• Publications
  • Influence
Marfan syndrome caused by a recurrent de novo missense mutation in the fibrillin gene
TLDR
Fibrillin is implicate as the protein defective in patients with the Marfan syndrome and a de novo missense mutation in the fibrillin gene is described in two patients with sporadic disease. Expand
Dysregulation of TGF-beta activation contributes to pathogenesis in Marfan syndrome.
TLDR
It is shown that mice deficient in fibrillin-1 have marked dysregulation of transforming growth factor-beta (TGF-beta) activation and signaling, resulting in apoptosis in the developing lung, and that perturbation of this function can contribute to the pathogenesis of disease. Expand
Latent Transforming Growth Factor β-binding Protein 1 Interacts with Fibrillin and Is a Microfibril-associated Protein*
TLDR
Immunolocalization data were consistent with the hypothesis that LTBP-1 is a fibrillin-associated protein present in certain tissues but not in others, and a model depicting the relationship between LT BP-1 and fibrillins microfibrils is proposed. Expand
Dysregulation of TGF-β activation contributes to pathogenesis in Marfan syndrome
TLDR
It is shown that mice deficient in fibrillin-1 have marked dysregulation of transforming growth factor-β (TGF-β) activation and signaling, resulting in apoptosis in the developing lung, and that perturbation of this function can contribute to the pathogenesis of disease. Expand
Evidence for a critical contribution of haploinsufficiency in the complex pathogenesis of Marfan syndrome.
TLDR
Using homologous recombination to generate mice heterozygous for a comparable missense mutation revealed impaired microfibrillar deposition, skeletal deformity, and progressive deterioration of aortic wall architecture, comparable to characteristics of the human condition, consistent with a model that invokes haploinsufficiency for WT fibrillin-1, rather than production of mutant protein, as the primary determinant of failed microfibillar assembly. Expand
Fibrillin, a new 350-kD glycoprotein, is a component of extracellular microfibrils
TLDR
Investigation of the connective tissue matrices of skin, lung, kidney, vasculature, cartilage, tendon, muscle, cornea, and ciliary zonule demonstrated its widespread distribution, and immunolocalization suggested that fibrillin is arrayed periodically along the individual microfibril and that individualmicrofibrils may be aligned within bundles. Expand
Prolyl 3-Hydroxylase 1, Enzyme Characterization and Identification of a Novel Family of Enzymes*
TLDR
Prolyl 3-hydroxylase activity of the purified enzyme P3H1 is demonstrated on a full-length procollagen substrate and shown to specifically interact with denatured collagen and to exist in a tight complex with other endoplasmic reticulum-resident proteins. Expand
Pathogenetic sequence for aneurysm revealed in mice underexpressing fibrillin-1.
TLDR
Another gene-targeting mutation, mgR, is described, which shows that underexpression of fibrillin-1 similarly leads to MFS-like manifestations, and Histopathological analysis of mgR/mgR specimens implicates medial calcification, the inflammatory-fibroproliferative response, and inflammation-mediated elastolysis in the natural history of dissecting aneurysm. Expand
Targeting of Bone Morphogenetic Protein Growth Factor Complexes to Fibrillin*
TLDR
Data implicate the fibrillin microfibril network in the extracellular control of BMP signaling and demonstrate differences in how prodomains target their growth factors to theextracellular space. Expand
Fibrillins 1 and 2 Perform Partially Overlapping Functions during Aortic Development*
TLDR
The results demonstrated that fibrillins 1 and 2 perform partially overlapping functions during aortic development and that continued fibrillin-1 deposition is absolutely required for the maturation and function of the vessel during neonatal life. Expand
...
1
2
3
4
5
...