Fibulin-5 interacts with fibrillin-1 molecules and microfibrils
Lyle J. Freeman, Amanda Lomas, Nigel W. Hodson, Michael J. Sherratt, Kieran T. Mellody, Anthony S. Weiss, Adrian Shuttleworth, Cay M. Kielty
Abstract
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Lyle J. Freeman, Amanda Lomas, Nigel W. Hodson, Michael J. Sherratt, Kieran T. Mellody, Anthony S. Weiss, Adrian Shuttleworth, Cay M. Kielty
Abstract
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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 (microfibril-associated glycoprotein-1) or decorin. Fibulin-5 did not inhibit interactions between fibrillin-1 N- and C-terminal fragments, or fibrillin-1 interactions with tropoelastin. Fibulin-5 may provide a link between tropoelastin and microfibrils in the pericellular space during elastic fibre assembly.
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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 (microfibril-associated glycoprotein-1) or decorin. Fibulin-5 did not inhibit interactions between fibrillin-1 N- and C-terminal fragments, or fibrillin-1 interactions with tropoelastin. Fibulin-5 may provide a link between tropoelastin and microfibrils in the pericellular space during elastic fibre assembly.
Key concepts: Tropoelastin, Fibulin, Fibrillin, Elastin, Microfibril, Elastic fiber, Decorin, Glycoprotein