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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.
The coordinate upregulation of fibrillin-1 and fibrillin-2 (show FBN2 ELISA Kits) expression with the onset of tropoelastin (show ELN ELISA Kits) production is consistent with a role in elastic fiber assembly.
a calcium-binding epidermal growth factor (show EGF ELISA Kits)-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 (show TGFB1 ELISA Kits) binding proteins affecting TGFbeta (show TGFB1 ELISA Kits) bioavailability in the ovary.
Mutation in FBN1 is associated with Marfan syndrome.
A novel heterozygous missense mutation c.2243 T>G (p.C781W) in exon 19 of FBN1 was identified in 5 family members with autosomal dominant Marfan syndrome.
Data suggest that FBN1 sequencing should be considered in individuals with familial thoracic aortic aneurysms and dissections (FTAAD) even without significant systemic features of Marfan syndrome (MFS).
This report broadens the phenotypic spectrum of growth disorders associated with FBN1 mutations. Identical mutations give rise to a wide phenotypic spectrum, ranging from isolated short stature to a more classic picture of GD2 with cardiac involvement, distinct facial dysmorphisms and various skeletal anomalies.
A subgroup of patients with Marfan syndrome (MFS) who have mutations in exons 24-32 of the FBN1 gene manifests severe atrioventricular valve insufficiency and skeletal problems as early as the neonatal period. These patients usually die in the first 2 years of life, thus a region between exons 24 and 32 of FBN1 is recognized as a critical region for this neonatal form of MFS (nMFS). [review, case reports]
FBN1 gene mutation is associated with Marfan syndrome.
Results showed two novel mutations in exon 12 and 50 of FBN1 identified in two Chinese family members with Marfan syndrome (MFS) which may be responsible for cardiovascular manifestations.
The results expand the FBN1 mutation spectrum and enrich our knowledge of genotype-phenotype correlations. Genetic testing for MFS and its related aortic diseases is increasingly important for early intervention and treatment.
miR (show MLXIP ELISA Kits)-486-5p induces papillary thyroid carcinoma cell growth inhibition and apoptosis by targeting and suppressing FBN1.
information of genotype-phenotype correlation owing to FBN1 mutations; the same FBN1 mutation, c. 1633C>T (Arg545Cys), was detected simultaneously in three different cardinal (show CARD8 ELISA Kits) phenotypes (ectopia lentis, aortic dissection and unaffected) within one family.
Resveratrol inhibits aortic root dilatation in Fbn1C1039G/+ Marfan mice by promoting elastin (show ELN ELISA Kits) 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 (show FBN2 ELISA Kits) expression is required to form thick oxytalan fibers in periodontal ligament.
findings show that fibrillin-1 regulates MSC (show MSC ELISA Kits) activity by modulating TGFbeta (show TGFB1 ELISA Kits) 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 (show P4HB ELISA Kits)-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 (show ALMS1 ELISA Kits)/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 (show IL4R ELISA Kits)/mTOR (show FRAP1 ELISA Kits) protein signaling.
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