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Article: Influence of Sterilization Technologies on Electrospun Poly(ester urea)s for Soft Tissue Repair

Wade, Mary Beth / Rodenberg Eric / Patel Umesh / Shah Bhavin / Becker Matthew L

Biomacromolecules. 2016 Oct. 10, v. 17, no. 10

2016

Abstract: Degradable poly(ester urea)s (PEU)s were electrospun into nanofiber sheets and assessed for their potential to be used in soft tissue repair. The level of residual solvent was measured and the effects of ethylene oxide and electron beam sterilization ... ...

Abstract	Degradable poly(ester urea)s (PEU)s were electrospun into nanofiber sheets and assessed for their potential to be used in soft tissue repair. The level of residual solvent was measured and the effects of ethylene oxide and electron beam sterilization techniques on molecular mass, mass distribution, and morphology were quantified. Two PEU compositions that formed stable nanofiber sheets were advanced into a pilot study in vitro and in vivo as candidate materials for hernia repair. Cell viability, spreading, proliferation, and migration were examined in vitro. Nanofiber sheets were implanted subcutaneously into mice and analyzed via microangiography and histology for tissue incorporation. Nanofiber sheets performed similarly to decellularized extracellular matrix (ECM) in vitro, but the lack of sufficient pore structure inhibited cellular infiltration after 14 days of culture. The lack of microporous features in nanofiber sheets also contributed to low levels of cellular infiltration, angiogenesis, and matrix deposition in vivo. A preliminary study to increase pore size in nanofibers was performed using coaxial electrospinning resulting in significant improvement in tissue infiltration in vivo.
Keywords	angiogenesis ; cell viability ; ethylene oxide ; extracellular matrix ; hernia ; histology ; mice ; molecular weight ; nanofibers ; porosity ; porous media ; solvents ; tissue repair ; tissues
Language	English
Dates of publication	2016-1010
Size	p. 3363-3374.
Publishing place	American Chemical Society
Document type	Article
ISSN	1526-4602
DOI	10.1021%2Facs.biomac.6b01158
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Catheter-based retrograde coronary sinus infusion is a practical delivery technique for introducing biological molecules into the cardiac system.

Rodenberg, Eric J / Patel, Dimki S / Shirley, Brad / Young, Brandt W / Taylor, Amanda F / Steidinger, Hayley R / Fisher, Scott J / Patel, Amit N

Catheterization and cardiovascular interventions : official journal of the Society for Cardiac Angiography & Interventions

2019 Volume 94, Issue 5, Page(s) 669–676

Abstract: Objectives: To demonstrate coronary sinus (CS) retrograde catheterization as a practicable technique for delivering biologics into the heart.: Background: There are many options to deliver biologics into the heart. However, there is no single optimal ...

Abstract	Objectives: To demonstrate coronary sinus (CS) retrograde catheterization as a practicable technique for delivering biologics into the heart. Background: There are many options to deliver biologics into the heart. However, there is no single optimal technique when considering safety, biologic retention, and reproducibility. Retrograde delivery has the potential to address many of these concerns. This study evaluated retrograde CS infusion of luciferase-expressing plasmid in a porcine model using the Advance® CS Coronary Sinus Infusion Catheter and bioluminescence imaging to track the expression of the infused biological markers. Methods: Plasmid was delivered retrograde into the CS in one of three infusion volumes. Twenty-four hours post-infusion, hearts were excised and underwent bioluminescence imaging to characterize the expression of the infusates. Heart and lung biopsies were also assessed for luciferase expression using RT-qPCR. Results: Retrograde infusion was safe and successful in all nine test subjects. Luciferase detection was inconsistent in the low volume group. Bioluminescence was confined predominantly along the posterolateral left ventricle for medium volume infusions and was more broadly dispersed along the anterior side of the heart for high volume infusions. Tissue mRNA analysis corroborated the bioluminescence results, with the highest concentration of luciferase expression localized in the left ventricle. Conclusions: Retrograde CS infusion is a promising technique for delivering biological molecules to the heart. Specifically, this study demonstrated that the low pressure coronary venous system accommodates a wide range of infusion volumes and that biological infusates can be maintained in situ following the resumption of coronary venous flow.
MeSH term(s)	Animals ; Cardiac Catheterization ; Coronary Sinus ; Gene Transfer Techniques ; Infusions, Intravenous ; Luciferases/administration & dosage ; Luciferases/biosynthesis ; Luciferases/genetics ; Luminescent Measurements ; Models, Animal ; Myocardium/metabolism ; Plasmids/administration & dosage ; Plasmids/biosynthesis ; Plasmids/genetics ; RNA, Messenger/biosynthesis ; Sus scrofa ; Time Factors
Chemical Substances	RNA, Messenger ; Luciferases (EC 1.13.12.-)
Language	English
Publishing date	2019-03-13
Publishing country	United States
Document type	Journal Article
ZDB-ID	1459995-8
ISSN	1522-726X ; 1522-1946
ISSN (online)	1522-726X
ISSN	1522-1946
DOI	10.1002/ccd.28159
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Article ; Online: Influence of Sterilization Technologies on Electrospun Poly(ester urea)s for Soft Tissue Repair.

Wade, Mary Beth / Rodenberg, Eric / Patel, Umesh / Shah, Bhavin / Becker, Matthew L

Biomacromolecules

2016 Volume 17, Issue 10, Page(s) 3363–3374

Abstract	Degradable poly(ester urea)s (PEU)s were electrospun into nanofiber sheets and assessed for their potential to be used in soft tissue repair. The level of residual solvent was measured and the effects of ethylene oxide and electron beam sterilization techniques on molecular mass, mass distribution, and morphology were quantified. Two PEU compositions that formed stable nanofiber sheets were advanced into a pilot study in vitro and in vivo as candidate materials for hernia repair. Cell viability, spreading, proliferation, and migration were examined in vitro. Nanofiber sheets were implanted subcutaneously into mice and analyzed via microangiography and histology for tissue incorporation. Nanofiber sheets performed similarly to decellularized extracellular matrix (ECM) in vitro, but the lack of sufficient pore structure inhibited cellular infiltration after 14 days of culture. The lack of microporous features in nanofiber sheets also contributed to low levels of cellular infiltration, angiogenesis, and matrix deposition in vivo. A preliminary study to increase pore size in nanofibers was performed using coaxial electrospinning resulting in significant improvement in tissue infiltration in vivo.
MeSH term(s)	Ethylene Oxide/chemistry ; Extracellular Matrix/drug effects ; Hernia/therapy ; Herniorrhaphy/methods ; Humans ; Nanofibers/chemistry ; Nanofibers/therapeutic use ; Polyesters/chemistry ; Polyesters/therapeutic use ; Sterilization ; Tissue Engineering ; Tissue Scaffolds/chemistry ; Urea/chemistry ; Urea/therapeutic use
Chemical Substances	Polyesters ; Urea (8W8T17847W) ; Ethylene Oxide (JJH7GNN18P)
Language	English
Publishing date	2016-10-10
Publishing country	United States
Document type	Journal Article
ISSN	1526-4602
ISSN (online)	1526-4602
DOI	10.1021/acs.biomac.6b01158
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Peptides derived from fibronectin type III connecting segments promote endothelial cell adhesion but not platelet adhesion: implications in tissue-engineered vascular grafts.

Rodenberg, Eric J / Pavalko, Fredrick M

Tissue engineering

2007 Volume 13, Issue 11, Page(s) 2653–2666

Abstract: The development of a completely tissue-engineered small-caliber prosthesis suitable for incorporation into an in vivo vascular network is fraught with many challenges, including overcoming resistance to endothelialization and susceptibility to ... ...

Abstract	The development of a completely tissue-engineered small-caliber prosthesis suitable for incorporation into an in vivo vascular network is fraught with many challenges, including overcoming resistance to endothelialization and susceptibility to thrombogenesis. In this work, recombinant human fibronectin-derived low-molecular-weight peptide fragments were studied for their ability to promote cell type-specific alpha(4) integrin-mediated adhesion. Two populations of primary human endothelial cells were examined and found to express alpha(4) integrin receptors on their surfaces; on the contrary, human platelets were not found to be expressers of alpha(4) integrins. A peptide fragment isolated from the variably spliced human fibronectin type III connecting segment-1 (CS-1) domain was determined to mediate statistically significant endothelial cell alpha(4) integrin-mediated adhesion. In contrast, the fibronectin type III CS-1 fragment did not support human platelet adhesion under physiological fluid shear conditions, although fully intact human fibronectin molecules supported shear-induced platelet adhesion. This suggests that platelets bind to fibronectin in regions not encompassing the CS-1 domain. In conclusion, this work has demonstrated that the low-molecular-weight peptide CS-1 could serve as a cell-selective adhesion mediator in the engineering of a more-compatible small-caliber vascular graft lumen interface.
MeSH term(s)	Amino Acid Sequence ; Cell Adhesion/drug effects ; Cell Culture Techniques/methods ; Cell Movement/drug effects ; Cells, Cultured ; Coronary Vessels/cytology ; Culture Media ; Endothelial Cells/cytology ; Endothelial Cells/drug effects ; Endothelial Cells/physiology ; Endothelium, Vascular/cytology ; Fibronectins/chemistry ; Humans ; Integrin alpha4/metabolism ; Models, Biological ; Molecular Sequence Data ; Peptide Fragments/chemistry ; Peptide Fragments/genetics ; Peptide Fragments/pharmacology ; Platelet Adhesiveness/physiology ; Recombinant Proteins/chemistry ; Recombinant Proteins/pharmacology ; Stress, Mechanical ; Tissue Engineering/methods ; Umbilical Veins/cytology
Chemical Substances	Culture Media ; Fibronectins ; Peptide Fragments ; Recombinant Proteins ; Integrin alpha4 (143198-26-9)
Language	English
Publishing date	2007-11
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1310000-2
ISSN	1557-8690 ; 1076-3279
ISSN (online)	1557-8690
ISSN	1076-3279
DOI	10.1089/ten.2007.0037
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Zs.A 5500: Show issues

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Article ; Online: Non-overlapping functions for Pyk2 and FAK in osteoblasts during fluid shear stress-induced mechanotransduction.

Young, Suzanne R L / Hum, Julia M / Rodenberg, Eric / Turner, Charles H / Pavalko, Fredrick M

PloS one

2011 Volume 6, Issue 1, Page(s) e16026

Abstract: Mechanotransduction, the process by which cells convert external mechanical stimuli such as fluid shear stress (FSS) into biochemical changes, plays a critical role in maintenance of the skeleton. We have proposed that mechanical stimulation by FSS ... ...

Abstract	Mechanotransduction, the process by which cells convert external mechanical stimuli such as fluid shear stress (FSS) into biochemical changes, plays a critical role in maintenance of the skeleton. We have proposed that mechanical stimulation by FSS across the surfaces of bone cells results in formation of unique signaling complexes called mechanosomes that are launched from sites of adhesion with the extracellular matrix and with other bone cells [1]. Deformation of adhesion complexes at the cell membrane ultimately results in alteration of target gene expression. Recently, we reported that focal adhesion kinase (FAK) functions as a part of a mechanosome complex that is required for FSS-induced mechanotransduction in bone cells. This study extends this work to examine the role of a second member of the FAK family of non-receptor protein tyrosine kinases, proline-rich tyrosine kinase 2 (Pyk2), and determine its role during osteoblast mechanotransduction. We use osteoblasts harvested from mice as our model system in this study and compared the contributions of Pyk2 and FAK during FSS induced mechanotransduction in osteoblasts. We exposed Pyk2(+/+) and Pyk2(-/-) primary calvarial osteoblasts to short period of oscillatory fluid flow and analyzed downstream activation of ERK1/2, and expression of c-fos, cyclooxygenase-2 and osteopontin. Unlike FAK, Pyk2 was not required for fluid flow-induced mechanotransduction as there was no significant difference in the response of Pyk2(+/+) and Pyk2(-/-) osteoblasts to short periods of fluid flow (FF). In contrast, and as predicted, FAK(-/-) osteoblasts were unable to respond to FF. These data indicate that FAK and Pyk2 have distinct, non-redundant functions in launching mechanical signals during osteoblast mechanotransduction. Additionally, we compared two methods of generating FF in both cell types, oscillatory pump method and another orbital platform method. We determined that both methods of generating FF induced similar responses in both primary calvarial osteoblasts and immortalized calvarial osteoblasts.
MeSH term(s)	Animals ; Cells, Cultured ; Focal Adhesion Kinase 1/metabolism ; Focal Adhesion Kinase 2/metabolism ; Mechanotransduction, Cellular ; Mice ; Osteoblasts/metabolism ; Rheology ; Skull ; Stress, Mechanical
Chemical Substances	Focal Adhesion Kinase 1 (EC 2.7.10.2) ; Focal Adhesion Kinase 2 (EC 2.7.10.2) ; Ptk2 protein, mouse (EC 2.7.10.2) ; Ptk2b protein, mouse (EC 2.7.10.2)
Language	English
Publishing date	2011-01-25
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0016026
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Sensory nerve induced inflammation contributes to heterotopic ossification.

Salisbury, Elizabeth / Rodenberg, Eric / Sonnet, Corinne / Hipp, John / Gannon, Francis H / Vadakkan, Tegy J / Dickinson, Mary E / Olmsted-Davis, Elizabeth A / Davis, Alan R

Journal of cellular biochemistry

2011 Volume 112, Issue 10, Page(s) 2748–2758

Abstract: Heterotopic ossification (HO), or bone formation in soft tissues, is often the result of traumatic injury. Much evidence has linked the release of BMPs (bone morphogenetic proteins) upon injury to this process. HO was once thought to be a rare occurrence, ...

Abstract	Heterotopic ossification (HO), or bone formation in soft tissues, is often the result of traumatic injury. Much evidence has linked the release of BMPs (bone morphogenetic proteins) upon injury to this process. HO was once thought to be a rare occurrence, but recent statistics from the military suggest that as many as 60% of traumatic injuries, resulting from bomb blasts, have associated HO. In this study, we attempt to define the role of peripheral nerves in this process. Since BMP2 has been shown previously to induce release of the neuroinflammatory molecules, substance P (SP) and calcitonin gene related peptide (CGRP), from peripheral, sensory neurons, we examined this process in vivo. SP and CGRP are rapidly expressed upon delivery of BMP2 and remain elevated throughout bone formation. In animals lacking functional sensory neurons (TRPV1(-/-) ), BMP2-mediated increases in SP and CGRP were suppressed as compared to the normal animals, and HO was dramatically inhibited in these deficient mice, suggesting that neuroinflammation plays a functional role. Mast cells, known to be recruited by SP and CGRP, were elevated after BMP2 induction. These mast cells were localized to the nerve structures and underwent degranulation. When degranulation was inhibited using cromolyn, HO was again reduced significantly. Immunohistochemical analysis revealed nerves expressing the stem cell markers nanog and Klf4, as well as the osteoblast marker osterix, after BMP2 induction, in mice treated with cromolyn. The data collectively suggest that BMP2 can act directly on sensory neurons to induce neurogenic inflammation, resulting in nerve remodeling and the migration/release of osteogenic and other stem cells from the nerve. Further, blocking this process significantly reduces HO, suggesting that the stem cell population contributes to bone formation.
MeSH term(s)	Animals ; Bone Morphogenetic Protein 2/genetics ; Bone Morphogenetic Protein 2/metabolism ; Calcitonin Gene-Related Peptide/metabolism ; Cell Line ; Cromolyn Sodium/pharmacology ; Immunohistochemistry ; Mice ; Mice, Inbred C57BL ; Neurogenic Inflammation/complications ; Neurogenic Inflammation/physiopathology ; Ossification, Heterotopic/etiology ; Ossification, Heterotopic/genetics ; Ossification, Heterotopic/metabolism ; Sensory Receptor Cells/immunology ; Sensory Receptor Cells/pathology ; Substance P/metabolism ; TRPV Cation Channels/genetics ; TRPV Cation Channels/metabolism ; X-Ray Microtomography
Chemical Substances	Bone Morphogenetic Protein 2 ; TRPV Cation Channels ; TRPV1 protein, mouse ; Substance P (33507-63-0) ; Calcitonin Gene-Related Peptide (JHB2QIZ69Z) ; Cromolyn Sodium (Q2WXR1I0PK)
Language	English
Publishing date	2011-06-15
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	392402-6
ISSN	1097-4644 ; 0730-2312
ISSN (online)	1097-4644
ISSN	0730-2312
DOI	10.1002/jcb.23225
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Zs.A 1114: Show issues

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Article ; Online: Matrix metalloproteinase-9 is a diagnostic marker of heterotopic ossification in a murine model.

Rodenberg, Eric / Azhdarinia, Ali / Lazard, ZaWaunyka W / Hall, Mary / Kwon, Sun Kuk / Wilganowski, Nathaniel / Salisbury, Elizabeth A / Merched-Sauvage, Maria / Olmsted-Davis, Elizabeth A / Sevick-Muraca, Eva M / Davis, Alan R

Tissue engineering. Part A

2011 Volume 17, Issue 19-20, Page(s) 2487–2496

Abstract: Heterotopic ossification (HO) is a serious disorder that occurs when there is aberrant bone morphogenic protein (BMP) signaling in soft tissues. Currently, there are no methods to detect HO before mineralization occurs. Yet once mineralization occurs, ... ...

Abstract	Heterotopic ossification (HO) is a serious disorder that occurs when there is aberrant bone morphogenic protein (BMP) signaling in soft tissues. Currently, there are no methods to detect HO before mineralization occurs. Yet once mineralization occurs, there are no effective treatments, short of surgery, to reverse HO. Herein, we used in vivo molecular imaging and confirmatory ex vivo tissue analyses of an established murine animal model of BMP-induced HO to show that matrix metalloproteinase-9 (MMP-9) can be detected as an early-stage biomarker before mineralization. Ex vivo analyses show that active MMP-9 protein is significantly elevated within tissues undergoing HO as early as 48 h after BMP induction, with its expression co-localizing to nerves and vessels. In vivo molecular imaging with a dual-labeled near-infrared fluorescence and micro-positron emission tomography (μPET) agent specific to MMP-2/-9 expression paralleled the ex vivo observations and reflected the site of HO formation as detected from microcomputed tomography 7 days later. The results suggest that the MMP-9 is a biomarker of the early extracellular matrix (ECM) re-organization and could be used as an in vivo diagnostic with confirmatory ex vivo tissue analysis for detecting HO or conversely for monitoring the success of tissue-engineered bone implants that employ ECM biology for engraftment.
MeSH term(s)	Amino Acid Sequence ; Animals ; Biomarkers/metabolism ; Disease Models, Animal ; Fluorescent Antibody Technique ; Gene Expression Regulation, Enzymologic/drug effects ; Hindlimb/drug effects ; Hindlimb/pathology ; Humans ; Matrix Metalloproteinase 2/metabolism ; Matrix Metalloproteinase 9/genetics ; Matrix Metalloproteinase 9/metabolism ; Mice ; Molecular Imaging ; Molecular Sequence Data ; Multimodal Imaging ; Ossification, Heterotopic/diagnosis ; Ossification, Heterotopic/enzymology ; Peptides, Cyclic/chemistry ; Peptides, Cyclic/pharmacology ; Positron-Emission Tomography ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; Spectroscopy, Near-Infrared ; Tomography, X-Ray Computed
Chemical Substances	Biomarkers ; Peptides, Cyclic ; RNA, Messenger ; Matrix Metalloproteinase 2 (EC 3.4.24.24) ; Matrix Metalloproteinase 9 (EC 3.4.24.35) ; Mmp9 protein, mouse (EC 3.4.24.35)
Language	English
Publishing date	2011-10
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2420582-5
ISSN	1937-335X ; 1937-3341
ISSN (online)	1937-335X
ISSN	1937-3341
DOI	10.1089/ten.TEA.2011.0007
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