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Article ; Online: β

Ou, Ziwei / Dolmatova, Elena / Lassègue, Bernard / Griendling, Kathy K

American journal of physiology. Heart and circulatory physiology

2020 Volume 320, Issue 2, Page(s) H734–H739

Abstract: The integrin family, an indispensable part of cell-cell and cell-matrix interactions, consists of a group of heterodimeric adhesion receptors formed by α- and β-integrin subunits. Their wide expression and unique bidirectional signaling pathways allow ... ...

Abstract	The integrin family, an indispensable part of cell-cell and cell-matrix interactions, consists of a group of heterodimeric adhesion receptors formed by α- and β-integrin subunits. Their wide expression and unique bidirectional signaling pathways allow them to play roles in a variety of biological activities including blood clot formation, cell attachment, and migration. Evidence suggests that integrins are essential regulators of the initiation of acute inflammation, especially two key aspects of this process i.e., vascular permeability and leukocyte recruitment. This mini-review discusses the importance of integrins at the onset of the acute inflammatory response and outlines research advances regarding the function of integrins and their modulators at different stages of this process. Insights into the fine-tuning of integrin signaling during acute inflammation may inspire the design of new drugs for inflammatory diseases.
MeSH term(s)	Animals ; CD18 Antigens/metabolism ; Capillary Permeability ; Cell Adhesion ; Cell Communication ; Chemotaxis, Leukocyte ; Endothelium, Vascular/immunology ; Endothelium, Vascular/metabolism ; Endothelium, Vascular/physiopathology ; Humans ; Inflammation/immunology ; Inflammation/metabolism ; Inflammation/physiopathology ; Inflammation Mediators/metabolism ; Integrin beta1/metabolism ; Leukocyte Rolling ; Leukocytes/immunology ; Leukocytes/metabolism ; Signal Transduction ; Transendothelial and Transepithelial Migration
Chemical Substances	CD18 Antigens ; Inflammation Mediators ; Integrin beta1
Language	English
Publishing date	2020-12-18
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	603838-4
ISSN	1522-1539 ; 0363-6135
ISSN (online)	1522-1539
ISSN	0363-6135
DOI	10.1152/ajpheart.00518.2020
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Article ; Online: How does the chloride/proton antiporter ClC-3 control NADPH oxidase?

Lassègue, Bernard

Circulation research

2007 Volume 101, Issue 7, Page(s) 648–650

MeSH term(s)	Animals ; Antiporters/physiology ; Chloride Channels/physiology ; Humans ; NADPH Oxidases/metabolism ; NADPH Oxidases/physiology ; Proton Pumps/physiology
Chemical Substances	Antiporters ; Chloride Channels ; ClC-3 channel ; Proton Pumps ; NADPH Oxidases (EC 1.6.3.-)
Language	English
Publishing date	2007-09-28
Publishing country	United States
Document type	Editorial ; Research Support, N.I.H., Extramural ; 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.107.161869
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Article ; Online: Polymerase δ-interacting Protein 2: A Multifunctional Protein.

Hernandes, Marina S / Lassègue, Bernard / Griendling, Kathy K

Journal of cardiovascular pharmacology

2017 Volume 69, Issue 6, Page(s) 335–342

Abstract: Polymerase δ-interacting protein 2 (Poldip2) is a multifunctional protein originally described as a binding partner of the p50 subunit of DNA polymerase δ and proliferating cell nuclear antigen. In addition to its role in DNA replication and damage ... ...

Abstract	Polymerase δ-interacting protein 2 (Poldip2) is a multifunctional protein originally described as a binding partner of the p50 subunit of DNA polymerase δ and proliferating cell nuclear antigen. In addition to its role in DNA replication and damage repair, Poldip2 has been implicated in mitochondrial function, extracellular matrix regulation, cell cycle progression, focal adhesion turnover, and cell migration. However, Poldip2 functions are incompletely understood. In this review, we discuss recent literature on Poldip2 tissue distribution, subcellular localization, and function. We also address the putative function of Poldip2 in cardiovascular disease, neurodegenerative conditions and in renal pathophysiology.
Language	English
Publishing date	2017-06
Publishing country	United States
Document type	Journal Article
ZDB-ID	391970-5
ISSN	1533-4023 ; 0160-2446
ISSN (online)	1533-4023
ISSN	0160-2446
DOI	10.1097/FJC.0000000000000465
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Article ; Online: Myeloid Poldip2 Contributes to the Development of Pulmonary Inflammation by Regulating Neutrophil Adhesion in a Murine Model of Acute Respiratory Distress Syndrome.

Ou, Ziwei / Dolmatova, Elena / Mandavilli, Rohan / Qu, Hongyan / Gafford, Georgette / White, Taylor / Valdivia, Alejandra / Lassègue, Bernard / Hernandes, Marina S / Griendling, Kathy K

Journal of the American Heart Association

2022 Volume 11, Issue 10, Page(s) e025181

Abstract: Background Lung injury, a severe adverse outcome of lipopolysaccharide-induced acute respiratory distress syndrome, is attributed to excessive neutrophil recruitment and effector response. Poldip2 (polymerase δ-interacting protein 2) plays a critical ... ...

Abstract	Background Lung injury, a severe adverse outcome of lipopolysaccharide-induced acute respiratory distress syndrome, is attributed to excessive neutrophil recruitment and effector response. Poldip2 (polymerase δ-interacting protein 2) plays a critical role in regulating endothelial permeability and leukocyte recruitment in acute inflammation. Thus, we hypothesized that
MeSH term(s)	Animals ; Cell Adhesion ; Disease Models, Animal ; Focal Adhesion Kinase 2/metabolism ; Integrins/metabolism ; Lipopolysaccharides/pharmacology ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Mitochondrial Proteins/genetics ; Mitochondrial Proteins/metabolism ; Neutrophils/metabolism ; Neutrophils/pathology ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; Pneumonia/genetics ; Pneumonia/metabolism ; Pneumonia/pathology ; Respiratory Distress Syndrome/genetics ; Respiratory Distress Syndrome/metabolism ; Respiratory Distress Syndrome/pathology
Chemical Substances	Integrins ; Lipopolysaccharides ; Mitochondrial Proteins ; Nuclear Proteins ; mitogenin 1 protein, mouse ; Focal Adhesion Kinase 2 (EC 2.7.10.2)
Language	English
Publishing date	2022-05-10
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	2653953-6
ISSN	2047-9980 ; 2047-9980
ISSN (online)	2047-9980
ISSN	2047-9980
DOI	10.1161/JAHA.121.025181
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Article ; Online: Correction: Platelet-derived growth factor (PDGF) regulates slingshot phosphatase activity via Nox1-dependent auto-dephosphorylation of serine 834 in vascular smooth muscle cells.

Maheswaranathan, Mithu / Gole, Hope K A / Fernandez, Isabel / Lassègue, Bernard / Griendling, Kathy K / San Martín, Alejandra

The Journal of biological chemistry

2020 Volume 295, Issue 24, Page(s) 8348

Language	English
Publishing date	2020-06-12
Publishing country	United States
Document type	Journal Article ; Published Erratum
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.AAC120.014380
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Article ; Online: The cofilin phosphatase slingshot homolog 1 restrains angiotensin II-induced vascular hypertrophy and fibrosis in vivo.

Williams, Holly C / Ma, Jing / Weiss, Daiana / Lassègue, Bernard / Sutliff, Roy L / San Martín, Alejandra

Laboratory investigation; a journal of technical methods and pathology

2018 Volume 99, Issue 3, Page(s) 399–410

Abstract: The dual specificity phosphatase slingshot homolog 1 (SSH1) contributes to actin remodeling by dephosphorylating and activating the actin-severing protein cofilin. The reorganization of the actin cytoskeleton has been implicated in chronic hypertension ... ...

Abstract	The dual specificity phosphatase slingshot homolog 1 (SSH1) contributes to actin remodeling by dephosphorylating and activating the actin-severing protein cofilin. The reorganization of the actin cytoskeleton has been implicated in chronic hypertension and the subsequent mechano-adaptive rearrangement of vessel wall components. Therefore, using a novel Ssh1
MeSH term(s)	Angiotensin II/metabolism ; Animals ; Aorta/metabolism ; Aorta/pathology ; Disease Models, Animal ; Female ; Fibrosis ; Hypertension/etiology ; Hypertension/metabolism ; Hypertension/pathology ; Hypertrophy ; Male ; Mice ; Mice, 129 Strain ; Mice, Inbred C57BL ; Mice, Knockout ; Phosphoprotein Phosphatases/deficiency ; Phosphoprotein Phosphatases/genetics ; Phosphoprotein Phosphatases/metabolism ; Transforming Growth Factor beta1/metabolism ; Vascular Remodeling/genetics ; Vascular Remodeling/physiology
Chemical Substances	Tgfb1 protein, mouse ; Transforming Growth Factor beta1 ; Angiotensin II (11128-99-7) ; Phosphoprotein Phosphatases (EC 3.1.3.16) ; SSH1 protein, mouse (EC 3.1.3.16)
Language	English
Publishing date	2018-10-05
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	80178-1
ISSN	1530-0307 ; 0023-6837
ISSN (online)	1530-0307
ISSN	0023-6837
DOI	10.1038/s41374-018-0116-6
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Article ; Online: Poldip2 controls leukocyte infiltration into the ischemic brain by regulating focal adhesion kinase-mediated VCAM-1 induction.

Eidson, Lori N / Gao, Qingzeng / Qu, Hongyan / Kikuchi, Daniel S / Campos, Ana Carolina P / Faidley, Elizabeth A / Sun, Yu-Yo / Kuan, Chia-Yi / Pagano, Rosana L / Lassègue, Bernard / Tansey, Malú G / Griendling, Kathy K / Hernandes, Marina S

Scientific reports

2021 Volume 11, Issue 1, Page(s) 5533

Abstract: Stroke is a multiphasic process involving a direct ischemic brain injury which is then exacerbated by the influx of immune cells into the brain tissue. Activation of brain endothelial cells leads to the expression of adhesion molecules such vascular cell ...

Abstract	Stroke is a multiphasic process involving a direct ischemic brain injury which is then exacerbated by the influx of immune cells into the brain tissue. Activation of brain endothelial cells leads to the expression of adhesion molecules such vascular cell adhesion molecule 1 (VCAM-1) on endothelial cells, further increasing leukocyte recruitment. Polymerase δ-interacting protein 2 (Poldip2) promotes brain vascular inflammation and leukocyte recruitment via unknown mechanisms. This study aimed to define the role of Poldip2 in mediating vascular inflammation and leukocyte recruitment following cerebral ischemia. Cerebral ischemia was induced in Poldip2
MeSH term(s)	Animals ; Brain/metabolism ; Brain Ischemia/genetics ; Brain Ischemia/metabolism ; Focal Adhesion Kinase 1/genetics ; Focal Adhesion Kinase 1/metabolism ; Ischemic Stroke/genetics ; Ischemic Stroke/metabolism ; Leukocytes/metabolism ; Mice ; Mice, Mutant Strains ; Mitochondrial Proteins/genetics ; Mitochondrial Proteins/metabolism ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; Vascular Cell Adhesion Molecule-1/genetics ; Vascular Cell Adhesion Molecule-1/metabolism
Chemical Substances	Mitochondrial Proteins ; Nuclear Proteins ; Vascular Cell Adhesion Molecule-1 ; mitogenin 1 protein, mouse ; Focal Adhesion Kinase 1 (EC 2.7.10.2) ; Ptk2 protein, mouse (EC 2.7.10.2)
Language	English
Publishing date	2021-03-10
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-021-84987-z
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Article ; Online: Characterization of Poldip2 knockout mice: Avoiding incorrect gene targeting.

Lassègue, Bernard / Kumar, Sandeep / Mandavilli, Rohan / Wang, Keke / Tsai, Michelle / Kang, Dong-Won / Demos, Catherine / Hernandes, Marina S / San Martín, Alejandra / Taylor, W Robert / Jo, Hanjoong / Griendling, Kathy K

PloS one

2021 Volume 16, Issue 12, Page(s) e0247261

Abstract: POLDIP2 is a multifunctional protein whose roles are only partially understood. Our laboratory previously reported physiological studies performed using a mouse gene trap model, which suffered from three limitations: perinatal lethality in homozygotes, ... ...

Abstract	POLDIP2 is a multifunctional protein whose roles are only partially understood. Our laboratory previously reported physiological studies performed using a mouse gene trap model, which suffered from three limitations: perinatal lethality in homozygotes, constitutive Poldip2 inactivation and inadvertent downregulation of the adjacent Tmem199 gene. To overcome these limitations, we developed a new conditional floxed Poldip2 model. The first part of the present study shows that our initial floxed mice were affected by an unexpected mutation, which was not readily detected by Southern blotting and traditional PCR. It consisted of a 305 kb duplication around Poldip2 with retention of the wild type allele and could be traced back to the original targeted ES cell clone. We offer simple suggestions to rapidly detect similar accidents, which may affect genome editing using both traditional and CRISPR-based methods. In the second part of the present study, correctly targeted floxed Poldip2 mice were generated and used to produce a new constitutive knockout line by crossing with a Cre deleter. In contrast to the gene trap model, many homozygous knockout mice were viable, in spite of having no POLDIP2 expression. To further characterize the effects of Poldip2 ablation in the vasculature, RNA-seq and RT-qPCR experiments were performed in constitutive knockout arteries. Results show that POLDIP2 inactivation affects multiple cellular processes and provide new opportunities for future in-depth study of its functions.
MeSH term(s)	Animals ; CRISPR-Cas Systems ; Gene Targeting ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Mice ; Mice, Knockout ; Mitochondrial Proteins/deficiency ; Mitochondrial Proteins/metabolism ; Mouse Embryonic Stem Cells/metabolism ; Nuclear Proteins/deficiency ; Nuclear Proteins/metabolism ; RNA-Seq
Chemical Substances	Membrane Proteins ; Mitochondrial Proteins ; Nuclear Proteins ; mitogenin 1 protein, mouse
Language	English
Publishing date	2021-12-20
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2267670-3
ISSN	1932-6203 ; 1932-6203
ISSN (online)	1932-6203
ISSN	1932-6203
DOI	10.1371/journal.pone.0247261
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Article ; Online: Endothelial Poldip2 regulates sepsis-induced lung injury via Rho pathway activation.

Dolmatova, Elena V / Forrester, Steven J / Wang, Keke / Ou, Ziwei / Williams, Holly C / Joseph, Giji / Kumar, Sandeep / Valdivia, Alejandra / Kowalczyk, Andrew P / Qu, Hongyan / Jo, Hanjoong / Lassègue, Bernard / Hernandes, Marina S / Griendling, Kathy K

Cardiovascular research

2021 Volume 118, Issue 11, Page(s) 2506–2518

Abstract: Aims: Sepsis-induced lung injury is associated with significant morbidity and mortality. Previously, we showed that heterozygous deletion of polymerase δ-interacting protein 2 (Poldip2) was protective against sepsis-induced lung injury. Since ... ...

Abstract	Aims: Sepsis-induced lung injury is associated with significant morbidity and mortality. Previously, we showed that heterozygous deletion of polymerase δ-interacting protein 2 (Poldip2) was protective against sepsis-induced lung injury. Since endothelial barrier disruption is thought to be the main mechanism of sepsis-induced lung injury, we sought to determine if the observed protection was specifically due to the effect of reduced endothelial Poldip2. Methods and results: Endothelial-specific Poldip2 knock-out mice (EC-/-) and their wild-type littermates (EC+/+) were injected with saline or lipopolysaccharide (18 mg/kg) to model sepsis-induced lung injury. At 18 h post-injection mice, were euthanized and bronchoalveolar lavage (BAL) fluid and lung tissue were collected to assess leucocyte infiltration. Poldip2 EC-/- mice showed reduced lung leucocyte infiltration in BAL (0.21 ± 0.9×106 vs. 1.29 ± 1.8×106 cells/mL) and lung tissue (12.7 ± 1.8 vs. 23 ± 3.7% neutrophils of total number of cells) compared to Poldip2 EC+/+ mice. qPCR analysis of the lung tissue revealed a significantly dampened induction of inflammatory gene expression (TNFα 2.23 ± 0.39 vs. 4.15 ± 0.5-fold, IκBα 4.32 ± 1.53 vs. 8.97 ± 1.59-fold), neutrophil chemoattractant gene expression (CXCL1 68.8 ± 29.6 vs. 147 ± 25.7-fold, CXCL2 65 ± 25.6 vs. 215 ± 27.3-fold) and a marker of endothelial activation (VCAM1 1.25 ± 0.25 vs. 3.8 ± 0.38-fold) in Poldip2 EC-/- compared to Poldip2 EC+/+ lungs. An in vitro model using human pulmonary microvascular endothelial cells was used to assess the effect of Poldip2 knock-down on endothelial activation and permeability. TNFα-induced endothelial permeability and VE-cadherin disruption were significantly reduced with siRNA-mediated knock-down of Poldip2 (5 ± 0.5 vs. 17.5 ± 3-fold for permeability, 1.5 ± 0.4 vs. 10.9 ± 1.3-fold for proportion of disrupted VE-cadherin). Poldip2 knock-down altered expression of Rho-GTPase-related genes, which correlated with reduced RhoA activation by TNFα (0.94 ± 0.05 vs. 1.29 ± 0.01 of relative RhoA activity) accompanied by redistribution of active-RhoA staining to the centre of the cell. Conclusion: Poldip2 is a potent regulator of endothelial dysfunction during sepsis-induced lung injury, and its endothelium-specific inhibition may provide clinical benefit.
MeSH term(s)	Animals ; Endothelium/metabolism ; Humans ; Lung/metabolism ; Lung Injury/genetics ; Mice ; Mitochondrial Proteins/genetics ; Mitochondrial Proteins/metabolism ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; Sepsis/complications ; Sepsis/genetics ; Sepsis/metabolism ; Tumor Necrosis Factor-alpha/metabolism
Chemical Substances	Mitochondrial Proteins ; Nuclear Proteins ; POLDIP2 protein, human ; Tumor Necrosis Factor-alpha ; mitogenin 1 protein, mouse
Language	English
Publishing date	2021-12-02
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	80340-6
ISSN	1755-3245 ; 0008-6363
ISSN (online)	1755-3245
ISSN	0008-6363
DOI	10.1093/cvr/cvab295
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Article ; Online: Polymerase-δ-interacting protein 2 activates the RhoGEF epithelial cell transforming sequence 2 in vascular smooth muscle cells.

Huff, Lauren Parker / Kikuchi, Daniel Seicho / Faidley, Elizabeth / Forrester, Steven J / Tsai, Michelle Z / Lassègue, Bernard / Griendling, Kathy K

American journal of physiology. Cell physiology

2019 Volume 316, Issue 5, Page(s) C621–C631

Abstract: Polymerase-δ-interacting protein 2 (Poldip2) controls a wide variety of cellular functions and vascular pathologies. To mediate these effects, Poldip2 interacts with numerous proteins and generates reactive oxygen species via the enzyme NADPH oxidase 4 ( ... ...

Abstract	Polymerase-δ-interacting protein 2 (Poldip2) controls a wide variety of cellular functions and vascular pathologies. To mediate these effects, Poldip2 interacts with numerous proteins and generates reactive oxygen species via the enzyme NADPH oxidase 4 (Nox4). We have previously shown that Poldip2 can activate the Rho family GTPase RhoA, another signaling node within the cell. In this study, we aimed to better understand how Poldip2 activates Rho family GTPases and the functions of the involved proteins in vascular smooth muscle cells (VSMCs). RhoA is activated by guanine nucleotide exchange factors. Using nucleotide-free RhoA (isolated from bacteria) to pulldown active RhoGEFs, we found that the RhoGEF epithelial cell transforming sequence 2 (Ect2) is activated by Poldip2. Ect2 is a critical RhoGEF for Poldip2-mediated RhoA activation, because siRNA against Ect2 prevented Poldip2-mediated RhoA activity (measured by rhotekin pulldowns). Surprisingly, we were unable to detect a direct interaction between Poldip2 and Ect2, as they did not coimmunoprecipitate. Nox4 is not required for Poldip2-driven Ect2 activation, as Poldip2 overexpression induced Ect2 activation in Nox4 knockout VSMCs similar to wild-type cells. However, antioxidant treatment blocked Poldip2-induced Ect2 activation. This indicates a novel reactive oxygen species-driven mechanism by which Poldip2 regulates Rho family GTPases. Finally, we examined the function of these proteins in VSMCs, using siRNA against Poldip2 or Ect2 and determined that Poldip2 and Ect2 are both essential for vascular smooth muscle cell cytokinesis and proliferation.
MeSH term(s)	Animals ; Cell Proliferation/physiology ; HEK293 Cells ; Humans ; Male ; Mice ; Mice, Inbred C57BL ; Muscle, Smooth, Vascular/cytology ; Muscle, Smooth, Vascular/metabolism ; Nuclear Proteins/antagonists & inhibitors ; Nuclear Proteins/metabolism ; Proto-Oncogene Proteins/antagonists & inhibitors ; Proto-Oncogene Proteins/metabolism ; RNA, Small Interfering/pharmacology ; Rats ; Rats, Sprague-Dawley ; Rho Guanine Nucleotide Exchange Factors/metabolism
Chemical Substances	ECT2 protein, human ; Nuclear Proteins ; POLDIP2 protein, human ; Proto-Oncogene Proteins ; RNA, Small Interfering ; Rho Guanine Nucleotide Exchange Factors
Language	English
Publishing date	2019-02-06
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	392098-7
ISSN	1522-1563 ; 0363-6143
ISSN (online)	1522-1563
ISSN	0363-6143
DOI	10.1152/ajpcell.00208.2018
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