Abstract Search

ba0005op24 | Clinical (1) | ECTS2016

Secondary bone size deficit in patients with Ehlers–Danlos syndrome

Verroken Charlotte , Calders Patrick , Wandele Inge De , Malfait Fransiska , Zmierczak Hans , Goemaere Stefan , Kaufman Jean-Marc , Lapauw Bruno , Rombaut Lies

see P462....

0 shares

ba0005p462 | Other diseases of bone and mineral metabolism | ECTS2016

Secondary bone size deficit in patients with Ehlers–Danlos syndrome

Verroken Charlotte , Calders Patrick , Wandele Inge De , Malfait Fransiska , Zmierczak Hans , Goemaere Stefan , Kaufman Jean-Marc , Lapauw Bruno , Rombaut Lies

Background: EhlersDanlos syndrome (EDS) comprises a group of inherited connective tissue disorders, caused by various defects in the biosynthesis or secretion of fibrillar collagens. As collagen represents a major constituent of the bone matrix as well as of tendons and muscle, bone strength in EDS patients might be impaired both via direct and indirect pathways. Although decreased muscle strength, decreased areal bone mineral density (BMD) and increased fracture risk ha...

0 shares

ePoster Contact

ba0005op14 | Pre-Clinical | ECTS2016

Loss of type I collagen telopeptide lysyl hydroxylation causes musculoskeletal abnormalities in a zebrafish model of Bruck syndrome

Willaert Andy , Ghistelinck Charlotte , Witten P Eckhard , Huysseune Ann , Simoens Pascal , Symoens Sofie , Malfait Fransiska , De Muynck Amelie , De Paepe Anne , Kwon Ronald Y , Weiss Mary Ann , Eyre David E , Coucke Paul

see P483....

0 shares

ba0005p483 | Paediatric bone disease | ECTS2016

Loss of type I collagen telopeptide lysyl hydroxylation causes musculoskeletal abnormalities in a zebrafish model of Bruck syndrome

Willaert Andy , Ghistelinck Charlotte , Witten P Eckhard , Huysseune Ann , Simoens Pascal , Symoens Sofie , Malfait Fransiska , De Muynck Amelie , De Paepe Anne , Kwon Ronald Y , Weiss Mary Ann , Eyre David E , Coucke Paul

Bruck syndrome, a disorder caused by bi-allelic mutations in either PLOD2 or FKBP10, is characterized by flexion contractures and bone fractures and shows strong clinical overlap with the brittle bone disease Osteogenesis Imperfecta. PLOD2 encodes the Lysyl hydroxylase 2 (LH2) enzyme, which is responsible for the hydroxylation of lysine residues in the type-I collagen telopeptides. This hydroxylation directs cross-linking of the collagen fibrils in t...

0 shares

Bone Abstracts

Secondary bone size deficit in patients with Ehlers–Danlos syndrome

Secondary bone size deficit in patients with Ehlers–Danlos syndrome

Loss of type I collagen telopeptide lysyl hydroxylation causes musculoskeletal abnormalities in a zebrafish model of Bruck syndrome

Loss of type I collagen telopeptide lysyl hydroxylation causes musculoskeletal abnormalities in a zebrafish model of Bruck syndrome

BiosciAbstracts