The Molecular Basis for TGFBIp-Related Corneal Dystrophies

Marcel Renè Stenvang, Maria Andreasen, Daniel Otzen

Publikation: Bidrag til bog/antologi/rapport/proceedingBidrag til bog/antologiForskning


Several forms of the familial protein aggregation disease corneal dystrophy (CD) have been linked to mutations in transforming growth factor β-induced protein (TGFBIp). More than 30 point mutations in TGFBIp lead to CD, but the mutations induce many different aggregates in the cornea, ranging from granular to lattice and rod-like deposits. Biophysical methods have begun to help us elucidate how and why these mutations lead to polymorphic aggregates. Most CD-inducing mutations are found in the fourth fasciclin-1 domain of TGFBIp, and this domain also controls the stability of the entire TGFBIp molecule. Some mutations decrease TGFBIp stability, others increase it, and there is as yet no simple link between phenotype and stability. The mutations also affect surface electrostatics, proteolytic cleavage susceptibility, oligomerization propensities and interactions with other macromolecules. We highlight ways in which these changes can affect corneal aggregation. Future investigations will hopefully provide us with a clearer view of the links between biophysical properties and clinical manifestations
TitelBio-nanoimaging : Protein Misfolding and Aggregation
Antal sider10
ISBN (Elektronisk)978-0-12-394431-3
StatusUdgivet - 2014


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