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Homotypic Fibrillin-1 Interactions in Microfibril Assembly

2004; Elsevier BV; Volume: 280; Issue: 6 Linguagem: Inglês

10.1074/jbc.m409029200

1083-351X

Andrew Marson, Matthew J. Rock, Stuart A. Cain, Lyle J. Freeman, Amanda Morgan, Kieran T. Mellody, C. Adrian Shuttleworth, Clair Baldock, Cay M. Kielty,

Cell Adhesion Molecules Research

We have defined the homotypic interactions of fibrillin-1 to obtain new insights into microfibril assembly. Dose-dependent saturable high affinity binding was demonstrated between N-terminal fragments, between furin processed C-terminal fragments, and between these N- and C-terminal fragments. The N terminus also interacted with a downstream fragment. A post-furin cleavage site C-terminal sequence also interacted with the N terminus, with itself and with the furin-processed fragment. No other homotypic fibrillin-1 interactions were detected. Some terminal homotypic interactions were inhibited by other terminal sequences, and were strongly calcium-dependent. Treatment of an N-terminal fragment with N-ethylmaleimide reduced homotypic binding. Microfibril-associated glycoprotein-1 inhibited N- to C-terminal interactions but not homotypic N-terminal interactions. These fibrillin-1 interactions are likely to regulate pericellular fibrillin-1 microfibril assembly.