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Article ; Online: Contribution of membrane raft redox signalling to visfatin-induced inflammasome activation and podocyte injury.

Koka, Saisudha / Surineni, Sreenidhi / Singh, Gurinder Bir / Boini, Krishna M

Aging

2023 Volume 15, Issue 22, Page(s) 12738–12748

Abstract: Recently we have shown that adipokine visfatin-induced NLRP3 inflammasome activation contributes to podocyte injury. However, the molecular mechanisms of how visfatin-induces the Nlrp3 inflammasome activation and podocyte damage is still unknown. The ... ...

Abstract	Recently we have shown that adipokine visfatin-induced NLRP3 inflammasome activation contributes to podocyte injury. However, the molecular mechanisms of how visfatin-induces the Nlrp3 inflammasome activation and podocyte damage is still unknown. The present study tested whether membrane raft (MR) redox signalling pathway plays a central role in visfatin-induced NLRP3 inflammasomes formation and activation in podocytes. Upon visfatin stimulation an aggregation of NADPH oxidase subunits, gp91phox and p47phox was observed in the membrane raft (MR) clusters, forming a MR redox signalling platform in podocytes. The formation of this signalling platform was blocked by prior treatment with MR disruptor MCD or NADPH oxidase inhibitor DPI. In addition, visfatin stimulation significantly increased the colocalization of Nlrp3 with Asc or Nlrp3 with caspase-1, IL-β production, cell permeability in podocytes compared to control cells. Pretreatment with MCD, DPI, WEHD significantly abolished the visfatin-induced colocalization of NLRP3 with Asc or NLRP3 with caspase-1, IL-1β production and cell permeability in podocytes. Furthermore, Immunofluorescence analysis demonstrated that visfatin treatment significantly decreased the podocin and nephrin expression (podocyte damage) and prior treatments with DPI, WEHD, MCD attenuated this visfatin-induced podocin and nephrin reduction. In conclusion, our results suggest that visfatin stimulates membrane raft clustering in the membrane of podocytes to form redox signaling platforms by aggregation and activation of NADPH oxidase subunits enhancing O
MeSH term(s)	Inflammasomes/metabolism ; Podocytes/metabolism ; NLR Family, Pyrin Domain-Containing 3 Protein/metabolism ; Nicotinamide Phosphoribosyltransferase/metabolism ; NADPH Oxidases/metabolism ; Caspase 1/metabolism ; Oxidation-Reduction
Chemical Substances	Inflammasomes ; NLR Family, Pyrin Domain-Containing 3 Protein ; Nicotinamide Phosphoribosyltransferase (EC 2.4.2.12) ; NADPH Oxidases (EC 1.6.3.-) ; Caspase 1 (EC 3.4.22.36)
Language	English
Publishing date	2023-11-17
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ISSN	1945-4589
ISSN (online)	1945-4589
DOI	10.18632/aging.205243
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: High Mobility Group Box 1 Mediates TMAO-Induced Endothelial Dysfunction.

Singh, Gurinder Bir / Zhang, Yang / Boini, Krishna M / Koka, Saisudha

International journal of molecular sciences

2019 Volume 20, Issue 14

Abstract: The intestinal microbe-derived metabolite trimethylamine N-oxide (TMAO) is implicated in the pathogenesis of cardiovascular diseases (CVDs). The molecular mechanisms of how TMAO induces atherosclerosis and CVDs' progression are still unclear. In this ... ...

Abstract	The intestinal microbe-derived metabolite trimethylamine N-oxide (TMAO) is implicated in the pathogenesis of cardiovascular diseases (CVDs). The molecular mechanisms of how TMAO induces atherosclerosis and CVDs' progression are still unclear. In this regard, high-mobility group box protein 1 (HMGB1), an inflammatory mediator, has been reported to disrupt cell-cell junctions, resulting in vascular endothelial hyper permeability leading to endothelial dysfunction. The present study tested whether TMAO associated endothelial dysfunction results via HMGB1 activation. Biochemical and RT-PCR analysis showed that TMAO increased the HMGB1 expression in a dose-dependent manner in endothelial cells. However, prior treatment with glycyrrhizin, an HMGB1 binder, abolished the TMAO-induced HMGB1 production in endothelial cells. Furthermore, Western blot and immunofluorescent analysis showed significant decrease in the expression of cell-cell junction proteins ZO-2, Occludin, and VE-cadherin in TMAO treated endothelial cells compared with control cells. However, prior treatment with glycyrrhizin attenuated the TMAO-induced cell-cell junction proteins' disruption. TMAO increased toll-like receptor 4 (TLR4) expression in endothelial cells. Inhibition of TLR4 expression by TLR4 siRNA protected the endothelial cells from TMAO associated tight junction protein disruption via HMGB1. In conclusion, our results demonstrate that HMGB1 is one of the important mediators of TMAO-induced endothelial dysfunction.
MeSH term(s)	Cells, Cultured ; Endothelial Cells/drug effects ; Endothelial Cells/metabolism ; Endothelium/drug effects ; Endothelium/metabolism ; Extracellular Space/metabolism ; HMGB1 Protein/metabolism ; Humans ; Intercellular Junctions/drug effects ; Intercellular Junctions/metabolism ; Methylamines/pharmacology ; Tight Junctions/drug effects ; Tight Junctions/metabolism ; Toll-Like Receptor 4/metabolism
Chemical Substances	HMGB1 Protein ; Methylamines ; TLR4 protein, human ; Toll-Like Receptor 4 ; trimethyloxamine (FLD0K1SJ1A)
Language	English
Publishing date	2019-07-22
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms20143570
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Article ; Online: High Mobility Group Box 1 Mediates TMAO-Induced Endothelial Dysfunction

Gurinder Bir Singh / Yang Zhang / Krishna M. Boini / Saisudha Koka

International Journal of Molecular Sciences, Vol 20, Iss 14, p

2019 Volume 3570

Abstract	The intestinal microbe-derived metabolite trimethylamine N-oxide (TMAO) is implicated in the pathogenesis of cardiovascular diseases (CVDs). The molecular mechanisms of how TMAO induces atherosclerosis and CVDs’ progression are still unclear. In this regard, high-mobility group box protein 1 (HMGB1), an inflammatory mediator, has been reported to disrupt cell−cell junctions, resulting in vascular endothelial hyper permeability leading to endothelial dysfunction. The present study tested whether TMAO associated endothelial dysfunction results via HMGB1 activation. Biochemical and RT-PCR analysis showed that TMAO increased the HMGB1 expression in a dose-dependent manner in endothelial cells. However, prior treatment with glycyrrhizin, an HMGB1 binder, abolished the TMAO-induced HMGB1 production in endothelial cells. Furthermore, Western blot and immunofluorescent analysis showed significant decrease in the expression of cell−cell junction proteins ZO-2, Occludin, and VE-cadherin in TMAO treated endothelial cells compared with control cells. However, prior treatment with glycyrrhizin attenuated the TMAO-induced cell−cell junction proteins’ disruption. TMAO increased toll-like receptor 4 (TLR4) expression in endothelial cells. Inhibition of TLR4 expression by TLR4 siRNA protected the endothelial cells from TMAO associated tight junction protein disruption via HMGB1. In conclusion, our results demonstrate that HMGB1 is one of the important mediators of TMAO-induced endothelial dysfunction.
Keywords	HMGB1 ; TMAO ; tight junction ; ZO2 ; glycyrrhizin ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
Language	English
Publishing date	2019-07-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
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Article ; Online: Podocyte NLRP3 Inflammasome Activation and Formation by Adipokine Visfatin.

Koka, Saisudha / Xia, Min / Zhang, Chun / Zhang, Yang / Li, Pin-Lan / Boini, Krishna M

Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology

2019 Volume 53, Issue 2, Page(s) 355–365

Abstract: Background/aims: NLRP3 inflammasome activation has been reported to be an early mechanism responsible for glomerular inflammation and injury in obese mice. However, the precise mechanism of obesity-induced NLRP3 inflammasome activation remains unknown. ... ...

Abstract	Background/aims: NLRP3 inflammasome activation has been reported to be an early mechanism responsible for glomerular inflammation and injury in obese mice. However, the precise mechanism of obesity-induced NLRP3 inflammasome activation remains unknown. The present study explored whether adipokine visfatin mediates obesity-induced NLRP3 inflammasome activation and consequent podocyte injury. Methods: Inflammasome formation and immunofluorescence expressions were quantified by confocal microscopy. Caspase-activity, IL-1β production and VEGF concentrations were measured by ELISA. Results: Confocal microscopic analysis showed that visfatin treatment increased the colocalization of Nlrp3 with Asc or Nlrp3 with caspase-1 in podocytes indicating the formation of NLRP3 inflammasomes. This visfatin-induced NLRP3 inflammasome formation was abolished by pretreatment of podocytes with Asc siRNA. Correspondingly, visfatin treatment significantly increased the caspase-1 activity and IL-1β production in podocytes, which was significantly attenuated by Asc siRNA transfection. Further RT-PCR and confocal microscopic analysis demonstrated that visfatin treatment significantly decreased the podocin expression (podocyte damage). Podocytes pretreatment with Asc siRNA or caspase-1 inhibitor, WEHD attenuated this visfatin-induced podocin reduction. Furthermore, Asc siRNA transfection was found to preserve podocyte morphology by maintaining the distinct arrangement of F-actin fibers normally lost in response to visfatin. It also prevented podocyte dysfunction by restoring visfatin-induced suppression of VEGF production and secretion. Conclusion: Visfatin induces NLRP3 inflammasome activation in podocytes and thereby resulting in podocyte injury.
MeSH term(s)	Adipokines/immunology ; Animals ; Cell Line ; Inflammasomes/immunology ; Inflammation/immunology ; Inflammation/pathology ; Interleukin-1beta/immunology ; Mice ; NLR Family, Pyrin Domain-Containing 3 Protein/immunology ; Nicotinamide Phosphoribosyltransferase/immunology ; Obesity/immunology ; Obesity/pathology ; Podocytes/cytology ; Podocytes/immunology ; Podocytes/pathology ; Vascular Endothelial Growth Factor A/immunology
Chemical Substances	Adipokines ; Inflammasomes ; Interleukin-1beta ; NLR Family, Pyrin Domain-Containing 3 Protein ; Nlrp3 protein, mouse ; Vascular Endothelial Growth Factor A ; vascular endothelial growth factor A, mouse ; Nicotinamide Phosphoribosyltransferase (EC 2.4.2.12)
Language	English
Publishing date	2019-05-14
Publishing country	Germany
Document type	Journal Article
ZDB-ID	1067572-3
ISSN	1421-9778 ; 1015-8987
ISSN (online)	1421-9778
ISSN	1015-8987
DOI	10.33594/000000143
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Article ; Online: Nicotine instigates podocyte injury via NLRP3 inflammasomes activation.

Singh, Gurinder Bir / Kshirasagar, Naresh / Patibandla, Sai / Puchchakayala, Goverdhan / Koka, Saisudha / Boini, Krishna M

Aging

2019 Volume 11, Issue 24, Page(s) 12810–12821

Abstract: Background/aims: Recent studies have shown that nicotine induces podocyte damage. However, it remains unknown how nicotine induces podocyte injury. The present study tested whether nicotine induces NLRP3 inflammasomes activation and thereby contributes ... ...

Abstract	Background/aims: Recent studies have shown that nicotine induces podocyte damage. However, it remains unknown how nicotine induces podocyte injury. The present study tested whether nicotine induces NLRP3 inflammasomes activation and thereby contributes to podocyte injury. Results: Nicotine treatment significantly increased the colocalization of NLRP3 with Asc, caspase-1 activity, IL-β production, cell permeability in podocytes compared to control cells. Pretreatment with caspase-1 inhibitor, WEHD significantly abolished the nicotine-induced colocalization of NLRP3 with Asc, caspase-1 activity, IL-1β production and cell permeability in podocytes. Immunofluorescence analysis showed that nicotine treatment significantly decreased the podocin and nephrin expression compared to control cells. However, prior treatment with WEHD attenuated the nicotine-induced podocin and nephrin reduction. In addition, we found that nicotine treatment significantly increased the O Conclusions: Nicotine-induced the NLRP3 inflammasome activation in podocytes and thereby results in podocyte injury. Methods: Inflammasome formation and immunofluorescence expressions were quantified by confocal microscopy. Caspase-1 activity, IL-1β production and O
MeSH term(s)	Adaptor Proteins, Signal Transducing/genetics ; Adaptor Proteins, Signal Transducing/metabolism ; Animals ; Apoptosis Regulatory Proteins/genetics ; Apoptosis Regulatory Proteins/metabolism ; Caspase 1/genetics ; Caspase 1/metabolism ; Cell Line ; Gene Expression Regulation/drug effects ; Inflammasomes/drug effects ; Inflammasomes/metabolism ; Interleukin-1beta/genetics ; Interleukin-1beta/metabolism ; Mice ; Nicotine/pharmacology ; Nicotinic Agonists/pharmacology ; Permeability ; Podocytes/drug effects ; Podocytes/metabolism
Chemical Substances	Adaptor Proteins, Signal Transducing ; Apoptosis Regulatory Proteins ; Inflammasomes ; Interleukin-1beta ; NALP1 protein, mouse ; Nicotinic Agonists ; Nicotine (6M3C89ZY6R) ; Caspase 1 (EC 3.4.22.36)
Language	English
Publishing date	2019-12-13
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	1945-4589
ISSN (online)	1945-4589
DOI	10.18632/aging.102611
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Article ; Online: Trimethylamine-N-Oxide Instigates NLRP3 Inflammasome Activation and Endothelial Dysfunction.

Boini, Krishna M / Hussain, Tahir / Li, Pin-Lan / Koka, Sai

Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology

2017 Volume 44, Issue 1, Page(s) 152–162

Abstract: Background/aim: Plasma trimethylamine-N-oxide (TMAO), a product of intestinal microbial metabolism of dietary phosphatidylcholine has been recently associated with atherosclerosis and increased risk of cardiovascular diseases (CVD) in rodents and humans. ...

Abstract	Background/aim: Plasma trimethylamine-N-oxide (TMAO), a product of intestinal microbial metabolism of dietary phosphatidylcholine has been recently associated with atherosclerosis and increased risk of cardiovascular diseases (CVD) in rodents and humans. However, the molecular mechanisms of how TMAO induces atherosclerosis and CVD progression are still unclear. The present study tested whether TMAO induces NLRP3 inflammasome formation and activation and thereby contributes to endothelial injury initiating atherogenesis. Methods: Inflammasome formation and activation was determined by confocal microscopy, caspase-1 activity was measured by colorimetric assay, IL-1β production was measured using ELISA, cell permeability was determined by microplate reader and ZO-1 expression was determined by western blot analysis and confocal microscopy. In in vivo experiments, TMAO was infused by osmotic pump implantation. Results: TMAO treatment significantly increased the colocalization of NLRP3 with Asc or NLRP3 with caspase-1, caspase-1 activity, IL-1β production, cell permeability in carotid artery endothelial cells (CAECs) compared to control cells. Pretreatment with caspase-1 inhibitor, WEHD or Nlrp3 siRNA abolished the TMAO-induced inflammasome formation, activation and cell permeability in these cells. In addition, we explored the mechanisms by which TMAO activates NLRP3 inflammasomes. TMAO-induced the activation of NLRP3 inflammasomes was associated with both redox regulation and lysosomal dysfunction. In animal experiments, direct infusion of TMAO in mice with partially ligated carotid artery were found to have increased NLRP3 inflammasome formation and IL-1β production in the intima of wild type mice. Conclusion: The formation and activation of NLRP3 inflammasomes by TMAO may be an important initiating mechanism to turn on the endothelial inflammatory response leading to endothelial dysfunction.
MeSH term(s)	Amino Acid Chloromethyl Ketones/pharmacology ; Animals ; Carotid Arteries/cytology ; Carotid Arteries/pathology ; Caspase 1/chemistry ; Caspase 1/metabolism ; Caspase Inhibitors/pharmacology ; Cells, Cultured ; Endothelial Cells/cytology ; Endothelial Cells/drug effects ; Endothelial Cells/metabolism ; Inflammasomes/drug effects ; Inflammasomes/metabolism ; Interleukin-1beta/metabolism ; Male ; Methylamines/toxicity ; Mice ; Mice, Inbred C57BL ; Microscopy, Fluorescence ; NLR Family, Pyrin Domain-Containing 3 Protein/antagonists & inhibitors ; NLR Family, Pyrin Domain-Containing 3 Protein/genetics ; NLR Family, Pyrin Domain-Containing 3 Protein/metabolism ; Permeability/drug effects ; RNA Interference ; RNA, Small Interfering/metabolism ; Signal Transduction/drug effects
Chemical Substances	Amino Acid Chloromethyl Ketones ; Caspase Inhibitors ; Inflammasomes ; Interleukin-1beta ; Methylamines ; NLR Family, Pyrin Domain-Containing 3 Protein ; RNA, Small Interfering ; benzyloxycarbonyltyrosyl-alanyl-valyl-aspartyl chloromethyl ketone ; Caspase 1 (EC 3.4.22.36) ; trimethyloxamine (FLD0K1SJ1A)
Language	English
Publishing date	2017-11-06
Publishing country	Germany
Document type	Journal Article
ZDB-ID	1067572-3
ISSN	1421-9778 ; 1015-8987
ISSN (online)	1421-9778
ISSN	1015-8987
DOI	10.1159/000484623
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Article ; Online: Tricyclic antidepressant amitriptyline inhibits autophagic flux and prevents tube formation in vascular endothelial cells.

Guan, Yinglu / Li, Xiang / Umetani, Michihisa / Boini, Krishna M / Li, Pin-Lan / Zhang, Yang

Basic & clinical pharmacology & toxicology

2018 Volume 124, Issue 4, Page(s) 370–384

Abstract: Amitriptyline is a tricyclic antidepressant and an inhibitor of lysosomal acid sphingomyelinase (ASM). Amitriptyline is well known for its cardiovascular side effects and toxicity in psychiatric patients. However, the mechanisms underlying the ... ...

Abstract	Amitriptyline is a tricyclic antidepressant and an inhibitor of lysosomal acid sphingomyelinase (ASM). Amitriptyline is well known for its cardiovascular side effects and toxicity in psychiatric patients. However, the mechanisms underlying the cardiovascular side effects of amitriptyline remain largely undefined. This study aimed to determine the effects of amitriptyline on angiogenic capability of vascular endothelial cells in physiological settings and identify its mechanism of action. The ex vivo aortic ring angiogenesis and in vitro-cultured endothelial cell tube formation assay were used to assess the effects of amitriptyline on endothelial angiogenic capability. It was demonstrated that amitriptyline impaired the angiogenesis of aortic rings, which was similar to that found in aortic rings with haploinsufficiency of the ASM gene. In cultured mouse microvascular endothelial cells (MVECs), amitriptyline impaired the proliferation and tube formation under basal condition, which were accompanied by attenuated angiogenic signalling pathways such as endothelial nitric oxide synthase, Akt and Erk1/2 pathways. Mechanistically, amitriptyline inhibited autophagic flux without affecting autophagosome biogenesis at basal condition. ASM gene silencing or autophagy inhibition mimics the inhibitory effects of amitriptyline on endothelial cell proliferation and tube formation. Collectively, our data suggest that amitriptyline inhibits endothelial cell proliferation and angiogenesis via blockade of ASM-autophagic flux axis. It is implicated that the cardiovascular side effects of amitriptyline may be associated with its inhibitory action on physiological angiogenesis.
MeSH term(s)	Amitriptyline/toxicity ; Animals ; Antidepressive Agents, Tricyclic/toxicity ; Aorta, Thoracic/drug effects ; Aorta, Thoracic/pathology ; Autophagy/drug effects ; Cell Proliferation/drug effects ; Cells, Cultured ; Endothelial Cells/drug effects ; Endothelial Cells/pathology ; Gene Knockdown Techniques ; Male ; Mice ; Mice, Inbred C57BL ; Neovascularization, Physiologic/drug effects ; Signal Transduction/drug effects
Chemical Substances	Antidepressive Agents, Tricyclic ; Amitriptyline (1806D8D52K)
Language	English
Publishing date	2018-11-15
Publishing country	England
Document type	Journal Article
ZDB-ID	2134679-3
ISSN	1742-7843 ; 1742-7835
ISSN (online)	1742-7843
ISSN	1742-7835
DOI	10.1111/bcpt.13146
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Article ; Online: Inflammasome Activation in Chronic Glomerular Diseases.

Conley, Sabena M / Abais, Justine M / Boini, Krishna M / Li, Pin-Lan

Current drug targets

2016 Volume 18, Issue 9, Page(s) 1019–1029

Abstract: Background: The intracellular multiprotein complex termed the inflammasome functions as a platform of pro-inflammatory cytokine production such as IL-1β and IL-18. Under certain conditions, however, the inflammasome produces non-canonical effects such ... ...

Abstract	Background: The intracellular multiprotein complex termed the inflammasome functions as a platform of pro-inflammatory cytokine production such as IL-1β and IL-18. Under certain conditions, however, the inflammasome produces non-canonical effects such as induction of cell death, pyroptosis and cell metabolism alterations. Objective: In mammalian cells, several types of inflammasomes were identified, but the most widely studied one is the inflammasome containing NOD-like receptor with pyrin domain 3 (NLRP3), which has recently been reported as a central pathogenic mechanism of chronic degenerative diseases. Many activators or risk factors exert their actions through the activation of the NLRP3 inflammasome to produce a variety of functional changes in different cells including inflammatory, metabolic or survival responses. Several molecular signaling pathways are shown to mediate the activation of the NLRP3 inflammasome, and they are related to the modifications in K+ efflux, increased lysosome leakage and activation of cathepsin B or enhanced reactive oxygen species (ROS) production. In the kidney, inflammation is believed to mediate or promote the progression of glomerular sclerotic pathologies resulting in end-stage renal disease (ESRD). NLRP3 inflammasome activation may turn on glomerular inflammation and other cell damages, contributing to the onset of glomerular injury and ESRD. This inflammasome activation not only occurs in immune cells, but also in residential cells such as endothelial cells and podocytes in the glomeruli. Summary: This review briefly summarizes current evidence of NLRP3 inflammasome activation and related molecular mechanisms in renal glomeruli. The possible canonical and non-canonical effects of this inflammasome activation and its potential implication in the development of different glomerular diseases are highlighted.
MeSH term(s)	Chronic Disease ; Glomerulonephritis/immunology ; Glomerulonephritis/metabolism ; Glomerulonephritis/therapy ; Humans ; Inflammasomes/immunology ; Inflammasomes/metabolism ; Kidney Glomerulus/metabolism ; NLR Family, Pyrin Domain-Containing 3 Protein/metabolism
Chemical Substances	Inflammasomes ; NLR Family, Pyrin Domain-Containing 3 Protein ; NLRP3 protein, human
Language	English
Publishing date	2016-06-13
Publishing country	United Arab Emirates
Document type	Journal Article ; Review
ZDB-ID	2064859-5
ISSN	1873-5592 ; 1389-4501
ISSN (online)	1873-5592
ISSN	1389-4501
DOI	10.2174/1389450117666160817103435
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Zs.A 5578: Show issues

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Article: Risk factors associated with saphenous vein graft aneurysm after coronary artery bypass graft.

Ghosh, Bikona / SIbi Krishna, Thiyagarajan / Boini, Aishwarya / Castillo Miranda, Jose C D / Sinha, Mehul / Bansal, Radha / Visconti-Lopez, Fabriccio J / Mesfin Girma, Samuel / Aliye Asfaw, Yonathan

Annals of medicine and surgery (2012)

2023 Volume 85, Issue 11, Page(s) 5604–5610

Abstract: Introduction: Saphenous vein graft aneurysm (SVGA) is a rare but life-threatening complication following coronary artery bypass grafting (CABG). The authors aim to identify the potential risk factors that lead to SVGA in post-CABG patients.: Methods: ...

Abstract	Introduction: Saphenous vein graft aneurysm (SVGA) is a rare but life-threatening complication following coronary artery bypass grafting (CABG). The authors aim to identify the potential risk factors that lead to SVGA in post-CABG patients. Methods: A systematic review of original studies, observational studies, systematic reviews, meta-analyses, case studies, and case series was conducted using PubMed, Web of Science, Scopus, EMBASE, and Google Scholar involving adult patients (>18) with SVGA after CABG using MESH terminology in a broad search strategy. All searches were performed and analyzed according to PRISMA and duplicates were removed via Rayyan. Two independent investigators extracted and assessed the data involving demographics, and baseline data related to CABG and its manifestations. Results: Out of 487 finalized articles, 14 of them matched the inclusion requirements and reported 12 cases of SVGAs following CABG. Atherosclerosis with intimal calcification was the most common risk factor followed by infection. Others included hyperlipidemia, pneumonia, and cardiac pathologies mostly related to the ventricles and valves. Conclusion: Atherosclerosis associated with intimal calcification is the most common risk factor. Patient outcomes seem to improve upon early identification and regular follow-up imaging. The exclusion criteria indicated the study's limits, and future studies that address these constraints may be able to better understand the risk variables involved in the genesis of SVGA.
Language	English
Publishing date	2023-09-08
Publishing country	England
Document type	Journal Article
ZDB-ID	2745440-X
ISSN	2049-0801
ISSN	2049-0801
DOI	10.1097/MS9.0000000000001289
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Article ; Online: Sphingolipids in obesity and related complications.

Boini, Krishna M / Xia, Min / Koka, Saisudha / Gehr, Todd W B / Li, Pin-Lan

Frontiers in bioscience (Landmark edition)

2017 Volume 22, Issue 1, Page(s) 96–116

Abstract: Sphingolipids are biologically active lipids ubiquitously produced in all vertebrate cells. Asides from structural components of cell membrane, sphingolipids also function as intracellular and extracellular mediators that regulate many important ... ...

Abstract	Sphingolipids are biologically active lipids ubiquitously produced in all vertebrate cells. Asides from structural components of cell membrane, sphingolipids also function as intracellular and extracellular mediators that regulate many important physiological cellular processes including cell survival, proliferation, apoptosis, differentiation, migration and immune processes. Recent studies have also indicated that disruption of sphingolipid metabolism is strongly associated with different diseases that exhibit diverse neurological and metabolic consequences. Here, we briefly summarize current evidence for understanding of sphingolipid pathways in obesity and associated complications. The regulation of sphingolipids and their enzymes may have a great impact in the development of novel therapeutic modalities for a variety of metabolic diseases.
MeSH term(s)	Adipokines/biosynthesis ; Adipose Tissue/metabolism ; Animals ; Atherosclerosis/etiology ; Atherosclerosis/metabolism ; Diabetes Mellitus/etiology ; Diabetes Mellitus/metabolism ; Energy Intake ; Humans ; Hypertension/etiology ; Hypertension/metabolism ; Inflammasomes/metabolism ; Insulin Resistance ; Obesity/complications ; Obesity/etiology ; Obesity/metabolism ; Oxidative Stress ; Renal Insufficiency, Chronic/etiology ; Renal Insufficiency, Chronic/metabolism ; Sphingolipids/antagonists & inhibitors ; Sphingolipids/metabolism
Chemical Substances	Adipokines ; Inflammasomes ; Sphingolipids
Language	English
Publishing date	2017-01-01
Publishing country	Singapore
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	2704569-9
ISSN	2768-6698 ; 1093-9946
ISSN (online)	2768-6698
ISSN	1093-9946
DOI	10.2741/4474
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