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Article: Impact of extracellular vesicles on the pathogenesis, diagnosis, and potential therapy in cardiopulmonary disease.

Soto-Vázquez, Yixel M / Genschmer, Kristopher R

2023 Volume 14, Page(s) 1081015

Abstract: Cardiopulmonary diseases span a wide breadth of conditions affecting both heart and lung, the burden of which is globally significant. Chronic pulmonary disease and cardiovascular disease are two of the leading causes of morbidity and mortality worldwide. ...

Abstract	Cardiopulmonary diseases span a wide breadth of conditions affecting both heart and lung, the burden of which is globally significant. Chronic pulmonary disease and cardiovascular disease are two of the leading causes of morbidity and mortality worldwide. This makes it critical to understand disease pathogenesis, thereby providing new diagnostic and therapeutic avenues to improve clinical outcomes. Extracellular vesicles provide insight into all three of these features of the disease. Extracellular vesicles are membrane-bound vesicles released by a multitude, if not all, cell types and are involved in multiple physiological and pathological processes that play an important role in intercellular communication. They can be isolated from bodily fluids, such as blood, urine, and saliva, and their contents include a variety of proteins, proteases, and microRNA. These vesicles have shown to act as effective transmitters of biological signals within the heart and lung and have roles in the pathogenesis and diagnosis of multiple cardiopulmonary diseases as well as demonstrate potential as therapeutic agents to treat said conditions. In this review article, we will discuss the role these extracellular vesicles play in the diagnosis, pathogenesis, and therapeutic possibilities of cardiovascular, pulmonary, and infection-related cardiopulmonary diseases.
Language	English
Publishing date	2023-02-20
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2587355-6
ISSN	1663-9812
ISSN	1663-9812
DOI	10.3389/fphar.2023.1081015
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Article ; Online: Neutrophil elastase-dependent cleavage of LTA4H alters its aminopeptidase activity in cystic fibrosis.

Xu, Xin / Li, Jin-Dong / Green, Todd J / Wilson, Landon / Genschmer, Kristopher / Russell, Derek / Blalock, J Edwin / Gaggar, Amit

The European respiratory journal

2024 Volume 63, Issue 3

MeSH term(s)	Humans ; Leukocyte Elastase ; Cystic Fibrosis ; Proteolysis ; Aminopeptidases/genetics ; Neutrophils
Chemical Substances	Leukocyte Elastase (EC 3.4.21.37) ; Aminopeptidases (EC 3.4.11.-)
Language	English
Publishing date	2024-03-07
Publishing country	England
Document type	Letter
ZDB-ID	639359-7
ISSN	1399-3003 ; 0903-1936
ISSN (online)	1399-3003
ISSN	0903-1936
DOI	10.1183/13993003.01512-2023
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Article ; Online: Extracellular Vesicles as Central Mediators of COPD Pathophysiology.

Russell, Derek W / Genschmer, Kristopher R / Blalock, J Edwin

Annual review of physiology

2021 Volume 84, Page(s) 631–654

Abstract: Chronic obstructive pulmonary disease (COPD) is a complex, heterogeneous, smoking-related disease of significant global impact. The complex biology of COPD is ultimately driven by a few interrelated processes, including proteolytic tissue remodeling, ... ...

Abstract	Chronic obstructive pulmonary disease (COPD) is a complex, heterogeneous, smoking-related disease of significant global impact. The complex biology of COPD is ultimately driven by a few interrelated processes, including proteolytic tissue remodeling, innate immune inflammation, derangements of the host-pathogen response, aberrant cellular phenotype switching, and cellular senescence, among others. Each of these processes are engendered and perpetuated by cells modulating their environment or each other. Extracellular vesicles (EVs) are powerful effectors that allow cells to perform a diverse array of functions on both adjacent and distant tissues, and their pleiotropic nature is only beginning to be appreciated. As such, EVs are candidates to play major roles in these fundamental mechanisms of disease behind COPD. Furthermore, some such roles for EVs are already established, and EVs are implicated in significant aspects of COPD pathogenesis. Here, we discuss known and potential ways that EVs modulate the environment of their originating cells to contribute to the processes that underlie COPD.
MeSH term(s)	Cellular Senescence ; Exosomes ; Extracellular Vesicles ; Humans ; Inflammation ; Pulmonary Disease, Chronic Obstructive
Language	English
Publishing date	2021-11-01
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	207933-1
ISSN	1545-1585 ; 0066-4278
ISSN (online)	1545-1585
ISSN	0066-4278
DOI	10.1146/annurev-physiol-061121-035838
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Article ; Online: Therapeutic effect of two strategies directed at disruption of pathogenic neutrophil extracellular vesicles in a murine emphysema model.

Genschmer, Kristopher R / Madison, Matthew / Viera, Liliana / Margaroli, Camilla / Gaggar, Amit / Blalock, J Edwin / Russell, Derek W

American journal of physiology. Lung cellular and molecular physiology

2023 Volume 324, Issue 5, Page(s) L694–L699

Abstract: Chronic obstructive pulmonary disease (COPD) is characterized by lung extracellular matrix (ECM) remodeling that contributes to obstruction. This is driven, in part by extracellular vesicles (EVs) from activated neutrophils (PMNs), which express on their ...

Abstract	Chronic obstructive pulmonary disease (COPD) is characterized by lung extracellular matrix (ECM) remodeling that contributes to obstruction. This is driven, in part by extracellular vesicles (EVs) from activated neutrophils (PMNs), which express on their surface an α-1 antitrypsin (AAT) insensitive form of neutrophil elastase (NE). These EVs are predicted to bind to collagen fibers via Mac-1 integrins, during which time NE can enzymatically degrade the collagen. Protamine sulfate (PS), a cationic compound used safely for decades in humans, has been shown, in vitro, to dissociate this NE from the EV surface, rendering it AAT-sensitive. In addition, a nonapeptide inhibitor, MP-9, has been shown to prevent EV association with collagen. We sought to test whether PS, MP-9, or a combination of the two could effectively prevent NE+ EV-driven ECM remodeling in an animal COPD model. EVs were preincubated with PBS, protamine sulfate (25 μM), MP-9 (50 μM), or a combination of PS and MP-9. These were delivered intratracheally to anesthetized female 10- to 12-wk-old A/J mice for a 7-day time period. One group of mice was euthanized and lungs sectioned for morphometry, and the other group was used for live pulmonary function testing. The effect of alveolar destruction by activated neutrophil EVs was abrogated by pretreatment with PS or MP-9. However, in pulmonary function tests, only the PS groups (and combined PS/MP-9 groups) returned pulmonary function to near-control levels. These data presented here offer an insight into the effective use of PS in therapeutic setting for EV-derived alveolar damage.
MeSH term(s)	Humans ; Female ; Mice ; Animals ; Leukocyte Elastase/metabolism ; Neutrophils/metabolism ; Pulmonary Emphysema/metabolism ; Pulmonary Disease, Chronic Obstructive/metabolism ; Collagen/metabolism ; Emphysema ; Extracellular Vesicles/metabolism
Chemical Substances	Leukocyte Elastase (EC 3.4.21.37) ; Collagen (9007-34-5)
Language	English
Publishing date	2023-04-04
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1013184-x
ISSN	1522-1504 ; 1040-0605
ISSN (online)	1522-1504
ISSN	1040-0605
DOI	10.1152/ajplung.00057.2023
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Article ; Online: Comment on: Pathological consequences of Anti-Citrullinated Protein Antibodies in Tear Fluid and therapeutic potential of Pooled Human Immune Globulin-Eye Drops in Dry Eye Disease: Too much of a good thing, how chronic neutrophilic inflammation can drive human disease.

Genschmer, Kristopher R / Russel, Derek W / Blalock, J Edwin

The ocular surface

2019 Volume 18, Issue 2, Page(s) 193–195

MeSH term(s)	Anti-Citrullinated Protein Antibodies ; Dry Eye Syndromes ; Humans ; Inflammation ; Ophthalmic Solutions ; Tears
Chemical Substances	Anti-Citrullinated Protein Antibodies ; Ophthalmic Solutions
Language	English
Publishing date	2019-12-19
Publishing country	United States
Document type	Editorial ; Comment
ZDB-ID	2208578-6
ISSN	1937-5913 ; 1542-0124
ISSN (online)	1937-5913
ISSN	1542-0124
DOI	10.1016/j.jtos.2019.12.003
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Article ; Online: An in vivo model for extracellular vesicle-induced emphysema.

Margaroli, Camilla / Madison, Matthew C / Viera, Liliana / Russell, Derek W / Gaggar, Amit / Genschmer, Kristopher R / Blalock, J Edwin

JCI insight

2022 Volume 7, Issue 4

Abstract: Chronic obstructive pulmonary disease (COPD) is a debilitating chronic disease and the third-leading cause of mortality worldwide. It is characterized by airway neutrophilia, promoting tissue injury through release of toxic mediators and proteases. ... ...

Abstract	Chronic obstructive pulmonary disease (COPD) is a debilitating chronic disease and the third-leading cause of mortality worldwide. It is characterized by airway neutrophilia, promoting tissue injury through release of toxic mediators and proteases. Recently, it has been shown that neutrophil-derived extracellular vesicles (EVs) from lungs of patients with COPD can cause a neutrophil elastase-dependent (NE-dependent) COPD-like disease upon transfer to mouse airways. However, in vivo preclinical models elucidating the impact of EVs on disease are lacking, delaying opportunities for therapeutic testing. Here, we developed an in vivo preclinical mouse model of lung EV-induced COPD. EVs from in vivo LPS-activated mouse neutrophils induced COPD-like disease in naive recipients through an α-1 antitrypsin-resistant, NE-dependent mechanism. Together, these results show a key pathogenic and mechanistic role for neutrophil-derived EVs in a mouse model of COPD. Broadly, the in vivo model described herein could be leveraged to develop targeted therapies for severe lung disease.
MeSH term(s)	Animals ; Disease Models, Animal ; Extracellular Vesicles/pathology ; Mice ; Pulmonary Disease, Chronic Obstructive/diagnosis ; Pulmonary Disease, Chronic Obstructive/etiology ; Pulmonary Disease, Chronic Obstructive/metabolism ; Pulmonary Emphysema/complications ; Pulmonary Emphysema/metabolism
Language	English
Publishing date	2022-01-25
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ISSN	2379-3708
ISSN (online)	2379-3708
DOI	10.1172/jci.insight.153560
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Article ; Online: Protease-armed, Pathogenic Extracellular Vesicles Link Smoking and Chronic Obstructive Pulmonary Disease.

Madison, Matthew C / Margaroli, Camilla / Genschmer, Kristopher R / Russell, Derek W / Wells, James M / Sari, Ezgi / Soto-Vazquez, Yixel M / Guo, Yuan-Yuan / Mincham, Kyle T / Snelgrove, Robert J / Gaggar, Amit / Blalock, James E

American journal of respiratory and critical care medicine

2023 Volume 208, Issue 10, Page(s) 1115–1125

Abstract: Rationale: ...

Abstract	Rationale:
MeSH term(s)	Humans ; Animals ; Mice ; Peptide Hydrolases/metabolism ; Matrix Metalloproteinase 12/metabolism ; Pulmonary Disease, Chronic Obstructive/pathology ; Lung ; Pulmonary Emphysema/etiology ; Emphysema ; Pancreatic Elastase/metabolism ; Smoking/adverse effects ; Disease Models, Animal
Chemical Substances	Peptide Hydrolases (EC 3.4.-) ; Matrix Metalloproteinase 12 (EC 3.4.24.65) ; Pancreatic Elastase (EC 3.4.21.36)
Language	English
Publishing date	2023-09-15
Publishing country	United States
Document type	Journal Article
ZDB-ID	1180953-x
ISSN	1535-4970 ; 0003-0805 ; 1073-449X
ISSN (online)	1535-4970
ISSN	0003-0805 ; 1073-449X
DOI	10.1164/rccm.202303-0471OC
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Article ; Online: Different-sized extracellular vesicles derived from stored red blood cells package diverse cargoes and cause distinct cellular effects.

Oh, Joo-Yeun / Marques, Marisa B / Xu, Xin / Li, Jindong / Genschmer, Kristopher R / Phillips, Edward / Chimento, Melissa F / Mobley, James / Gaggar, Amit / Patel, Rakesh P

Transfusion

2023 Volume 63, Issue 3, Page(s) 586–600

Abstract: Background: The formation of extracellular vesicles (EVs) occurs during cold storage of RBCs. Transfusion of EVs may contribute to adverse responses in recipients receiving RBCs. However, EVs are poorly characterized with limited data on whether ... ...

Abstract	Background: The formation of extracellular vesicles (EVs) occurs during cold storage of RBCs. Transfusion of EVs may contribute to adverse responses in recipients receiving RBCs. However, EVs are poorly characterized with limited data on whether distinct vesicles are formed, their composition, and potential biological effects. Study design and methods: Stored RBC-derived EVs were purified using protocols that separate larger microvesicle-like EVs (LEVs) from smaller exosome-like vesicles (SEVs). Vesicles were analyzed by electron microscopy, content of hemoglobin, heme, and proteins (by mass spectrometry), and the potential to mediate lipid peroxidation and endothelial cell permeability in vitro. Results: SEVs were characterized by having an electron-dense double membrane whereas LEVs had more uniform electron density across the particles. No differences in hemoglobin nor heme levels per particle were observed, however, due to smaller volumes, SEVs had higher concentrations of oxyHb and heme. Both particles contained antioxidant proteins peroxiredoxin-2 and copper/zinc superoxide dismutase, these were present in higher molecular weight fractions in SEVs suggesting either oxidized proteins are preferentially packaged into smaller vesicles and/or that the environment associated with SEVs is more pro-oxidative. Furthermore, total glutathione (GSH + GSSG) levels were lower in SEVs. Both EVs mediated oxidation of liposomes that were prevented by hemopexin, identifying heme as the pro-oxidant effector. Addition of SEVs, but not LEVs, induced endothelial permeability in a process also prevented by hemopexin. Conclusion: These data show that distinct EVs are formed during cold storage of RBCs with smaller particles being more likely to mediate pro-oxidant and inflammatory effects associated with heme.
MeSH term(s)	Humans ; Hemopexin/analysis ; Hemopexin/metabolism ; Reactive Oxygen Species/metabolism ; Extracellular Vesicles/metabolism ; Erythrocytes/metabolism ; Hemoglobins/analysis ; Heme/metabolism
Chemical Substances	Hemopexin (9013-71-2) ; Reactive Oxygen Species ; Hemoglobins ; Heme (42VZT0U6YR)
Language	English
Publishing date	2023-02-08
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	208417-x
ISSN	1537-2995 ; 0041-1132
ISSN (online)	1537-2995
ISSN	0041-1132
DOI	10.1111/trf.17271
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Article ; Online: The Modified Surface Killing Assay Distinguishes between Protective and Nonprotective Antibodies to PspA.

Genschmer, Kristopher R / Vadesilho, Cintia F M / McDaniel, Larry S / Park, Sang-Sang / Hale, Yvette / Miyaji, Eliane N / Briles, David E

mSphere

2019 Volume 4, Issue 6

Abstract: Pneumococcal surface protein A (PspA) elicits antibody protective against lethal challenge ... ...

Abstract	Pneumococcal surface protein A (PspA) elicits antibody protective against lethal challenge by
MeSH term(s)	Animals ; Antibodies, Bacterial/immunology ; Antibodies, Monoclonal/immunology ; Bacterial Proteins/immunology ; Binding Sites ; Blood Bactericidal Activity ; Disease Models, Animal ; Immunization, Passive ; Immunoassay/methods ; Mice ; Neutrophils/immunology ; Pneumococcal Infections/prevention & control ; Protein Binding ; Streptococcus pneumoniae/immunology ; Treatment Outcome
Chemical Substances	Antibodies, Bacterial ; Antibodies, Monoclonal ; Bacterial Proteins ; pneumococcal surface protein A
Language	English
Publishing date	2019-12-11
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	2379-5042
ISSN (online)	2379-5042
DOI	10.1128/mSphere.00589-19
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Article ; Online: The diversity of the proline-rich domain of pneumococcal surface protein A (PspA): Potential relevance to a broad-spectrum vaccine.

Mukerji, Reshmi / Hendrickson, Curtis / Genschmer, Kristopher R / Park, Sang-Sang / Bouchet, Valérie / Goldstein, Richard / Lefkowitz, Elliot J / Briles, David E

Vaccine

2018 Volume 36, Issue 45, Page(s) 6834–6843

Abstract: Pneumococcal surface protein A (PspA) is a surface exposed, highly immunogenic protein of Streptococcus pneumoniae. Its N-terminal α-helical domain (αHD) elicits protective antibody in humans and animals that can protect mice from fatal infections with ... ...

Abstract	Pneumococcal surface protein A (PspA) is a surface exposed, highly immunogenic protein of Streptococcus pneumoniae. Its N-terminal α-helical domain (αHD) elicits protective antibody in humans and animals that can protect mice from fatal infections with pneumococci and can be detected in vitro with opsonophagocytosis assays. The proline-rich domain (PRD) in the center of the PspA sequence can also elicit protection. This study revealed that although the sequence of PRD was diverse, PRD from different pneumococcal isolates contained many shared elements. The inferred amino acid sequences of 123 such PRDs, which were analyzed by assembly and alignment-free (AAF) approaches, formed three PRD groups. Of these sequences, 45 were classified as Group 1, 19 were classified as Group 2, and 59 were classified as Group 3. All Group 3 sequences contained a highly conserved 22-amino acid non-proline block (NPB). A significant polymorphism was observed, however, at a single amino acid position within NPB. Each of the three PRD groups had characteristic patterns of short amino acid repeats, with most of the repeats being found in more than one PRD group. One of these repeats, PKPEQP as well as the NPB were previously shown to elicit protective antibodies in mice. In this study, we found that sera from 12 healthy human adult volunteers contained antibodies to all three PRD groups. This suggested that a PspA-containing vaccine containing carefully selected PRDs and αHDs could redundantly cover the known diversity of PspA. Such an approach might reduce the chances of PspA variants escaping a PspA vaccine's immunity.
MeSH term(s)	Adult ; Antibodies, Bacterial/immunology ; Bacterial Proteins/immunology ; Humans ; Phylogeny ; Pneumococcal Vaccines/immunology ; Protein Domains
Chemical Substances	Antibodies, Bacterial ; Bacterial Proteins ; Pneumococcal Vaccines ; pneumococcal surface protein A
Language	English
Publishing date	2018-10-05
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	605674-x
ISSN	1873-2518 ; 0264-410X
ISSN (online)	1873-2518
ISSN	0264-410X
DOI	10.1016/j.vaccine.2018.08.045
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