Atomic force microscopy and modeling of natural elastic fibrillin polymers.
A central issue in the understanding of Marfan syndrome deals with the functional architecture of fibrillin-containing microfibrils. Fibrillin-rich microfibrils are long extracellular matrix fibrillar components exhibiting a 50 nm periodic beaded-structure with a width of around 20-25 nm after rotary shadowing and a 10-12 nm diameter when observed in ultra-thin sections. They are composed of fibrillin monomers more or less associated with many other components which are, for the most part, poorly characterized up to date. They are known to be elastic but few data have been accumulated to understand their properties. Atomic force microscopy (AFM) allowed us to morphologically differentiate fibrillin-rich microfibrils from other fibrillar components and to investigate the thin structure of these beaded filaments in their native state. They showed, in AFM, a periodic beaded structure ranging from 50 to 60 nm and a width of about 40 nm. The different sizes of fibrillin-containing microfibrils previously observed after rotary shadowing and in ultra-thin sections was resolved with our technique and is revealed to be 10 nm in diameter. Each beaded microfibril appears to be composed of heterogeneous beads connected by 2-3 arms. An orientation of the microfibrils has been shown, and allows us to propose a complementary model of microfibrillar monomer association.
Hanssen
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E
Institut de Biologie et de Chimie des Protéines, CNRS-UPR 412, Lyon, France.
Franc
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Garrone
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D000818:Animals; D001704:Biopolymers; D002417:Cattle; D004548:Elasticity; D016326:Extracellular Matrix Proteins / Q000032:analysis*; D000071837:Fibrillins; D008382:Marfan Syndrome / Q000378:metabolism*; D008840:Microfilament Proteins / Q000032:analysis*; D018625:Microscopy, Atomic Force
D001704:Biopolymers; D016326:Extracellular Matrix Proteins; D000071837:Fibrillins; D008840:Microfilament Proteins