Journal
BIOCHEMICAL JOURNAL
Volume 456, Issue -, Pages 283-295Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BJ20130699
Keywords
assembly; fibrillin; fibronectin; homoeostasis; microfibril
Categories
Funding
- Canadian Institutes of Health Research [M0P-106494]
- Natural Sciences and Engineering Research Council of Canada [RGPIN 375738-09]
- Canada Foundation for Innovation
- National Institutes of Health [HL021644]
- Network for Oral and Bone Health Research (Ph.D. student scholarship)
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Fibrillins constitute the backbone of extracellular multifunctional assemblies present in elastic and non-elastic matrices, termed microfibrils. Assembly of fibrillins into microfibrils and their homoeostasis is poorly understood and is often compromised in connective tissue disorders such as Marfan syndrome and other fibrillinopathies. Using interaction mapping studies, we demonstrate that fibrillins require the complete gelatin-binding region of fibronectin for interaction, which comprises domains FNI6-FNI9. However, the interaction of fibrillin-1 with the gelatin-binding domain of fibronectin is not involved in fibrillin-1 network assembly mediated by human skin fibroblasts. We show further that the fibronectin network is essential for microfibril homoeostasis in early stages. Fibronectin is present in extracted mature microfibrils from tissue and cells as well as in some in situ microfibrils observed at the ultrastructural level, indicating an extended mechanism for the involvement of fibronectin in microfibril assembly and maturation.
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