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抗Human Fibrillin 1 抗体:
抗Mouse (Murine) Fibrillin 1 抗体:
抗Rat (Rattus) Fibrillin 1 抗体:
Human Polyclonal Fibrillin 1 Primary Antibody for IHC, IHC (p) - ABIN4311653
Zhang, Ota, Shridhar, Chien, Wu, Kuang: Network-based survival analysis reveals subnetwork signatures for predicting outcomes of ovarian cancer treatment. in PLoS computational biology 2013
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Cow (Bovine) Polyclonal Fibrillin 1 Primary Antibody for ELISA - ABIN4272120
Morisaki, Akutsu, Ogino, Kondo, Yamanaka, Tsutsumi, Yoshimuta, Okajima, Matsuda, Minatoya, Sasaki, Tanaka, Ishibashi-Ueda, Morisaki: Mutation of ACTA2 gene as an important cause of familial and nonfamilial nonsyndromatic thoracic aortic aneurysm and/or dissection (TAAD). in Human mutation 2009
Study concludes that the c.8227-1G>A mutation is causative for Marfan syndrome-like disease.
Data suggest that genetic fibrillin-1 deficiency could alter normal endothelial signaling.
In cases of vascular calcification, the decreased expression of FBN1 may be partially responsible for decreased vascular elasticity and also for the decreased formation of new elastic fibers.
Results describe the intrinsic elastic properties of individual fibrillin microfibrils, which act as reinforcing fibres in fibrous composite tissues.
The coordinate upregulation of fibrillin-1 and fibrillin-2 expression with the onset of tropoelastin production is consistent with a role in elastic fiber assembly.
a calcium-binding epidermal growth factor-like domain of fibrillin-1 c.3598G > A, p.E1200K mutation is responsible for a bovine model of Marfan syndrome
This is the first study to investigate the expression and localization of fibrillin proteins and latent TGF-beta binding proteins affecting TGFbeta bioavailability in the ovary.
The majority of the identified P/LP variants were in the FBN1 gene ..we found 4.9% of patients carried a P/LP variant as the underlying cause of their Thoracic aortic aneurysm/aortic dissection (TAAD), predominantly within FBN1 but with substantial contributions from TGFBR and COL genes.
Reports a novel mutation in FBN1 in a Chinese family and to diagnose this family as Marfan syndrome, this also expands the genotype-phenotype correlation of this disease.
analysis of body height and growth charts for children with FBN1 gene mutation and fulfilling Ghent 1 criteria for Marfan syndrome
Our finding expands the mutation spectrum of large FBN1 deletions and emphasizes the importance of screening for large FBN1 deletions in clinical genetic testing, especially for those with classic Marfan phenotype.
Eye-derived fibrillin-1 exhibits different regional patterns of elastase susceptibility compared with skin-derived.
Three novel pathogenic variants were detected. Two of these variants [c.6610T>C; p.(Cys2204Arg) and c.1956T>G; p.(Cys652Trp)], which affect a cysteine residue, were associated with MS with ectopia lentis, whereas the mutation causing a premature stop codon [c.2506delA; p.(Ser836ValfsX10)] leads to a classical MS of a milder phenotype.
Two rare missense mutations in the fibrillin1 gene associated with atypical cardiovascular manifestations in a Chinese patient affected by Marfan syndrome.
This study has confirmed or corrected the clinical diagnosis, and enlarged the mutation spectrum of FBN1 and TGFBR2 and confirmed that parental mosaicism may be the cause of the varied phenotypic expression of these connective tissue disorders. The results should be helpful for prenatal diagnosis and genetic counseling.
Novel FBN1 mutation (p.Cys2672Arg) has been described in a family with inherited Marfan Syndrome.
A heterozygous mutation c.5284G > A (p.Gly1762Ser) in FBN1 gene was identified in all individuals affected with acromelic dysplasia in three families.
Results demonstrate that the deleterious mutations in FBN1 largely contribute to pathogenesis of sporadic non-syndromic AD, which expands our knowledge of FBN1 variants and the genetic basis and pathology of AD.
deletions in FBN1 results in variable phenotypes of Marfan syndrome
Although causation has not been proven by this report, it certainly raises interest in a mechanistic relationship between FBN1 and left ventricular non-compaction cardiomyopathy.
Most individuals meeting these criteria have a pathogenic variant in FBN1, usually unique or observed rarely. Individuals with EL alone may also have FBN1 pathogenic variants, and the risk for aortic disease is not well known. We identified a unique cohort of 31 individuals (mean age 29, range 2-78) from nine families ascertained by a proband with EL alone, who had the same FBN1 p.R650C variant
A missense mutation (c.G6953A:p.C2318Y) and a nonsense mutation (c.C4786T:p.R1596X) were identified in the fibrillin 1 gene.
Aortic stiffness is increased in Marfan syndrome, independently from fibrillin-1 genotype.
The overexpression of miR-133b and silence of FBN1 could inhibit the cell proliferative, migratory and invasive abilities of gastric cancer cells, while the influence of down-regulated miR-133b expression and up-regulated FBN1 expression were quite the contrary.
The N-terminal domain of FBN-1 mediates a bipartite interaction with LTBP1.
The de novo mutation c.2647T>C (p.Trp883Arg) in FBN1 was identified in a Chinese patient with Marfan syndrome.
In addition to performing a glucogenic function, asprosin is a centrally acting orexigenic hormone that is a potential therapeutic target in the treatment of both obesity and diabetes.
These results suggest that the establishment of the DNA methylation pattern within the FBN1 CpG island shore occurs after the blastocyst stage, likely during organogenesis. In conclusion, Hypo-allele ratios of the FBN1 CpG island shore correlated with FBN1 expression levels in porcine tissues.
The abundance of elastic fibers was reduced and fragmented in obesity, suggesting that the reduction in elastic fibers is initially caused by increased neprilysin and decreased fibrillin-1 expression, which may inhibit formation and stabilization of elastic fibers, resulting in skin fragility in obesity.
fibrillin-1 contributes little to lipid storage and metabolic homeostasis, which is in contrast to the obesity and metabolic changes associated with MAGP1 deficiency.
In young Fbn1(C1039G/+) mice, aortopathy develops in the absence of detectable alterations in smooth muscle cell (SMC) TGF-beta signaling. Loss of physiologic SMC TGF-beta signaling exacerbates MFS-associated aortopathy. Our data support a protective role for SMC TGF-beta signaling during early development of MFS-associated aortopathy.
Studies of Marfan syndrome and congenital contractural arachnodactyly mice have correlated the skeletal phenotypes of these mutant animals with distinct pathophysiological mechanisms that reflect the contextual contribution of fibrillin-1 and -2 scaffolds to TGFbeta and BMP signaling during bone patterning, growth and metabolism. [review]
Findings demonstrate that loss of fibrillin-1 in the mouse's marrow causes significant hematopoietic abnormalities, such as hematopoietic stem cell (HSC) depletion and augmented erythropoiesis (polycythemia). Furthermore, the distinct outcomes of systemic TGFbeta neutralization in mutant mice strongly suggest that fibrillin-1 differentially modulates TGFbeta signaling within HSC and erythroid niches.
This study shows that Raman microspectroscopy is able to reveal structural changes in fibrillin-1 microfibrils and elastic fiber networks and to discriminate between normal and diseased networks in vivo and in vitro.
Resveratrol inhibits aortic root dilatation in Fbn1C1039G/+ Marfan mice by promoting elastin integrity and smooth muscle cell survival, involving downregulation of the aneurysm-related micro-RNA-29b in the aorta.
These results suggest that both fibrillin-1 and fibrillin-2 expression is required to form thick oxytalan fibers in periodontal ligament.
findings show that fibrillin-1 regulates MSC activity by modulating TGFbeta bioavailability within the microenvironment of marrow niches.
Fibrillin-1 mgDelta(lpn) Marfan syndrome mutation associates with preserved proteostasis and bypass of a protein disulfide isomerase-dependent quality checkpoint
fibrillin-1 deficiency is associated with relevant dysfunction of the endothelial barrier that enables adenovirus to induce vessel-harming inflammation.
the Fbn1(C1039G/+) mouse model demonstrates mild intrinsic left ventricular dysfunction
This study demonstrated that dysfunctional fibrillin-1 impairs blood-brain barrier permeability /BCSFB integrity, facilitating peripheral leukocyte infiltration, which further degrades the BBB/BCSFB.
The review discuss FBN1 point mutations on the structure and function of the protein associated with Marfan syndrome in affected patients impairing protein folding and traficking, secretion, proteolysis or heparin binding.
The concomitant induction of both fibrillin-1 and alpha8 integrin in a self-limited model of glomerular injury points to a protective role of the interaction of fibrillin-1 with alpha8 integrin in the glomerulus.
Data show that fibrillin-1 (FBN1) modulates bone marrow mesenchymal stem cells (BMMSCs) lineage differentiation via IL4 receptor alpha/mTOR protein signaling.
latent transforming growth factor-beta-1 binding protein-2 was prominently associated with annular fibrils containing fibrillin-1
Activation of IL-6-STAT3 signaling contributes to aneurysmal dilation in fibrillin-1 deficient mice through increased MMP-9 activity, aggravating extracellular matrix degradation.
We targeted mutations in Pkd1 and Fbn1. Double heterozygotes displayed an exacerbation of the typical Fbn1 heterozygous aortic phenotype. The basis of this genetic interaction results from upregulation of TGF-beta signaling caused by Pkd1 haploinsufficiency.
Report immunolocalization of fibrillin-1/perlecan in HS-deficient hspg2 exon 3 null mutant mouse intervertebral disc.
the generation of a rabbit Marfanoid-progeroid-lipodystrophy model with C-terminal truncation of fibrillin-1 using a CRISPR/Cas9 system, is reported.
This gene encodes a member of the fibrillin family. The encoded protein is a large, extracellular matrix glycoprotein that serve as a structural component of 10-12 nm calcium-binding microfibrils. These microfibrils provide force bearing structural support in elastic and nonelastic connective tissue throughout the body. Mutations in this gene are associated with Marfan syndrome, isolated ectopia lentis, autosomal dominant Weill-Marchesani syndrome, MASS syndrome, and Shprintzen-Goldberg craniosynostosis syndrome.
, fibrillin 15
, fibrillin 1 (Marfan syndrome)
, tight skin