Influence of fibrillin-1 genotype on the aortic stiffness in men

2005 ◽  
Vol 99 (3) ◽  
pp. 1036-1040 ◽  
Author(s):  
J. T. Powell ◽  
R. J. Turner ◽  
M. Sian ◽  
R. Debasso ◽  
T. Länne
Keyword(s):  
Mechanical Properties ◽  
Pulse Pressure ◽  
Aortic Stiffness ◽  
Collagen Type ◽  
Collagen Type I ◽  
Type I ◽  
Increased Risk ◽  
Fibrillin 1 ◽  
Echo Tracking

Aortic stiffness is a predictor of cardiovascular mortality. The mechanical properties of the arterial wall depend on the connective tissue framework, with variation in fibrillin-1 and collagen I genes being associated with aortic stiffness and/or pulse pressure elevation. The aim of this study was to investigate whether variation in fibrillin-1 genotype was associated with aortic stiffness in men. The mechanical properties of the abdominal aorta of 79 healthy men (range 28–81 yr) were investigated by ultrasonographic phase-locked echo tracking. Fibrillin-1 genotype, characterized by the variable tandem repeat in intron 28, and collagen type I alpha 1 genotype characterized by the 2,064 G>T polymorphism, were determined by using DNA from peripheral blood cells. Three common fibrillin-1 genotypes, 2-2, 2-3, and 2-4, were observed in 50 (64%), 10 (13%), and 11 (14%) of the men, respectively. Those of 2-3 genotype had higher pressure strain elastic modulus and aortic stiffness compared with men of 2-2 or 2-4 genotype ( P = 0.005). Pulse pressure also was increased in the 2-3 genotype ( P = 0.04). There was no significant association between type 1 collagen genotype and aortic stiffness in this cohort. In conclusion, the fibrillin-1 2-3 genotype in men was associated with increased aortic stiffness and pulse pressure, indicative of an increased risk for cardiovascular disease.

scholarly journals Influence of fibrillin-1 genotype on aortic stiffness in men: a note of caution

2006 ◽  
Vol 100 (4) ◽  
pp. 1431-1432
Author(s):  
Yasmin ◽  
Ian B. Wilkinson ◽  
Kevin M. O’Shaughnessy
Keyword(s):  
Mechanical Properties ◽  
Pulse Pressure ◽  
Aortic Stiffness ◽  
Collagen Type ◽  
Collagen Type I ◽  
Type I ◽  
Increased Risk ◽  
Fibrillin 1 ◽  
Echo Tracking

Aortic stiffness is a predictor of cardiovascular mortality. The mechanical properties of the arterial wall depend on the connective tissue framework, with variation in fibrillin-1 and collagen I genes being associated with aortic stiffness and/or pulse pressure elevation. The aim of this study was to investigate whether variation in fibrillin-1 genotype was associated with aortic stiffness in men. The mechanical properties of the abdominal aorta of 79 healthy men (range 28–81 yr) were investigated by ultrasonographic phase-locked echo tracking. Fibrillin-1 genotype, characterized by the variable tandem repeat in intron 28, and collagen type I alpha 1 genotype characterized by the 2,064 G\?\T polymorphism, were determined by using DNA from peripheral blood cells. Three common fibrillin-1 genotypes, 2-2, 2-3, and 2-4, were observed in 50 (64%), 10 (13%), and 11 (14%) of the men, respectively. Those of 2-3 genotype had higher pressure strain elastic modulus and aortic stiffness compared with men of 2-2 or 2-4 genotype ( P = 0.005). Pulse pressure also was increased in the 2-3 genotype ( P = 0.04). There was no significant association between type 1 collagen genotype and aortic stiffness in this cohort. In conclusion, the fibrillin-1 2-3 genotype in men was associated with increased aortic stiffness and pulse pressure, indicative of an increased risk for cardiovascular disease.

Glycation end-product cross-link breaker reduces collagen and improves cardiac function in aging diabetic heart

2003 ◽  
Vol 285 (6) ◽  
pp. H2587-H2591 ◽  
Author(s):  
Jing Liu ◽  
Malthi R. Masurekar ◽  
Dorothy E. Vatner ◽  
Garikiparthy N. Jyothirmayi ◽  
Timothy J. Regan ◽  
...  
Keyword(s):  
Ejection Fraction ◽  
Cardiac Function ◽  
Protein Content ◽  
Aortic Stiffness ◽  
Collagen Type ◽  
Collagen Type I ◽  
Type I ◽  
Cross Link ◽  
Aging Heart ◽  
Lv Ejection Fraction

Aging and diabetes mellitus (DM) both affect the structure and function of the myocardium, resulting in increased collagen in the heart and reduced cardiac function. As part of this process, hyperglycemia is a stimulus for the production of advanced glycation end products (AGEs), which covalently modify proteins and impair cell function. The goals of this study were first to examine the combined effects of aging and DM on hemodynamics and collagen types in the myocardium in 12 dogs, 9–12 yr old, and second to examine the effects of the AGE cross-link breaker phenyl-4,5-dimethylthazolium chloride (ALT-711) on myocardial collagen protein content, aortic stiffness, and left ventricular (LV) function in the aged diabetic heart. The alloxan model of DM was utilized to study the effects of DM on the aging heart. DM induced in the aging heart decreased LV systolic function (LV ejection fraction fell by 25%), increased aortic stiffness, and increased collagen type I and type III protein content. ALT-711 restored LV ejection fraction, reduced aortic stiffness and LV mass with no reduction in blood glucose level (199 ± 17 mg/dl), and reversed the upregulation of collagen type I and type III. Myocardial LV collagen solubility (%) increased significantly after treatment with ALT-711. These data suggest that an AGE cross-link breaker may have a therapeutic role in aged patients with DM.

scholarly journals Pro-fibrotic phenotype of bone marrow stromal cells in Modic type 1 changes

2021 ◽  
Vol 41 ◽  
pp. 648-667
Author(s):  
I Heggli ◽  
◽  
S Epprecht ◽  
A Juengel ◽  
R Schuepbach ◽  
...  
Keyword(s):  
Bone Marrow ◽  
Stromal Cells ◽  
Bone Marrow Stromal Cells ◽  
Collagen Type ◽  
Collagen Type I ◽  
Marrow Stromal Cells ◽  
Type I ◽  
Cell Contractility ◽  
Modic Type

Modic type 1 changes (MC1) are painful vertebral bone marrow lesions frequently found in patients suffering from chronic low-back pain. Marrow fibrosis is a hallmark of MC1. Bone marrow stromal cells (BMSCs) are key players in other fibrotic bone marrow pathologies, yet their role in MC1 is unknown. The present study aimed to characterise MC1 BMSCs and hypothesised a pro-fibrotic role of BMSCs in MC1. BMSCs were isolated from patients undergoing lumbar spinal fusion from MC1 and adjacent control vertebrae. Frequency of colony-forming unit fibroblast (CFU-F), expression of stem cell surface markers, differentiation capacity, transcriptome, matrix adhesion, cell contractility as well as expression of pro-collagen type I alpha 1, α-smooth muscle actin, integrins and focal adhesion kinase (FAK) were compared. More CFU-F and increased expression of C-X-C-motif-chemokine 12 were found in MC1 BMSCs, possibly indicating overrepresentation of a perisinusoidal BMSC population. RNA sequencing analysis showed enrichment in extracellular matrix proteins and fibrosis-related signalling genes. Increases in pro-collagen type I alpha 1 expression, cell adhesion, cell contractility and phosphorylation of FAK provided further evidence for their pro-fibrotic phenotype. Moreover, a leptin receptor high expressing (LEPRhigh) BMSC population was identified that differentiated under transforming growth factor beta 1 stimulation into myofibroblasts in MC1 but not in control BMSCs. In conclusion, pro-fibrotic changes in MC1 BMSCs and a LEPRhigh MC1 BMSC subpopulation susceptible to myofibroblast differentiation were found. Fibrosis is a hallmark of MC1 and a potential therapeutic target. A causal link between the pro-fibrotic phenotype and clinical characteristics needs to be demonstrated.

Membranes of Chitosan and Collagen-Type 1 for Biomineralization/Ostheogenesis

2013 ◽  
Vol 587 ◽  
pp. 222-226
Author(s):  
Ricardo B. Pacheco ◽  
Marina Salvarani Tonoli ◽  
Marisa Masumi Beppu
Keyword(s):  
Collagen Type ◽  
Collagen Type I ◽  
Calcium Deposition ◽  
Collagen Membrane ◽  
Type I ◽  
Chitosan Membranes ◽  
Collagen Membranes ◽  
Collagen Type 1

The main objective of this work was to produce membranes of chitosan and collagen type I and check their ability to undergo “in vitro” calcification. The membranes of chitosan-collagen blends were characterized by TGA, infra-red spectroscopy and DSC. Samples of dense and porous membranes were immersed in solution SBF (Simulated Body Fluid) in order to verify their “in vitro” calcification. The membranes were observed by SEM. The production of chitosan-collagen membranes is possible, in dense and porous versions. We can conclude that the blend is less resistant to high temperatures, in comparison to pristine chitosan membranes shown in literature. Through the initial assays of calcification, we observe that it is possible to induce the calcium deposition on a chitosan-collagen membrane, as seen by SEM. Microscopy of fracture surfaces showed fibril structures, probably formed by collagen.

Mechanical properties of single electrospun collagen type I fibers

Biomaterials ◽  
2008 ◽  
Vol 29 (8) ◽  
pp. 955-962 ◽  
Author(s):  
Lanti Yang ◽  
Carel F.C. Fitié ◽  
Kees O. van der Werf ◽  
Martin L. Bennink ◽  
Pieter J. Dijkstra ◽  
...  
Keyword(s):  
Mechanical Properties ◽  
Collagen Type ◽  
Collagen Type I ◽  
Type I ◽  
Type I Fibers

scholarly journals The role of collagen in extralobar pulmonary artery stiffening in response to hypoxia-induced pulmonary hypertension

2010 ◽  
Vol 299 (6) ◽  
pp. H1823-H1831 ◽  
Author(s):  
Chen Yen Ooi ◽  
Zhijie Wang ◽  
Diana M. Tabima ◽  
Jens C. Eickhoff ◽  
Naomi C. Chesler
Keyword(s):  
Mechanical Properties ◽  
Pulmonary Hypertension ◽  
Elastic Modulus ◽  
Pulmonary Artery ◽  
Chronic Hypoxia ◽  
Collagen Type ◽  
High Strain ◽  
Collagen Type I ◽  
Mouse Strains ◽  
Type I

Hypoxic pulmonary hypertension (HPH) causes extralobar pulmonary artery (PA) stiffening, which potentially impairs right ventricular systolic function. Changes in the extracellular matrix proteins collagen and elastin have been suggested to contribute to this arterial stiffening. We hypothesized that vascular collagen accumulation is a major cause of extralobar PA stiffening in HPH and tested our hypothesis with transgenic mice that synthesize collagen type I resistant to collagenase degradation (Col1a1R/R). These mice and littermate controls that have normal collagen degradation (Col1a1+/+) were exposed to hypoxia for 10 days; some were allowed to recover for 32 days. In vivo PA pressure and isolated PA mechanical properties and collagen and elastin content were measured for all groups. Vasoactive studies were also performed with U-46619, Y-27632, or calcium- and magnesium-free medium. Pulmonary hypertension occurred in both mouse strains due to chronic hypoxia and resolved with recovery. HPH caused significant PA mechanical changes in both mouse strains: circumferential stretch decreased, and mid-to-high-strain circumferential elastic modulus increased ( P < 0.05 for both). Impaired collagen type I degradation prevented a return to baseline mechanical properties with recovery and, in fact, led to an increase in the low and mid-to-high-strain moduli compared with hypoxia ( P < 0.05 for both). Significant changes in collagen content were found, which tended to follow changes in mid-to-high-strain elastic modulus. No significant changes in elastin content or vasoactivity were observed. Our results demonstrate that collagen content is important to extralobar PA stiffening caused by chronic hypoxia.

scholarly journals Nephroprotective Effect of Pentoxyphylline Through Improvement in the Expression of TGF-beta1, Collagen Type-1, and Renal Interstitial Fibrosis in Swiss Strain Mice After Being Induced by Doxorubicin

2010 ◽  
Vol 2 (2) ◽  
pp. 46
Author(s):  
Bambang Purwanto ◽  
A Guntur Hermawan
Keyword(s):  
Collagen Type ◽  
Interstitial Fibrosis ◽  
Collagen Type I ◽  
Type I ◽  
Renal Interstitial Fibrosis ◽  
Collagen Type 1 ◽  
Nephroprotective Effect ◽  
Tgf Β1 ◽  
Swiss Strain

BACKGROUND: Use of doxorubicin (DXR) in the treatment of cancer has been increasing along with the increase in cancer morbidity. Nephrotoxic effects of DXR are still a problem. Pentoxyphylline (PTX) as an electron-donor material can be nephroprotective, so the combination of DXR and PTX might reduce the nephrotoxic effects of DXR. The aim of this study was to prove the nephroprotective effect of PTX and DXR nephrotoxicity through the improvement of TGF-β1, collage type-1, and renal interstitial fibrosis.METHODS: Twenty-four males Swiss strain mice, divided into three groups namely Control (C) injected with NaCl 0.9%; DXR induced nephrotoxicity (D); and effect of PTX on D (P/D) by intraperitoneally, respectively, each group consisted of 8 mice. Injections were given once a week for three consecutive weeks. At 8th week post-treatment, all eight mice of each group were sacrificed. Examination of TGF-β1 and collagen type-I expression was done by immunohistochemistry with monoclonal antibody. Renal interstitial fibrosis examination was done by a histopathologist, using Verheoff van Giesen staining. The statistic analysis was carried out using one-way ANOVA.RESULTS: TGF-β1 expression increased from C to D and subsequently decreased in P/D (4.50±3.89 vs. 177.88±68.78 vs. 36.88±9.51). Collagen type-I expression increased from C to D and subsequently decreased in P/D (12.00±14.32 vs. 186.25±125.62 vs. 36.00±29.14). Renal interstitial fibrosis expression increased from C to D and subsequently decreased in P/D (16.75±6.14 vs. 85.00±7.33 vs. 60.50±11.40). The expression of TGF-β1, collagen type-1, and renal interstitial fibrosis were higher significantly in D group as compared to C group (p<0,001). The expression of TGF-β1, collagen type-1, and renal interstitial fibrosis were lower significantly in P/D group as compared to D group (p<0.005).CONCLUSIONS: PTX was proved to be nephroprotector inducing by DXR.KEYWORDS: PTX, nephroprotector, TGF-β1, collagen type-I, renal interstitial fibrosis

Tensile mechanical properties of collagen type I and its enzymatic crosslinks

2016 ◽  
Vol 214-215 ◽  
pp. 1-10 ◽  
Author(s):  
Albert L. Kwansa ◽  
Raffaella De Vita ◽  
Joseph W. Freeman
Keyword(s):  
Mechanical Properties ◽  
Collagen Type ◽  
Collagen Type I ◽  
Type I

A novel ADAMTS17 variant that causes Weill-Marchesani syndrome 4 alters fibrillin-1 and collagen type I deposition in the extracellular matrix

2020 ◽  
Vol 88 ◽  
pp. 1-18 ◽  
Author(s):  
Stylianos Z. Karoulias ◽  
Aude Beyens ◽  
Zerina Balic ◽  
Sofie Symoens ◽  
Anthony Vandersteen ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Collagen Type ◽  
Collagen Type I ◽  
Type I ◽  
Fibrillin 1
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