Results 11 to 20 of about 1,871 (159)
Fibrillin-1 Regulates Arteriole Integrity in the Retina
Biomolecules, 2022 Fibrillin-1 is an extracellular matrix protein that assembles into microfibrils that provide critical functions in large blood vessels and other tissues.
Florian Alonso +4 more
doaj +4 more sources
Fibrillin-1 and fibrillin-2 in human embryonic and early fetal development
Matrix Biology, 2002 The extracellular glycoproteins fibrillin-1 and fibrillin-2 are major components of connective tissue microfibrils. Mutations in the fibrillin-1 and fibrillin-2 genes are responsible for the phenotypical manifestations of Marfan syndrome and congenital contractural arachnodactyly respectively, which emphasizes their essential roles in developmental ...
Fabio Quondamatteo +2 more
exaly +5 more sources
Fibrillin-1 regulates endothelial sprouting during angiogenesis
Proceedings of the National Academy of Sciences of the United States of America, 2023 Fibrillin-1 is an extracellular matrix protein that assembles into microfibrils which provide critical functions in large blood vessels and other tissues. Mutations in the fibrillin-1 gene are associated with cardiovascular, ocular, and skeletal abnormalities in Marfan syndrome. Here, we reveal that fibrillin-1 is critical for angiogenesis
Florian Alonso +2 more
exaly +4 more sources
Fibrillin-1 Misfolding and Disease
Antioxidants & Redox Signaling, 2006 Fibrillin-1 is a 350 kDa calcium-binding protein which assembles to form 10-12 nm microfibrils in the extracellular matrix (ECM). The structure of fibrillin-1 is dominated by two types of disulfide-rich motifs, the calcium- binding epidermal growth factor-like (cbEGF) and transforming growth factor beta binding protein-like (TB) domains.
Whiteman, P, Hutchinson, S, Handford, P
openaire +4 more sources
Is There a Relationship Between Pelvic Organ Prolapse and Tissue Fibrillin-1 Levels? [PDF]
International Neurourology Journal, 2015 Purpose: Pelvic organ prolapse is a multifactorial disorder in which extracellular matrix defects are implicated. Fibrillin-1 level is reduced in stress urinary incontinence.
Ayla Eser +8 more
doaj +2 more sources
Homotypic Fibrillin-1 Interactions in Microfibril Assembly [PDF]
Journal of Biological Chemistry, 2005 We have defined the homotypic interactions of fibrillin-1 to obtain new insights into microfibril assembly. Dose-dependent saturable high affinity binding was demonstrated between N-terminal fragments, between furin processed C-terminal fragments, and between these N- and C-terminal fragments.
Marson, Andrew +8 more
openaire +4 more sources
Material and mechanical properties of bones deficient for fibrillin-1 or fibrillin-2 microfibrils [PDF]
Matrix Biology, 2011 The contribution of non-collagenous components of the extracellular matrix to bone strength is largely undefined. Here we report that deficiency of fibrillin-1 or fibrillin-2 microfibrils causes distinct changes in bone material and mechanical properties. Morphometric examination of mice with hypomorphic or null mutations in fibrillin-1 or fibrillin-2,
Emilio Arteaga-Solis +2 more
exaly +3 more sources
ADAMTSL-6 Is a Novel Extracellular Matrix Protein That Binds to Fibrillin-1 and Promotes Fibrillin-1 Fibril Formation [PDF]
Journal of Biological Chemistry, 2010 ADAMTS (A disintegrin and metalloproteinase with thrombospondin motifs)-like (ADAMTSL) proteins, a subgroup of the ADAMTS superfamily, share several domains with ADAMTS proteinases, including thrombospondin type I repeats, a cysteine-rich domain, and an ADAMTS spacer, but lack a catalytic domain.
Tsutsui, Ko +8 more
openaire +5 more sources
The distribution of fibrillin‐2 and LTBP‐2, and their co‐localisation with fibrillin‐1 in adult bovine tail disc [PDF]
Journal of Anatomy, 2011 AbstractWe investigated the distribution of fibrillin‐2 and LTBP‐2 (latent TGF‐β binding protein‐2) in the intervertebral disc of the adult bovine tail. The association of fibrillin‐2 and of LTBP‐2 with fibrillin‐1 was examined by dual immunofluorescence staining. Both fibrillin‐2 and LTBP‐2 were found extensively distributed in all regions of the disc
Li, B, Urban, J, Yu, J
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Fibulin-5 interacts with fibrillin-1 molecules and microfibrils [PDF]
Biochemical Journal, 2005 Fibulin-5 plays an important role in elastic fibre formation in vivo. We have investigated the molecular interactions between fibulin-5 and components of fibrillin-rich microfibrils which form a template for elastin. Fibulin-5 interacted in a dose-dependent manner with a fibrillin-1 N-terminal sequence and with tropoelastin, but not with MAGP-1 ...
Freeman, LJ +7 more
openaire +4 more sources