, the incidence of delayed afterdepolarizations (DADs) and beat-to-beat variability of repolarization (BVR) was higher in the peri-infarct than in the remote region. Myocytes isolated from the peri-infarct region, in comparison to myocytes from the remote region, had more DADs, associated with spontaneous Ca
MeSH term(s)	Action Potentials ; Adrenergic Agents ; Animals ; Arrhythmias, Cardiac/etiology ; Myocardial Infarction ; Myocytes, Cardiac ; Swine
Chemical Substances	Adrenergic Agents
Language	English
Publishing date	2020-02-11
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	3115-x
ISSN	1469-7793 ; 0022-3751
ISSN (online)	1469-7793
ISSN	0022-3751
DOI	10.1113/JP278839
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Article: Isoproterenol Increases the Fraction of Spark-Dependent RyR-Mediated Leak in Ventricular Myocytes

Santiago, Demetrio J / Ríos, Eduardo / Shannon, Thomas R

Biophysical journal. 2013 Mar. 5, v. 104, no. 5

2013

Abstract: Recent research suggests that the diastolic ryanodine-receptor-mediated release of Ca2+ (Jleak) from the sarcoplasmic reticulum of ventricular myocytes occurs in spark and nonspark forms. Further information about the role(s) of these release ... ...

Abstract	Recent research suggests that the diastolic ryanodine-receptor-mediated release of Ca2+ (Jleak) from the sarcoplasmic reticulum of ventricular myocytes occurs in spark and nonspark forms. Further information about the role(s) of these release manifestations is scarce, however. This study addresses whether the fraction of spark-mediated Jleak increases due to β-adrenergic stimulation. Confocal microscopy was used to simultaneously image Ca2+ sparks and quantify Jleak in intact rabbit myocytes, either in the absence or in the presence of 125 nM isoproterenol. It was found that isoproterenol treatment shifts the spark-frequency-Jleak relationship toward an increased sensitivity to a [Ca2+] trigger. In agreement, a small but significant increase in spark width was found for cells with matched baseline [Ca2+] and total SR [Ca2+]. The reconstruction of release fluxes, when applied to the average sparks from those selected cells, yielded a wider release source in the isoproterenol event, indicating the recruitment of peripheral ryanodine receptors. Overall, the results presented here indicate that β-adrenergic stimulation increases the spark-dependent fraction of Jleak. Working together, the increased Ca2+ sensitivity and the greater spark width found during isoproterenol treatment may increase the probability of Ca2+ wave generation.
Keywords	microscopy ; rabbits ; probability ; sarcoplasmic reticulum ; calcium ; myocytes ; ryanodine receptors
Language	English
Dates of publication	2013-0305
Size	p. 976-985.
Publishing place	Elsevier Inc.
Document type	Article
Note	2019-12-06
ZDB-ID	218078-9
ISSN	1542-0086 ; 0006-3495
ISSN (online)	1542-0086
ISSN	0006-3495
DOI	10.1016/j.bpj.2013.01.026
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: A cryo-EM-based model of phosphorylation- and FKBP12.6-mediated allosterism of the cardiac ryanodine receptor.

Dhindwal, Sonali / Lobo, Joshua / Cabra, Vanessa / Santiago, Demetrio J / Nayak, Ashok R / Dryden, Kelly / Samsó, Montserrat

Science signaling

2017 Volume 10, Issue 480

Abstract: Type 2 ryanodine receptors (RyR2s) are calcium channels that play a vital role in triggering cardiac muscle contraction by releasing calcium from the sarcoplasmic reticulum into the cytoplasm. Several cardiomyopathies are associated with the abnormal ... ...

Abstract	Type 2 ryanodine receptors (RyR2s) are calcium channels that play a vital role in triggering cardiac muscle contraction by releasing calcium from the sarcoplasmic reticulum into the cytoplasm. Several cardiomyopathies are associated with the abnormal functioning of RyR2. We determined the three-dimensional structure of rabbit RyR2 in complex with the regulatory protein FKBP12.6 in the closed state at 11.8 Å resolution using cryo-electron microscopy and built an atomic model of RyR2. The heterogeneity in the data set revealed two RyR2 conformations that we proposed to be related to the extent of phosphorylation of the P2 domain. Because the more flexible conformation may correspond to RyR2 with a phosphorylated P2 domain, we suggest that phosphorylation may set RyR2 in a conformation that needs less energy to transition to the open state. Comparison of RyR2 from cardiac muscle and RyR1 from skeletal muscle showed substantial structural differences between the two, especially in the helical domain 2 (HD2) structure forming the Clamp domain, which participates in quaternary interactions with the dihydropyridine receptor and neighboring RyRs in RyR1 but not in RyR2. Rigidity of the HD2 domain of RyR2 was enhanced by binding of FKBP12.6, a ligand that stabilizes RyR2 in the closed state. These results help to decipher the molecular basis of the different mechanisms of activation and oligomerization of the RyR isoforms and could be extended to RyR complexes in other tissues.
MeSH term(s)	Allosteric Site ; Animals ; Calcium/metabolism ; Cryoelectron Microscopy/methods ; Models, Molecular ; Myocardium/metabolism ; Phosphorylation ; Protein Binding ; Protein Conformation ; Rabbits ; Ryanodine Receptor Calcium Release Channel/chemistry ; Ryanodine Receptor Calcium Release Channel/metabolism ; Tacrolimus Binding Proteins/chemistry ; Tacrolimus Binding Proteins/metabolism
Chemical Substances	Ryanodine Receptor Calcium Release Channel ; Tacrolimus Binding Proteins (EC 5.2.1.-) ; tacrolimus binding protein 1B (EC 5.2.1.-) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2017-05-23
Publishing country	United States
Document type	Journal Article
ZDB-ID	2417226-1
ISSN	1937-9145 ; 1945-0877
ISSN (online)	1937-9145
ISSN	1945-0877
DOI	10.1126/scisignal.aai8842
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Article ; Online: Calcium/calmodulin-dependent kinase II and nitric oxide synthase 1-dependent modulation of ryanodine receptors during β-adrenergic stimulation is restricted to the dyadic cleft.

Dries, Eef / Santiago, Demetrio J / Johnson, Daniel M / Gilbert, Guillaume / Holemans, Patricia / Korte, Sanne M / Roderick, H Llewelyn / Sipido, Karin R

The Journal of physiology

2016 Volume 594, Issue 20, Page(s) 5923–5939

Abstract: Key points: The dyadic cleft, where coupled ryanodine receptors (RyRs) reside, is thought to serve as a microdomain for local signalling, as supported by distinct modulation of coupled RyRs dependent on Ca: Abstract: In cardiac myocytes, β-adrenergic ...

Abstract	Key points: The dyadic cleft, where coupled ryanodine receptors (RyRs) reside, is thought to serve as a microdomain for local signalling, as supported by distinct modulation of coupled RyRs dependent on Ca Abstract: In cardiac myocytes, β-adrenergic stimulation enhances Ca
MeSH term(s)	Adrenergic Agents/pharmacology ; Aniline Compounds/metabolism ; Animals ; Calcium/metabolism ; Calcium Signaling/drug effects ; Calcium Signaling/physiology ; Calcium-Binding Proteins/metabolism ; Calcium-Calmodulin-Dependent Protein Kinase Type 2/metabolism ; Calmodulin/metabolism ; Cyclic AMP-Dependent Protein Kinases/metabolism ; Myocytes, Cardiac/drug effects ; Myocytes, Cardiac/metabolism ; Nitric Oxide Synthase Type I/metabolism ; Receptors, Adrenergic, beta/metabolism ; Ryanodine Receptor Calcium Release Channel/metabolism ; Sarcoplasmic Reticulum/drug effects ; Sarcoplasmic Reticulum/metabolism ; Swine ; Xanthenes/metabolism
Chemical Substances	Adrenergic Agents ; Aniline Compounds ; Calcium-Binding Proteins ; Calmodulin ; Fluo 4 ; Receptors, Adrenergic, beta ; Ryanodine Receptor Calcium Release Channel ; Xanthenes ; phospholamban ; Nitric Oxide Synthase Type I (EC 1.14.13.39) ; Cyclic AMP-Dependent Protein Kinases (EC 2.7.11.11) ; Calcium-Calmodulin-Dependent Protein Kinase Type 2 (EC 2.7.11.17) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2016-10-15
Publishing country	England
Document type	Journal Article
ZDB-ID	3115-x
ISSN	1469-7793 ; 0022-3751
ISSN (online)	1469-7793
ISSN	0022-3751
DOI	10.1113/JP271965
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Article ; Online: Hyperactive ryanodine receptors in human heart failure and ischaemic cardiomyopathy reside outside of couplons.

Dries, Eef / Santiago, Demetrio J / Gilbert, Guillaume / Lenaerts, Ilse / Vandenberk, Bert / Nagaraju, Chandan K / Johnson, Daniel M / Holemans, Patricia / Roderick, H Llewelyn / Macquaide, Niall / Claus, Piet / Sipido, Karin R

Cardiovascular research

2018 Volume 114, Issue 11, Page(s) 1512–1524

Abstract: Aims: In ventricular myocytes from humans and large mammals, the transverse and axial tubular system (TATS) network is less extensive than in rodents with consequently a greater proportion of ryanodine receptors (RyRs) not coupled to this membrane ... ...

Abstract	Aims: In ventricular myocytes from humans and large mammals, the transverse and axial tubular system (TATS) network is less extensive than in rodents with consequently a greater proportion of ryanodine receptors (RyRs) not coupled to this membrane system. TATS remodelling in heart failure (HF) and after myocardial infarction (MI) increases the fraction of non-coupled RyRs. Here we investigate whether this remodelling alters the activity of coupled and non-coupled RyR sub-populations through changes in local signalling. We study myocytes from patients with end-stage HF, compared with non-failing (non-HF), and myocytes from pigs with MI and reduced left ventricular (LV) function, compared with sham intervention (SHAM). Methods and results: Single LV myocytes for functional studies were isolated according to standard protocols. Immunofluorescent staining visualized organization of TATS and RyRs. Ca2+ was measured by confocal imaging (fluo-4 as indicator) and using whole-cell patch-clamp (37°C). Spontaneous Ca2+ release events, Ca2+ sparks, as a readout for RyR activity were recorded during a 15 s period following conditioning stimulation at 2 Hz. Sparks were assigned to cell regions categorized as coupled or non-coupled sites according to a previously developed method. Human HF myocytes had more non-coupled sites and these had more spontaneous activity than in non-HF. Hyperactivity of these non-coupled RyRs was reduced by Ca2+/calmodulin-dependent kinase II (CaMKII) inhibition. Myocytes from MI pigs had similar changes compared with SHAM controls as seen in human HF myocytes. As well as by CaMKII inhibition, in MI, the increased activity of non-coupled sites was inhibited by mitochondrial reactive oxygen species (mito-ROS) scavenging. Under adrenergic stimulation, Ca2+ waves were more frequent and originated at non-coupled sites, generating larger Na+/Ca2+ exchange currents in MI than in SHAM. Inhibition of CaMKII or mito-ROS scavenging reduced spontaneous Ca2+ waves, and improved excitation-contraction coupling. Conclusions: In HF and after MI, RyR microdomain re-organization enhances spontaneous Ca2+ release at non-coupled sites in a manner dependent on CaMKII activation and mito-ROS production. This specific modulation generates a substrate for arrhythmia that appears to be responsive to selective pharmacologic modulation.
MeSH term(s)	Aged ; Animals ; Arrhythmias, Cardiac/metabolism ; Arrhythmias, Cardiac/physiopathology ; Calcium Signaling ; Calcium-Calmodulin-Dependent Protein Kinase Type 2/metabolism ; Cardiomyopathies/metabolism ; Cardiomyopathies/physiopathology ; Case-Control Studies ; Disease Models, Animal ; Excitation Contraction Coupling ; Female ; Heart Failure/metabolism ; Heart Failure/physiopathology ; Humans ; Male ; Membrane Potentials ; Middle Aged ; Mitochondria, Heart/metabolism ; Myocardial Contraction ; Myocardial Infarction/metabolism ; Myocardial Infarction/physiopathology ; Myocytes, Cardiac/metabolism ; NADPH Oxidase 2/metabolism ; Reactive Oxygen Species/metabolism ; Ryanodine Receptor Calcium Release Channel/metabolism ; Sodium-Calcium Exchanger/metabolism ; Sus scrofa ; Time Factors ; Ventricular Function, Left ; Ventricular Remodeling
Chemical Substances	Reactive Oxygen Species ; Ryanodine Receptor Calcium Release Channel ; Sodium-Calcium Exchanger ; NADPH Oxidase 2 (EC 1.6.3.-) ; Calcium-Calmodulin-Dependent Protein Kinase Type 2 (EC 2.7.11.17)
Language	English
Publishing date	2018-04-18
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80340-6
ISSN	1755-3245 ; 0008-6363
ISSN (online)	1755-3245
ISSN	0008-6363
DOI	10.1093/cvr/cvy088
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