| Biomechanical and microstructural properties of common carotid arteries from fibulin-5 null mice. | |
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MedLine Citation:
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PMID: 20614245 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Alteration in the mechanical properties of arteries occurs with aging and disease, and arterial stiffening is a key risk factor for subsequent cardiovascular events. Arterial stiffening is associated with the loss of functional elastic fibers and increased collagen content in the wall of large arteries. Arterial mechanical properties are controlled largely by the turnover and reorganization of key structural proteins and cells, a process termed growth and remodeling. Fibulin-5 (fbln5) is a microfibrillar protein that binds tropoelastin, interacts with integrins, and localizes to elastin fibers; tropoelastin and microfibrillar proteins constitute functional elastic fibers. We performed biaxial mechanical testing and confocal imaging of common carotid arteries (CCAs) from fibulin-5 null mice (fbln5 ⁻(/)⁻) and littermate controls (fbln5 (+/+)) to characterize the mechanical behavior and microstructural content of these arteries; mechanical testing data were fit to a four-fiber family constitutive model. We found that CCAs from fbln5 ⁻(/)⁻ mice exhibited lower in vivo axial stretch and lower in vivo stresses while maintaining a similar compliance over physiological pressures compared to littermate controls. Specifically, for fbln5 ⁻(/)⁻ the axial stretch λ = 1.41 ± 0.07, the circumferential stress σ(θ) = 101 ± 32 kPa, and the axial stress σ ( z ) = 74 ± 28 kPa; for fbln5 (+/+) λ = 1.64 ± 0.03, σ(θ) = 194 ± 38 kPa, and σ(z) = 159 ± 29 kPa. Structurally, CCAs from fbln5 ⁻(/)⁻ mice lack distinct functional elastic fibers defined by the lamellar structure of alternating layers of smooth muscle cells and elastin sheets. These data suggest that structural differences in fbln5 ⁻(/)⁻ arteries correlate with significant differences in mechanical properties. Despite these significant differences fbln5 ⁻(/)⁻ CCAs exhibited nearly normal levels of cyclic strain over the cardiac cycle. |
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Authors:
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William Wan; Hiromi Yanagisawa; Rudolph L Gleason |
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Publication Detail:
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Type: In Vitro; Journal Article; Research Support, N.I.H., Extramural Date: 2010-07-08 |
Journal Detail:
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Title: Annals of biomedical engineering Volume: 38 ISSN: 1573-9686 ISO Abbreviation: Ann Biomed Eng Publication Date: 2010 Dec |
Date Detail:
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Created Date: 2010-11-09 Completed Date: 2011-03-01 Revised Date: 2013-05-30 |
Medline Journal Info:
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Nlm Unique ID: 0361512 Medline TA: Ann Biomed Eng Country: United States |
Other Details:
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Languages: eng Pagination: 3605-17 Citation Subset: IM |
Affiliation:
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The George W. Woodruff School of Mechanical Engineering, Georgia Institute of Technology, Atlanta, 30332, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Animals Biomechanics Biomedical Engineering Carotid Artery, Common / physiology* Compliance Elastic Tissue / physiology Extracellular Matrix Proteins / deficiency*, genetics, physiology Male Mice Mice, 129 Strain Mice, Inbred C57BL Mice, Knockout Microscopy, Fluorescence, Multiphoton Models, Cardiovascular Recombinant Proteins / genetics Stress, Mechanical |
| Grant Support | |
ID/Acronym/Agency:
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R01 HD064824/HD/NICHD NIH HHS; R01 HL071157/HL/NHLBI NIH HHS; R01 HL106305/HL/NHLBI NIH HHS; R21 HL085822/HL/NHLBI NIH HHS; R21 HL085822-01A1/HL/NHLBI NIH HHS; R21 HL085822-02/HL/NHLBI NIH HHS; R21-HL085822/HL/NHLBI NIH HHS; T32-GM008433/GM/NIGMS NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Extracellular Matrix Proteins; 0/Fbln5 protein, mouse; 0/Recombinant Proteins |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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